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. 2023 Jun 6;19(2):2215153. doi: 10.1080/21645515.2023.2215153

Progress in Guillain–Barré syndrome immunotherapy—A narrative review of new strategies in recent years

Jiajia Yao 1, Rumeng Zhou 1, Yue Liu 1, Zuneng Lu 1,✉
PMCID: PMC10246479  PMID: 37278272

ABSTRACT

Guillain – Barré syndrome (GBS) is an immune-mediated neuropathy, the pathology of which is not clear. Both cellular and humoral immunity are involved in the occurrence of the disease, and molecular mimicry is currently the most widely recognized pathogenesis. Intravenous immunoglobulin (IVIg) and plasma exchange (PE) have been proven to be effective in improving the prognosis of patients with GBS, but there has been no progress in the treatment of the disease or strategies to improve the prognosis. New treatment strategies for GBS are mostly immunotherapies, including treatment against antibodies, complement pathways, immune cells and cytokines. Some of the new strategies are being investigated in clinical trials, but none of them have been approved for the treatment of GBS. Here, we summarized the current therapies for GBS, and new immunotherapies for GBS according to pathogenesis.

KEYWORDS: Guillain–Barré syndrome, treatment, complement pathway, immunotherapy

Introduction

Guillain–Barré syndrome (GBS) is an immune-mediated neuropathy that is the most common cause of acute flaccid paralysis and affects approximately 100,000 people per year worldwide. Antecedent events are often found 4 weeks before clinical syndromes appear in GBS patients, such as surgery or infection and Campylobacter jejuni, Haemophilus influenzae, cytomegalovirus, Zika virus and Japanese encephalitis virus are widely discussed.1–7

Depending on the different sites of the immune response, GBS is generally divided into demyelinating and axonal subtypes. Acute inflammatory demyelinating polyradiculoneuropathy (AIDP) is characterized by the demyelination of peripheral nerves and infiltration of inflammatory cells, with subsequent axonal damage. Antibodies can be detected on Schwann cells, and AIDP is the most common subtype in Western countries.8,9 Antigenic epitopes of bacteria and viruses are presented to T cells by activated macrophages, causing the cross reactivity of T cells. Activated T cells promote the release of cytokines and free radicals, disrupt the blood nerve barrier and damage myelin, ultimately leading to acute demyelination syndrome.10 Experimental autoimmune neuritis (EAN) is an animal model of AIDP that uses myelin epitopes P0 or P2 as major antigens to induce T-cell-mediated neuritis.1,11

Acute motor axonal neuropathy (AMAN) is the second most common subtype of GBS. AMAN presents as primary axonal injury with antibody and membrane attack complex (MAC) deposition in nodes of Ranvier without obvious inflammatory cell infiltration or demyelination.1,12–14 Antibodies related to AMAN include anti-GM1 and anti-GD1a antibodies.14–17 In AMAN patients related to Campylobacter jejuni, the gangliosides of the peripheral nerves are similar in structure to the lipo-oligosaccharides of Campylobacter jejuni. This suggests that the pathogenic mechanism of AMAN may be the cross-reaction of homologous epitopes between bacterial lipo-oligosaccharides and peripheral motor axon gangliosides.18–21

Miller-Fisher syndrome (MFS) is a variation of GBS, and the clinical features of MFS are facial muscle weakness and ataxia. Most MFS patients have anti-GQ1b antibodies, implying a potential role for ganglioside antibodies in disease pathogenesis or as reliable diagnostic biomarkers.22–24 Anti-GQ1b antibodies have been proven to activate complement at the neuromuscular junction in vitro, and complement activation is thought to be the primary pathogenic mechanism of MFS.25

Inflammatory cells and inflammatory factors play an important role in the pathogenesis of GBS. Macrophages play a dual role in the pathogenesis of GBS. Proinflammatory macrophages (M1) and anti-inflammatory macrophages (M2) play a decisive role in the initiation and development of GBS and EAN. M1 macrophages can promote the destruction of the blood-nerve barrier, induce the production of cytokines and chemokines, promote Th1 polarization, and eventually lead to demyelination of peripheral nerves. M2 macrophages play a protective role in the course of disease; they can promote T-cell apoptosis, remove myelin and axon fragments, inhibit inflammation, and promote the regeneration of axons and myelin.26,27

T-cell subtypes are also involved in the pathogenesis of GBS. The imbalance between Th1 and Th2 responses contributes to the pathogenesis of GBS.28–30 Th1 responses are thought to provoke disease by activating and recruiting macrophages to sites in peripheral nerves, subsequently leading to nerve damage induced by the direct action of macrophages or by toxic and inflammatory substances released in situ. On the other hand, the Th2 response acts as a suppressor and regulator of the Th1 pathway and therefore may have the resolving effect observed in the recovery phase of GBS and EAN.31–33 Recently, IL-17 and Th17 cells have been found to play an important role in many immune diseases, and Treg cells have a suppressive effect on inflammation.34 In the acute phase of the clinical course of GBS, the number and ratio of CD4+CD25+ T cells decrease, but this decrease is reversible.35 Another study found that regulatory T cells (Tregs) from GBS patients and Tregs from healthy controls showed equal expression of FoxP-3 mRNA, and their ability to suppress the proliferation and cytokine secretion of CD4+ effector T cells was unimpaired in GBS patients.36 Furthermore, adoptive infusion of autologous CD4+CD25+ Treg cells can reduce inflammatory cell infiltration of the sciatic nerve in EAN rats.37

Cytokines are small active proteins secreted by immune cells and some nonimmune cells that have several functions, such as regulating cell growth and differentiation, modulating the immune response, and participating in the inflammatory response. Proinflammatory cytokines such as interleukin (IL)-1β, IL-6, IL-12, tumor necrosis factor (TNF)-α, interferon (IFN)-γ, etc., damage myelin by recruiting effector cells to peripheral nerves and promoting the in situ release of toxic substances. Anti-inflammatory cytokines, such as IL-4 and IL-10, inhibit disease progression or promote myelin repair by exerting anti-inflammatory effects.38

Along with more studies on the pathogenesis of GBS, new strategies targeting at different points in the treatment of the disease have emerged. In this narrative review, we summarize the new approaches of classical therapies and new strategies in both animal models and clinical practice to identify potential therapies for GBS patients.

Materials and methods

Articles published between 2017 and 2022 were included in our research, and clinical trials, original articles, retrospective studies and systematic reviews in MEDLINE via PubMed interface and Cochrane Library were all carefully examined. Both animal experiments and human studies were included. Key words for searching included Guillain – Barré syndrome, treatment/therapy, experimental autoimmune neuritis, Miller-Fisher syndrome, etc. Clinical trials that were not completed were excluded. Titles and abstracts of papers were screened by reviewers to identify whether they met the criteria of the review. All references were examined for background information and potentially relevant articles.

