Skip to main content
PMC home page
Infection and Immunity logoLink to Infection and Immunity
. 1994 Feb;62(2):333–340. doi: 10.1128/iai.62.2.333-340.1994

Proteolytic activation of bacterial toxins: role of bacterial and host cell proteases.

V M Gordon 1, S H Leppla 1
PMCID: PMC186112  PMID: 8300195

Full text

PDF
333

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Ahnert-Hilger G., Dauzenroth M. E., Habermann E., Henschen A., Krieglstein K., Mauler F., Weller U. Chains and fragments of tetanus toxin, and their contribution to toxicity. J Physiol (Paris) 1990;84(3):229–236. [PubMed] [Google Scholar]
  2. Aktories K., Bärmann M., Ohishi I., Tsuyama S., Jakobs K. H., Habermann E. Botulinum C2 toxin ADP-ribosylates actin. Nature. 1986 Jul 24;322(6077):390–392. doi: 10.1038/322390a0. [DOI] [PubMed] [Google Scholar]
  3. Aktories K., Wegner A. Mechanisms of the cytopathic action of actin-ADP-ribosylating toxins. Mol Microbiol. 1992 Oct;6(20):2905–2908. doi: 10.1111/j.1365-2958.1992.tb01749.x. [DOI] [PubMed] [Google Scholar]
  4. Allured V. S., Collier R. J., Carroll S. F., McKay D. B. Structure of exotoxin A of Pseudomonas aeruginosa at 3.0-Angstrom resolution. Proc Natl Acad Sci U S A. 1986 Mar;83(5):1320–1324. doi: 10.1073/pnas.83.5.1320. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Arora N., Leppla S. H. Residues 1-254 of anthrax toxin lethal factor are sufficient to cause cellular uptake of fused polypeptides. J Biol Chem. 1993 Feb 15;268(5):3334–3341. [PubMed] [Google Scholar]
  6. Barr P. J. Mammalian subtilisins: the long-sought dibasic processing endoproteases. Cell. 1991 Jul 12;66(1):1–3. doi: 10.1016/0092-8674(91)90129-m. [DOI] [PubMed] [Google Scholar]
  7. Brennan S. O., Peach R. J. The processing of human proinsulin and chicken proalbumin by rat hepatic vesicles suggests a convertase specific for X-Y-Arg-Arg or Arg-X-Y-Arg sequences. J Biol Chem. 1991 Nov 15;266(32):21504–21508. [PubMed] [Google Scholar]
  8. Chaudhary V. K., Jinno Y., FitzGerald D., Pastan I. Pseudomonas exotoxin contains a specific sequence at the carboxyl terminus that is required for cytotoxicity. Proc Natl Acad Sci U S A. 1990 Jan;87(1):308–312. doi: 10.1073/pnas.87.1.308. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Chauhan S. S., Gottesman M. M. Construction of a new universal vector for insertional mutagenesis by homologous recombination. Gene. 1992 Oct 21;120(2):281–285. doi: 10.1016/0378-1119(92)90106-y. [DOI] [PubMed] [Google Scholar]
  10. Choe S., Bennett M. J., Fujii G., Curmi P. M., Kantardjieff K. A., Collier R. J., Eisenberg D. The crystal structure of