Results

Classical therapies for GBS

Intravenous immunoglobulin (IVIg) and plasma exchange (PE) have been proven to be effective in improving the prognosis of patients with GBS and should be applied before the occurrence of irreversible axonal injury as soon as possible.1 These two therapies have equal effects.1,39 Patients undergo five sessions of PE with 50 ml/kg plasma each session, administered over 1–2 weeks. The typical dose for IVIg is 0.4 g/kg body weight per day for five consecutive days.39–41 The mechanism by which IVIg and PE are effective for GBS is still unclear but mostly involves removing the antibodies and MAC in plasma and regulating immune cells.

A single course of IVIg is effective for GBS patients, but some patients still have poor outcomes. A possible cause for this may be the rapid consumption of immunoglobulin, and a second course of IVIg may benefit these patients. A retrospective study in 2020 and a prospective study in 2021 both showed that patients with poor outcomes after the first course of IVIg could not benefit from the repeated use of IVIg, and research suggested that other immunomodulatory treatments should be used for GBS patients with poor prognosis.42,43

Although IVIg and PE are the most effective therapies for GBS, it has been proven that neither IVIg nor PE can prevent the disease course or nerve damage.6 PE requires specific equipment, and hypocalcemia, thrombosis, pneumothorax, complications from central venous access and allergic reactions are the main complications. Moreover, PE should be avoided in patients with severe autonomic dysfunction.44 IVIg is more likely to be completed than PE but is much more expensive, and liver dysfunction and thromboembolic events are rare but severe adverse events of IVIg.1 More research on classical treatments is needed for patients with mild disease and patients whose treatment starts more than 2 weeks after disease onset, and new strategies are also needed for patients with poor outcomes after treatment with PE or IVIg.

Neither oral nor intravenous use of glucocorticoids in GBS can accelerate recovery, nor can they affect the long-term outcome of patients.45 The combination of glucocorticoids and IVIg does not have a better effect than IVIg alone,46,47 but in the early phase of the disease, the combination of glucocorticoids and IVIg has a better effect in GBS patients.47

New strategies in GBS treatment

Therapies for antibodies

Neonatal Fc receptor (FcRn) can adjust the concentration of endogenous IgG. Inhibiting FcRn can reduce the level of IgG in the body, and it has been proven effective in animal experiments. Anti-ganglioside antibody levels in mice lacking FcRn are significantly reduced. The use of FcRn inhibitors significantly reduces the antibody levels in mice, reducing nerve damage and clinical symptoms. This suggests that FcRn inhibitors can be used to treat GBS in the future.48

Immunoglobulin G-degrading enzyme of Streptococcus pyogenes (IdeS) is secreted by Streptococcus pyogenes and can cleave IgG antibodies into F(ab’)2 and Fc fragments, thereby inhibiting the killing of S. pyogenes by the immune response of hosts.49 Ryo Takahashi found that IdeS efficiently cleaved IgG and blocked complement activation in vitro.50 A further study showed that IdeS could reduce complement deposition in the spinal nerve heel and significantly facilitate the clinical recovery process in the rabbit model of AMAN, and axonal degeneration of the anterior spinal nerve root was significantly reduced in IdeS-treated rabbits.51

Therapies for the complement pathway

Anti-GQ1b antibodies bind and destroy neuromuscular junctions, causing muscle paralysis. This damage activates complement and ultimately leads to the deposition of membrane attack complex (MAC) C5b-9. Susan K. Halstead and colleagues conducted a study to block the role of C5b-9 in autoimmune peripheral neuropathy using eculizumab to treat MFS. Studies have shown that the application of eculizumab in MFS mice can effectively prevent respiratory failure and neurological symptoms.52 Furthermore, they conducted a randomized trial to investigate the effect of eculizumab in GBS patients. The clinical trial included 28 patients diagnosed with GBS on the basis of a functioning score greater than 2 points, and 8 subjects were finally recruited. Four weeks after recruitment, 2 out of 2 patients received placebo, and 2 out of 5 patients received eculizumab and had decreased functioning scores of more than one point. The results indicated the need for further studies on eculizumab.53 A prospective study was carried out on the application of eculizumab in GBS patients. The study included patients with a GBS disability score of 3–5. After 4 weeks of treatment, the proportion of patients in the eculizumab and placebo groups who were able to walk independently was 61% and 45%, respectively, but both groups had adverse events. However, because the outcome indicators did not meet expectations, the researchers suggested that further large-scale prospective studies were needed to prove the effect of eculizumab.54 The 2020 Cochrane Database of Systematic Reviews also pointed out that the current level of evidence for eculizumab in the treatment of GBS is low.46

Previous studies showed that C5 inhibition could mitigate nerve injuries, but Rhona McGonigal determined that the early stage of complement activation could also cause immune cell recruitment. C1q is the first complement cascade molecule in the classical pathway. Two animal models were used to evaluate the efficacy of the anti-C1q antibody (M1). Studies have shown that anti-C1q treatment reduces axonal injury, and improves respiratory function in mouse models.55 ANX005 is a humanized immunoglobulin G4 (IgG4) recombinant antibody against C1q that blocks the initiation of the classical complement cascade. Inhibition of C1q can be used in acute immune-mediated diseases such as GBS, and the pharmacokinetics and pharmacology are currently under study.56 ANX005 has not been used to treat in GBS patients or animal models, and it may be a promising treatment option.

Therapies inhibiting inflammatory cells and inflammatory factors

A study by Ranran Han et al. found that dimethyl fumarate (DMF) improved the demyelination and inflammatory cell infiltration of the sciatic nerve when used in the treatment of EAN rats. DMF reduces the level of M1 macrophages and increases the level of M2 macrophages in the spleen and sciatic nerve. In the sciatic nerve, DMF treatment increases the level of nuclear factor erythroid-derived 2-related factor 2 (Nrf2) and its target gene hemooxygenase-1 (HO-1), which can promote the transfer of macrophages to M2-type polarization. In addition, DMF also improves the inflammatory environment of the spleen of EAN rats, characterized by the downregulation of IFN-γ, TNF-α, IL-6 and IL-17 messenger RNA (mRNA) and upregulation of IL-4 and IL-10 mRNA levels.57 Another study showed that DMF regulated T-cell proliferation and differentiation through different regions and layers of the small intestine,58 indicating that DMF protects EAN rats from nerve damage through multiple mechanisms.

A preventive and therapeutic study of decitabine (DAC) in EAN suggests that DAC can increase the number of thymic Tregs and reduce the production of proinflammatory cytokines, thereby improving the clinical symptoms of EAN.59

Ru-Tao Liu’s research found that 2-deoxy-D glucose (2-DG) inhibits the initiation and development of EAN at the same time by inhibiting the glycolytic pathway, simultaneously inhibiting the differentiation of Th1 and Th17 cells and enhancing the development of Treg cells. The enhancement of the glycolysis pathway can promote the pathogenesis of EAN, and inhibiting glycolysis may be a new treatment for GBS.60

A study of fasudil for EAN found that Th1 cell and Th17 cell proportions were decreased in mice treated with fasudil, the proportion of Th2 cells was similar, and the proportion of Treg cells in splenocytes was increased. Fasudil has a good therapeutic effect on EAN by attenuating Th1/Th17 cells and promoting Treg activation and M2 macrophage polarization.61

Shi Peng et al. found that the level of Bifidobacterium in GBS patients was significantly lower than that in healthy controls (HCs), and the concentration of Bifidobacterium was negatively correlated with Th2 and Th17 subgroups. Treatment with Bifidobacterium significantly reduced the levels of Th2 and Th17 cells and increased the level of Treg cells in EAN rats. This finding suggested that Bifidobacterium could alleviate GBS by regulating Th17 and Treg cells.62 Further study showed that, the expression level of programmed death (PD)-1 increased in EAN rats treated with Bifidobacterium. The function of Bifidobacterium in regulating T cells was partly blocked by inhibiting the expression of PD-1, suggesting that Bifidobacterium alleviates GBS in a partial way through PD-1.63

The immunoproteasome plays a critical role in homeostasis and immunity, especially in processing antigens for presentation on major histocompatibility complex (MHC) class I molecules to CD8+ T lymphocytes.64–66 The subunit of the immunoproteasome, low-MW polypeptide (LMP) 7, has an important role in cytokine production. PR-957 is a highly selective inhibitor of LMP7, and previous studies found that PR-957 can regulate the differentiation of Th cells and reduce the amount of proinflammatory cytokines. PR-957 reduced the proportion of Th17 cells in the sciatic nerve and spleen in EAN rats, decreased the expression of IL-6 and IL-23, and downregulated STAT3 phosphorylation, thereby reducing the severity and duration of EAN.67

Chunrong Li et al. found that ginkgolide can decrease the score of EAN mice and delay the peak of disease. It can also downregulate the proportion of Th17 cells in the spleen of EAN mice and reduce the levels of IFN-γ and IL-12 in GBS patients, suggesting that ginkgolides have potential therapeutic effects in GBS patients and the EAN model.68

The class I phosphatidylinositol 3-kinase inhibitor 2-(2-difluoromethylbenzimidazol-1-yl)-4,6-dimorpholino-1,3,5-triazine (ZSTK474) was also proven to be effective in alleviating the inflammatory response of sciatic nerves. The author reported that ZSTK474 could reduce the number of Th1/Th17 cells and levels of proinflammatory cytokines through the PI3K/AKT/mTORC1 pathway, suggesting a possible anti-inflammatory therapy for GBS.69

Nanoparticles (NPs) can bind with monocytes and remove monocytes from the lesion site to the spleen.70 Ehsan Elahi et al. used drug-free poly-lactic coglycolic acid (PLGA)-based NPs to modulate the inflammatory cells of EAN rats and found that regardless of different treatment approaches, NPs showed good effects in modulating inflammatory cells in circulation system, helping to reduce disease severity.71

Kaixi Ren et al. found that ginsenoside Rd (GSRd) could also protect against nerve damage in EAN rats by modulating monocyte conversion and increasing resolution-phase macrophage infiltration, showing that GSRd may be useful for GBS patients.72

Furthermore, Hong Jiao et al. found that vasoactive intestinal peptide (VIP) can inhibit neural inflammation, reduce inflammatory cytokine levels and improve body functions in EAN rats.73

Björn Ambrosius et al. used fingolimod as an immunomodulator for the treatment of EAN rats. A study showed that low-dose fingolimod could reduce circulating peripheral blood T cells and infiltrating T cells and macrophages in the sciatic nerve, and fewer apoptotic Schwann cells were found in rats treated with fingolimod at disease nadir.74

Therapies targeting other mechanisms

Efrat Shavit-Stein found that thrombin and its protease-activated receptor 1 (PAR1) participate in the development of EAN. N-Tosyl-Lys-chloromethylketone (TLCK) and N-alpha 2 naphthalenesulfonylglycyl 4 amidino-phenylalaninepiperidide (NAPAP) were used as PAR1 inhibitors to block the thrombin-PAR1 pathway. In vitro studies showed that both TLCK and NAPAP could inhibit the thrombin-PAR1 pathway in rat sciatic nerve damage. In vivo studies showed that TLCK- or NAPAP-treated rats had improved clinical scores, and TLCK treatment could prevent structural damage to the node of Ranvier in the sciatic nerve.75

Neurotrophic factors are essential for the development and damage repair of the peripheral nervous system. The p75 neurotrophic receptor (p75NTR) is fundamental to peripheral nerve growth.76 Brain-derived neurotrophic factor (BDNF) promotes peripheral nerve myelination via the p75NTR pathway. David G. Gonsalvez used the cyclic pentapeptide cyclo-[DPro-Ala-Lys-Lys-Arg] (cyclo-DPAKKR), a structural mimetic of BDNF to investigate the therapeutic effect in EAN rats. The study found that cyclo-DPAKKR administration limited the extent of inflammatory demyelination and axonal damage by inhibiting the p75NTR pathway, and the therapeutic effect of cyclo-DPAKKR was abrogated.77

Kota Moriguchi found that 4-aminopyridine (4-AP) could reduce the clinical scores of EAN rats and improve the electrophysiological properties, but the histological assessment revealed no significant difference between the 4-AP and control groups.78 The mechanism of 4-AP in the treatment of EAN is not clear, and further studies are needed to investigate the therapeutic effect of 4-AP.

Discussion

In 1916, Guillain, Barré and Strohl reported two cases of acute flaccid paralysis with high cerebrospinal fluid (CSF) protein levels and normal cell counts, which is now known as GBS. In the past century, we have made great progress in understanding the clinical variations, pathology and treatment of GBS.79,80

Until the 1970s, there was no specific and effective treatment for GBS. In the late 1970s, PE was first used to treat GBS.81 In 1984, two clinical trials showed that PE was efficient in GBS patients.82,83 A year later, one larger study confirmed the results and found that PE could benefit patients who were unable to walk independently, especially when treatment was started within 2 weeks of disease onset.84 PE was the first treatment proven to be effective for GBS, but the treatment also carries risk for patients with autonomic dysfunctions, which are common in GBS patients.

Ten years after the first report of PE, immunoglobulin was first reported in the treatment of GBS.85 A randomized clinical trial (RCT) in 1992 compared the efficiency of PE and IVIg and found that IVIg was an effective alternative to PE; patients treated with IVIg showed more improvement after 4 weeks than those with PE.86 Currently, clinical trials have shown that PE and IVIg have equal effects.1,39 IVIg has become the most popular therapy in most countries, unless the costs limit its use.

The treatment of GBS is still challenging for neurologists. Traditional therapies such as PE and IVIg are effective, but the high price of immunoglobulin and lack of specific equipment and PE specialists limit their use. New immunotherapies start by clearing antibodies, reducing membrane attack complexes and regulating the immune response, and targeting other pathways are also considered to be effective in EAN models or clinical trials. New therapies are aimed at the pathology of GBS, which means they are more specific. Most of the new therapies are drugs that are easy to produce, transport and store, and the use of new therapies does not require specific equipment. The combination of new therapies with classical therapies could help to improve the prognosis in patients with poor outcomes after treatment with classical therapies alone. Immunotherapies are still the most popular methods for GBS treatment. Further clinical and basic studies are needed to prove the role of these methods in the treatment of GBS and provide more possibilities for treatment.

New therapies also have limitations. Most therapies have only been verified in animal models, and only eculizumab and IdeS are undergoing clinical trials. The Cochrane library also reviewed the therapeutic effect of methods that have been used in RCTs and found that IFNβ-1a, CSF filtration and the Chinese herb tripterygium polyglycoside all had a very low level of certainty based on the evidence.46 Further studies should focus on the translation of basic research to clinical trials. Nonetheless, it will take a long time for new strategies to be applied in clinical practice.

In conclusion, IVIg and PE are still the most effective therapies for GBS. Additionally, immunotherapies are still the most popular methods for GBS treatment (Table 1). Further clinical and basic studies are needed to prove the role of these methods in the treatment of GBS and provide more possibilities for treatment.

Table 1.

New therapies used for treatment of GBS in recent years.

Species Therapy Type Pathway or approach Year/author
Rat PR-957 Original article T cell and cytokine regulation 2017/Liu H 67
Rabbit IdeS Original article Cleaved antibodies 2017/Wang Y 51
Rat Fingolimod Original article Inflammatory cells (macrophages and T cells) 2017/Ambrosius B 74
Rat cyclo-DPAKKR Original article p75NTR pathway 2017/Gonsalvez DG 77
Rat 4-AP Original article Not clear 2017/Moriguchi K 78
Human Eculizumab Clinical trial Complement pathway 2018/Misawa S 54
Rat Decitabine (DAC) Original article Treg cell induction 2018/Fagone P 59
Rat 2-deoxy-D glucose (2-DG) Original article glycolytic pathway 2018/Liu RT 60
Rat Bifidobacterium Original article T cell regulation 2018/Shi P 62
Rat ZSTK474 Original article T cell and cytokine regulation 2018/Chen X 69
Rat Vasoactive intestinal peptide (VIP) Original article Inflammatory cells regulation 2018/Jiao H 73
Rat Dimethyl fumarate(DMF) Original article Inflammatory cells (macrophages and T cells) 2019/Pitarokoili K 58
Rat TLCK Original article Thrombin-PAR1 pathway 2019/Shavit-Stein E 75
Human Second course of IVIg Retrospective study Immune regulation 2020/Verboon C 42
Mouse Fasudil Original article Inflammatory cells (macrophages and T cells) 2020/Zhao Y 61
Human Second course of IVIg Clinical trial Immune regulation 2021/Walgaard C 43
Mouse Ginkgolide Original article T cell and cytokine regulation 2021/Li C 68
Rat Ginsenoside Rd Original article Monocyte modulation 2021/Ren K 72
Rat Nanoparticles (NPs) Original article Inflammatory cells regulation 2022/Elahi E 71
Rat Bifidobacterium Original article PD-1 signaling 2023/Shi P 63
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Funding Statement

The author(s) reported there is no funding associated with the work featured in this article.

Author contributions

JY and ZN provided the idea for the study, RZ, YL, JY collected the clinical data, JY analyzed the data and wrote the manuscript. All authors read and approved the final version of the manuscript and agreed with its submission for publication.

Disclosure statement

No potential conflict of interest was reported by the author(s).

References

  • 1.Shahrizaila N, Lehmann HC, Kuwabara S.. Guillain-Barré syndrome. Lancet. 2021;397(10280):1214–8. doi: 10.1016/S0140-6736(21)00517-1. [DOI] [PubMed] [Google Scholar]
  • 2.Jacobs BC, Rothbarth PH, van der Meché FG, Herbrink P, Schmitz PIM, de Klerk MA, van Doorn PA. The spectrum of antecedent infections in Guillain-Barré syndrome: a case-control study. Neurology. 1998;51(4):1110–15. doi: 10.1212/WNL.51.4.1110. [DOI] [PubMed] [Google Scholar]
  • 3.Cao-Lormeau VM, Blake A, Mons S, Lastère S, Roche C, Vanhomwegen J, Dub T, Baudouin L, Teissier A, Larre P, et al. Guillain-Barré syndrome outbreak associated with Zika virus infection in French Polynesia: a case-control study. Lancet. 2016;387(10027):1531–9. doi: 10.1016/S0140-6736(16)00562-6. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 4.Islam Z, Jacobs BC, van Belkum A, Mohammad QD, Islam MB, Herbrink P, Diorditsa S, Luby SP, Talukder KA, Endtz HP. Axonal variant of Guillain-Barre syndrome associated with Campylobacter infection in Bangladesh. Neurology. 2010;74(7):581–7. doi: 10.1212/WNL.0b013e3181cff735. [DOI] [PubMed] [Google Scholar]
  • 5.Hao Y, Wang W, Jacobs BC, Qiao B, Chen M, Liu D, Feng X, Wang Y. Antecedent infections in Guillain-Barré syndrome: a single-center, prospective study. Ann Clin Transl Neurol. 2019;6(12):2510–7. doi: 10.1002/acn3.50946. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 6.Leung J, Sejvar JJ, Soares J, Lanzieri TM. Guillain-Barré syndrome and antecedent cytomegalovirus infection, USA 2009-2015. Neurol Sci. 2020;41(4):885–91. doi: 10.1007/s10072-019-04156-z. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 7.Yamana M, Kuwahara M, Fukumoto Y, Yoshikawa K, Takada K, Kusunoki S. Guillain-Barré syndrome and related diseases after influenza virus infection. Neurol Neuroimmunol Neuroinflamm. 2019;6(4):e575. doi: 10.1212/NXI.0000000000000575. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 8.Asbury AK, Arnason BG, Adams RD. The inflammatory lesion in idiopathic polyneuritis. Its role in pathogenesis. Medicine (Baltimore). 1969;48(3):173–215. doi: 10.1097/00005792-196905000-00001. [DOI] [PubMed] [Google Scholar]
  • 9.Wanschitz J, Maier H, Lassmann H, Budka H, Berger T. Distinct time pattern of complement activation and cytotoxic T cell response in Guillain-Barré syndrome. Brain. 2003;126(Pt 9):2034–42. doi: 10.1093/brain/awg207. [DOI] [PubMed] [Google Scholar]
  • 10.Ebrahim Soltani Z, Rahmani F, Rezaei N. Autoimmunity and cytokines in Guillain-Barré syndrome revisited: review of pathomechanisms with an eye on therapeutic options. Eur Cytokine Netw. 2019;30(1):1–14. doi: 10.1684/ecn.2019.0424. [DOI] [PubMed] [Google Scholar]
  • 11.Zhang HL, Zheng XY, Zhu J. Th1/Th2/Th17/Treg cytokines in Guillain-Barré syndrome and experimental autoimmune neuritis. Cytokine Growth Factor Rev. 2013;24(5):443–53. doi: 10.1016/j.cytogfr.2013.05.005. [DOI] [PubMed] [Google Scholar]
  • 12.Griffin JW, Li CY, Macko C, Ho TW, Hsieh ST, Xue P, Wang FA, Cornblath DR, McKhann GM, Asbury AK. Early nodal changes in the acute motor axonal neuropathy pattern of the Guillain-Barré syndrome. J Neurocytol. 1996;25(1):33–51. doi: 10.1007/BF02284784. [DOI] [PubMed] [Google Scholar]
  • 13.Hafer-Macko C, Hsieh ST, Li CY, Sheikh K, Cornblath DR, Li CY, McKhann GM, Asbury AK, Griffin JW. Acute motor axonal neuropathy: an antibody-mediated attack on axolemma. Ann Neurol. 1996;40(4):635–44. doi: 10.1002/ana.410400414. [DOI] [PubMed] [Google Scholar]
  • 14.Kuwabara S, Yuki N. Axonal Guillain-Barré syndrome: concepts and controversies. Lancet Neurol. 2013;12(12):1180–8. doi: 10.1016/S1474-4422(13)70215-1. [DOI] [PubMed] [Google Scholar]
  • 15.Willison HJ, Jacobs BC, van Doorn PA. Guillain-Barré syndrome. Lancet. 2016;388(10045):717–27. doi: 10.1016/S0140-6736(16)00339-1. [DOI] [PubMed] [Google Scholar]
  • 16.Lopez PH, Zhang G, Bianchet MA, Schnaar RL, Sheikh KA. Structural requirements of anti-GD1a antibodies determine their target specificity. Brain. 2008;131(Pt 7):1926–39. doi: 10.1093/brain/awn074. [DOI] [PubMed] [Google Scholar]
  • 17.Willison HJ, Yuki N. Peripheral neuropathies and anti-glycolipid antibodies. Brain. 2002;125(Pt 12):2591–625. doi: 10.1093/brain/awf272. [DOI] [PubMed] [Google Scholar]
  • 18.Koga M, Takahashi M, Masuda M, Hirata K, Yuki N. Campylobacter gene polymorphism as a determinant of clinical features of Guillain-Barré syndrome. Neurology. 2005;65(9):1376–81. doi: 10.1212/01.wnl.0000176914.70893.14. [DOI] [PubMed] [Google Scholar]
  • 19.Godschalk PC, Kuijf ML, Li J, St. Michael F, Ang CW, Jacobs BC, Karwaski M-F, Brochu D, Moterassed A, Endtz HP, et al. Structural characterization of Campylobacter jejuni lipooligosaccharide outer cores associated with Guillain-Barre and Miller Fisher syndromes. Infect Immun. 2007;75(3):1245–54. doi: 10.1128/IAI.00872-06. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 20.Susuki K, Yuki N, Schafer DP, Hirata K, Zhang G, Funakoshi K, Rasband MN. Dysfunction of nodes of Ranvier: a mechanism for anti-ganglioside antibody-mediated neuropathies. Exp Neurol. 2012;233(1):534–42. doi: 10.1016/j.expneurol.2011.11.039. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 21.Willison HJ. The translation of the pathological findings described in humans to experimental models of acute motor axonal neuropathy. J Peripher Nerv Syst. 2012;17(Suppl 3):3–8. doi: 10.1111/j.1529-8027.2012.00423.x. [DOI] [PubMed] [Google Scholar]
  • 22.Mori M, Kuwabara S, Fukutake T, Yuki N, Hattori T. Clinical features and prognosis of Miller Fisher syndrome. Neurology. 2001;56(8):1104–6. doi: 10.1212/WNL.56.8.1104. [DOI] [PubMed] [Google Scholar]
  • 23.Chiba A, Kusunoki S, Shimizu T, Kanazawa I. Serum IgG antibody to ganglioside GQ1b is a possible marker of Miller Fisher syndrome. Ann Neurol. 1992;31(6):677–9. doi: 10.1002/ana.410310619. [DOI] [PubMed] [Google Scholar]
  • 24.Mori M, Kuwabara S. Fisher syndrome. Curr Treat Options Neurol. 2011;13(1):71–8. doi: 10.1007/s11940-010-0103-8. [DOI] [PubMed] [Google Scholar]
  • 25.Jacobs BC, O’Hanlon GM, Bullens RW, Veitch J, Plomp JJ, Willison HJ. Immunoglobulins inhibit pathophysiological effects of anti-GQ1b-positive sera at motor nerve terminals through inhibition of antibody binding. Brain. 2003;126(Pt 10):2220–34. doi: 10.1093/brain/awg235. [DOI] [PubMed] [Google Scholar]
  • 26.Shen D, Chu F, Lang Y, Geng Y, Zheng X, Zhu J, Liu K. Beneficial or harmful role of macrophages in Guillain-Barré syndrome and experimental autoimmune neuritis. Mediators Inflamm. 2018;2018:4286364. doi: 10.1155/2018/4286364. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 27.Koike H, Katsuno M. Macrophages and autoantibodies in demyelinating diseases. Cells. 2021;10(4):844. doi: 10.3390/cells10040844. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 28.Nyati KK, Prasad KN, Rizwan A, Verma A, Paliwal VK. TH1 and TH2 response to campylobacter jejuni antigen in Guillain-Barre syndrome. Arch Neurol. 2011;68(4):445–52. doi: 10.1001/archneurol.2011.51. [DOI] [PubMed] [Google Scholar]
  • 29.Zhu J, Bai XF, Mix E, Link H. Cytokine dichotomy in peripheral nervous system influences the outcome of experimental allergic neuritis: dynamics of mRNA expression for IL-1 beta, IL-6, IL-10, IL-12, TNF-alpha, TNF-beta, and cytolysin. Clin Immunol Immunopathol. 1997;84(1):85–94. doi: 10.1006/clin.1997.4356. [DOI] [PubMed] [Google Scholar]
  • 30.Yeghiazaryan NS, Zara F, Capovilla G, Brigati G, Falsaperla R, Striano P. Pyridoxine-dependent epilepsy: an under-recognised cause of intractable seizures. J Paediatr Child Health. 2012;48(3):E113–5. doi: 10.1111/j.1440-1754.2010.01866.x. [DOI] [PubMed] [Google Scholar]
  • 31.Créange A, Bélec L, Clair B, Degos JD, Raphaël JC, Gherardi RK. Circulating transforming growth factor beta 1 (TGF-beta1) in Guillain-Barré syndrome: decreased concentrations in the early course and increase with motor function. J Neurol Neurosurg Psychiatry. 1998;64(2):162–5. doi: 10.1136/jnnp.64.2.162. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 32.Dahle C, Ekerfelt C, Vrethem M, Samuelsson M, Ernerudh J. T helper type 2 like cytokine responses to peptides from P0 and P2 myelin proteins during the recovery phase of Guillain-Barré syndrome. J Neurol Sci. 1997;153(1):54–60. doi: 10.1016/S0022-510X(97)00178-0. [DOI] [PubMed] [Google Scholar]
  • 33.Deretzi G, Zou LP, Pelidou SH, Nennesmo I, Levi M, Wahren B, Mix E, Zhu J. Nasal administration of recombinant rat IL-4 ameliorates ongoing experimental autoimmune neuritis and inhibits demyelination. J Autoimmun. 1999;12(2):81–9. doi: 10.1006/jaut.1998.0259. [DOI] [PubMed] [Google Scholar]
  • 34.Wu X, Wang J, Liu K, Zhu J, Zhang HL. Are Th17 cells and their cytokines a therapeutic target in Guillain-Barré syndrome? Expert Opin Ther Targets. 2016;20(2):209–22. doi: 10.1517/14728222.2016.1086751. [DOI] [PubMed] [Google Scholar]
  • 35.Harness J, McCombe PA. Increased levels of activated T-cells and reduced levels of CD4/CD25+ cells in peripheral blood of Guillain-Barré syndrome patients compared to controls. J Clin Neurosci. 2008;15(9):1031–5. doi: 10.1016/j.jocn.2007.09.016. [DOI] [PubMed] [Google Scholar]
  • 36.Chi LJ, Wang HB, Zhang Y, Wang WZ. Abnormality of circulating CD4(+)CD25(+) regulatory T cell in patients with Guillain-Barré syndrome. J Neuroimmunol. 2007;192(1–2):206–14. doi: 10.1016/j.jneuroim.2007.09.034. [DOI] [PubMed] [Google Scholar]
  • 37.Wang FJ, Cui D, Qian WD. Therapeutic effect of CD4+CD25+ regulatory T cells amplified in vitro on experimental autoimmune neuritis in rats. Cell Physiol Biochem. 2018;47(1):390–402. doi: 10.1159/000489919. [DOI] [PubMed] [Google Scholar]
  • 38.Lu MO, Zhu J. The role of cytokines in Guillain-Barré syndrome. J Neurol. 2011;258(4):533–48. doi: 10.1007/s00415-010-5836-5. [DOI] [PubMed] [Google Scholar]
  • 39.Hughes RA, Swan AV, van Doorn PA. Intravenous immunoglobulin for Guillain-Barré syndrome. Cochrane Database Syst Rev. 2014;2014(9):Cd002063. doi: 10.1002/14651858.CD002063.pub6. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 40.Hughes RA, Swan AV, Raphaël JC, Annane D, van Koningsveld R, van Doorn PA. Immunotherapy for Guillain-Barré syndrome: a systematic review. Brain. 2007;130(Pt 9):2245–57. doi: 10.1093/brain/awm004. [DOI] [PubMed] [Google Scholar]
  • 41.Chevret S, Hughes RA, Annane D. Plasma exchange for Guillain-Barré syndrome. Cochrane Database Syst Rev. 2017;2(2):Cd001798. doi: 10.1002/14651858.CD001798.pub3. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 42.Verboon C, van den Berg B, Cornblath DR, Venema E, Gorson KC, Lunn MP, Lingsma H, Van den Bergh P, Harbo T, Bateman K, et al. Original research: second IVIg course in Guillain-Barré syndrome with poor prognosis: the non-randomised ISID study. J Neurol Neurosurg Psychiatry. 2020;91(2):113–21. doi: 10.1136/jnnp-2019-321496. [DOI] [PubMed] [Google Scholar]
  • 43.Walgaard C, Jacobs BC, Lingsma HF, Steyerberg EW, van den Berg B, Doets AY, Leonhard SE, Verboon C, Huizinga R, Drenthen J, et al. Second intravenous immunoglobulin dose in patients with Guillain-Barré syndrome with poor prognosis (SID-GBS): a double-blind, randomised, placebo-controlled trial. Lancet Neurol. 2021;20(4):275–83. doi: 10.1016/S1474-4422(20)30494-4. [DOI] [PubMed] [Google Scholar]
  • 44.Schröder A, Linker RA, Gold R. Plasmapheresis for neurological disorders. Expert Rev Neurother. 2009;9(9):1331–9. doi: 10.1586/ern.09.81. [DOI] [PubMed] [Google Scholar]
  • 45.Hughes RA, Brassington R, Gunn AA, van Doorn PA. Corticosteroids for Guillain-Barré syndrome. Cochrane Database Syst Rev. 2016;10(10):Cd001446. doi: 10.1002/14651858.CD001446.pub5. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 46.Doets AY, Hughes RA, Brassington R, Hadden RD, Pritchard J. Pharmacological treatment other than corticosteroids, intravenous immunoglobulin and plasma exchange for Guillain-Barré syndrome. Cochrane Database Syst Rev. 2020;1(1):Cd008630. doi: 10.1002/14651858.CD008630.pub5. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 47.van Koningsveld R, Schmitz PI, Meché FG, Visser LH, Meulstee J, van Doorn PA. Effect of methylprednisolone when added to standard treatment with intravenous immunoglobulin for Guillain-Barré syndrome: randomised trial. Lancet. 2004;363(9404):192–6. doi: 10.1016/S0140-6736(03)15324-X. [DOI] [PubMed] [Google Scholar]
  • 48.Zhang G, Lin J, Ghauri S, Sheikh KA. Modulation of IgG-FcRn interactions to overcome antibody-mediated inhibition of nerve regeneration. Acta Neuropathol. 2017;134(2):321–4. doi: 10.1007/s00401-017-1730-x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 49.von Pawel-Rammingen U, Johansson BP, Björck L. IdeS, a novel streptococcal cysteine proteinase with unique specificity for immunoglobulin G. Embo J. 2002;21(7):1607–15. doi: 10.1093/emboj/21.7.1607. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 50.Takahashi R, Yuki N. Streptococcal IdeS: therapeutic potential for Guillain-Barré syndrome. Sci Rep. 2015;5:10809. doi: 10.1038/srep10809. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 51.Wang Y, Shi Q, Lv H, Hu M, Wang W, Wang Q, Qiao B, Zhang G, Lv Z, Kjellman C, et al. IgG-degrading enzyme of Streptococcus pyogenes (IdeS) prevents disease progression and facilitates improvement in a rabbit model of Guillain-Barré syndrome. Exp Neurol. 2017;291:134–40. doi: 10.1016/j.expneurol.2017.02.010. [DOI] [PubMed] [Google Scholar]
  • 52.Halstead SK, Zitman FM, Humphreys PD, Greenshields K, Verschuuren JJ, Jacobs BC, Rother RP, Plomp JJ, Willison HJ. Eculizumab prevents anti-ganglioside antibody-mediated neuropathy in a murine model. Brain. 2008;131(5):1197–208. doi: 10.1093/brain/awm316. [DOI] [PubMed] [Google Scholar]
  • 53.Davidson AI, Halstead SK, Goodfellow JA, Chavada G, Mallik A, Overell J, Lunn MP, McConnachie A, van Doorn P, Willison HJ. Inhibition of complement in Guillain-Barré syndrome: the ICA-GBS study. J Peripher Nerv Syst. 2017;22(1):4–12. doi: 10.1111/jns.12194. [DOI] [PubMed] [Google Scholar]
  • 54.Misawa S, Kuwabara S, Sato Y, Yamaguchi N, Nagashima K, Katayama K, Sekiguchi Y, Iwai Y, Amino H, Suichi T, et al. Safety and efficacy of eculizumab in Guillain-Barré syndrome: a multicentre, double-blind, randomised phase 2 trial. Lancet Neurol. 2018;17(6):519–29. doi: 10.1016/S1474-4422(18)30114-5. [DOI] [PubMed] [Google Scholar]
  • 55.McGonigal R, Cunningham ME, Yao D, Barrie JA, Sankaranarayanan S, Fewou SN, Furukawa K, Yednock TA, Willison HJ. C1q-targeted inhibition of the classical complement pathway prevents injury in a novel mouse model of acute motor axonal neuropathy. Acta Neuropathol Commun. 2016;4:23. doi: 10.1186/s40478-016-0291-x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 56.Lansita JA, Mease KM, Qiu H, Yednock T, Sankaranarayanan S, Kramer S. Nonclinical development of ANX005: a humanized anti-C1q antibody for treatment of autoimmune and neurodegenerative diseases. Int J Toxicol. 2017;36(6):449–62. doi: 10.1177/1091581817740873. [DOI] [PubMed] [Google Scholar]
  • 57.Han R, Xiao J, Zhai H, Hao J. Dimethyl fumarate attenuates experimental autoimmune neuritis through the nuclear factor erythroid-derived 2-related factor 2/hemoxygenase-1 pathway by altering the balance of M1/M2 macrophages. J Neuroinflammation. 2016;13(1):97. doi: 10.1186/s12974-016-0559-x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 58.Pitarokoili K, Bachir H, Sgodzai M, Grüter T, Haupeltshofer S, Duscha A, Pedreiturria X, Motte J, Gold R. Induction of regulatory properties in the intestinal immune system by dimethyl fumarate in Lewis rat experimental autoimmune neuritis. Front Immunol. 2019;10:2132. doi: 10.3389/fimmu.2019.02132. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 59.Fagone P, Mazzon E, Chikovani T, Saraceno A, Mammana S, Colletti G, Mangano K, Bramanti P, Nicoletti F. Decitabine induces regulatory T cells, inhibits the production of IFN-gamma and IL-17 and exerts preventive and therapeutic efficacy in rodent experimental autoimmune neuritis. J Neuroimmunol. 2018;321:41–8. doi: 10.1016/j.jneuroim.2018.05.013. [DOI] [PubMed] [Google Scholar]
  • 60.Liu RT, Zhang M, Yang CL, Zhang P, Zhang N, Du T, Ge M-R, Yue L-T, Li X-L, Li H, et al. Enhanced glycolysis contributes to the pathogenesis of experimental autoimmune neuritis. J Neuroinflammation. 2018;15(1):51. doi: 10.1186/s12974-018-1095-7. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 61.Zhao Y, Liu B, Wang Y, Xiao B. Effect of fasudil on experimental autoimmune neuritis and its mechanisms of action. Braz J Med Biol Res. 2020;53(1):e8669. doi: 10.1590/1414-431x20198669. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 62.Shi P, Qu H, Nian D, Chen Y, Liu X, Li Q, Li Q, Wang C, Ye M, Ma B. Treatment of Guillain-Barré syndrome with Bifidobacterium infantis through regulation of T helper cells subsets. Int Immunopharmacol. 2018;61:290–6. doi: 10.1016/j.intimp.2018.06.015. [DOI] [PubMed] [Google Scholar]
  • 63.Shi P, Nian D, Qu H, Ye M, Wang C, Li L, Li Q. B.Infantis enhances immunotherapy for Guillain-Barre syndrome through regulating PD-1. BMC Neurol. 2023;23(1):48. doi: 10.1186/s12883-022-03046-w. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 64.Kimura H, Caturegli P, Takahashi M, Suzuki K. New insights into the function of the immunoproteasome in immune and nonimmune cells. J Immunol Res. 2015;2015:541984. doi: 10.1155/2015/541984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 65.Kloetzel PM, Ossendorp F. Proteasome and peptidase function in MHC-class-I-mediated antigen presentation. Curr Opin Immunol. 2004;16(1):76–81. doi: 10.1016/j.coi.2003.11.004. [DOI] [PubMed] [Google Scholar]
  • 66.Basler M, Youhnovski N, Van Den Broek M, Przybylski M, Groettrup M. Immunoproteasomes down-regulate presentation of a subdominant T cell epitope from lymphocytic choriomeningitis virus. J Immunol. 2004;173(6):3925–34. doi: 10.4049/jimmunol.173.6.3925. [DOI] [PubMed] [Google Scholar]
  • 67.Liu H, Wan C, Ding Y, Han R, He Y, Xiao J, Hao J. PR-957, a selective inhibitor of immunoproteasome subunit low-MW polypeptide 7, attenuates experimental autoimmune neuritis by suppressing T(h)17-cell differentiation and regulating cytokine productio. Faseb J. 2017;31(4):1756–66. doi: 10.1096/fj.201601147R. [DOI] [PubMed] [Google Scholar]
  • 68.Li C, Liu S, Aerqin Q, Shen D, Wu X, Liu K. The therapeutic effects of ginkgolides in Guillain-Barré syndrome and experimental autoimmune neuritis. J Clin Neurosci. 2021;87:44–9. doi: 10.1016/j.jocn.2021.02.016. [DOI] [PubMed] [Google Scholar]
  • 69.Chen X, Guo Y, Han R, Liu H, Ding Y, Shi Y, Kong D, Ma X. Class I PI3K inhibitor ZSTK474 attenuates experimental autoimmune neuritis by decreasing the frequency of Th1/Th17 cells and reducing the production of proinflammatory cytokines. Cell Immunol. 2018;329:41–9. doi: 10.1016/j.cellimm.2018.04.011. [DOI] [PubMed] [Google Scholar]
  • 70.Saito E, Kuo R, Pearson RM, Gohel N, Cheung B, King NJC, Miller SD, Shea LD. Designing drug-free biodegradable nanoparticles to modulate inflammatory monocytes and neutrophils for ameliorating inflammation. J Control Release. 2019;300:185–96. doi: 10.1016/j.jconrel.2019.02.025. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 71.Elahi E, Ali ME, Zimmermann J, Getts DR, Müller M, Lamprecht A. Immune modifying effect of drug free biodegradable nanoparticles on disease course of experimental autoimmune neuritis. Pharmaceutics. 2022;14(11):2410. doi: 10.3390/pharmaceutics14112410. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 72.Ren K, Li S, Ding J, Zhao S, Liang S, Cao X, Su C, Guo J. Ginsenoside Rd attenuates mouse experimental autoimmune neuritis by modulating monocyte subsets conversion. Biomed Pharmacother. 2021;138:111489. doi: 10.1016/j.biopha.2021.111489. [DOI] [PubMed] [Google Scholar]
  • 73.Jiao H, Ren H. The effects of vasoactive intestinal peptide in the rat model of experimental autoimmune neuritis and the implications for treatment of acute inflammatory demyelinating polyradiculoneuropathy or Guillain-Barré syndrome. Drug Des Devel Ther. 2018;12:3817–24. doi: 10.2147/DDDT.S175331. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 74.Ambrosius B, Pitarokoili K, Schrewe L, Pedreiturria X, Motte J, Gold R. Fingolimod attenuates experimental autoimmune neuritis and contributes to Schwann cell-mediated axonal protection. J Neuroinflammation. 2017;14(1):92. doi: 10.1186/s12974-017-0864-z. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 75.Shavit-Stein E, Aronovich R, Sylantiev C, Gera O, Gofrit SG, Chapman J, Dori A. Blocking thrombin significantly ameliorates experimental autoimmune neuritis. Front Neurol. 2018;9:1139. doi: 10.3389/fneur.2018.01139. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 76.Lee KF, Li E, Huber LJ, Landis SC, Sharpe AH, Chao MV, Jaenisch R. Targeted mutation of the gene encoding the low affinity NGF receptor p75 leads to deficits in the peripheral sensory nervous system. Cell. 1992;69(5):737–49. doi: 10.1016/0092-8674(92)90286-L. [DOI] [PubMed] [Google Scholar]
  • 77.Gonsalvez DG, Tran G, Fletcher JL, Hughes RA, Hodgkinson S, Wood RJ, Yoo SW, De Silva M, Agnes WW, McLean C, et al. A brain-derived neurotrophic factor-based p75(NTR) peptide mimetic ameliorates experimental autoimmune neuritis induced axonal pathology and demyelination. eNeuro. 2017;4(3):ENEURO.0142–17.2017. doi: 10.1523/ENEURO.0142-17.2017. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 78.Moriguchi K, Miyamoto K, Kusunoki S. 4-aminopyridine ameliorates experimental autoimmune neuritis in Lewis rats. J Neuroimmunol. 2017;305:72–4. doi: 10.1016/j.jneuroim.2017.01.023. [DOI] [PubMed] [Google Scholar]
  • 79.Goodfellow JA, Willison HJ. Guillain-Barré syndrome: a century of progress. Nat Rev Neurol. 2016;12(12):723–31. doi: 10.1038/nrneurol.2016.172. [DOI] [PubMed] [Google Scholar]
  • 80.Uncini A. Guillain-Barré syndrome: what have we learnt during one century? A personal historical perspective. Rev Neurol (Paris). 2016;172(10):632–44. doi: 10.1016/j.neurol.2016.08.006. [DOI] [PubMed] [Google Scholar]
  • 81.Brettle RP, Gross M, Legg NJ, Lockwood M, Pallis C. Treatment of acute polyneuropathy by plasma exchange. Lancet. 1978;2(8099):1100. doi: 10.1016/S0140-6736(78)91837-8. [DOI] [PubMed] [Google Scholar]
  • 82.Greenwood RJ, Newsom-Davis J, Hughes RA, Gordon NS, Millac P, Newsom-Davis J, Aslan S, Chadwick DW, Mclellan DL, Stott RB, et al. Controlled trial of plasma exchange in acute inflammatory polyradiculoneuropathy. Lancet. 1984;1(8382):877–9. doi: 10.1016/S0140-6736(84)91341-2. [DOI] [PubMed] [Google Scholar]
  • 83.Osterman PO, Fagius G, Pirskanen G, Fagius J, Pihlstedt P, Sidén Å, Säfwenberg J. Beneficial effects of plasma exchange in acute inflammatory polyradiculoneuropathy. Lancet. 1984;2(8415):1296–9. doi: 10.1016/S0140-6736(84)90819-5. [DOI] [PubMed] [Google Scholar]
  • 84.The Guillain-Barré syndrome Study Group . Plasmapheresis and acute Guillain-Barré syndrome. Neurology. 1985;35(8):1096–104. doi: 10.1212/WNL.35.8.1096. [DOI] [PubMed] [Google Scholar]
  • 85.Kleyweg RP, van der Meché FG, Meulstee J. Treatment of Guillain-Barré syndrome with high-dose gammaglobulin. Neurology. 1988;38(10):1639–41. doi: 10.1212/WNL.38.10.1639. [DOI] [PubMed] [Google Scholar]
  • 86.van der Meché FG, Schmitz PI. A randomized trial comparing intravenous immune globulin and plasma exchange in Guillain-Barré syndrome. Dutch Guillain-Barré study group. N Engl J Med. 1992;326(17):1123–9. doi: 10.1056/NEJM199204233261705. [DOI] [PubMed] [Google Scholar]

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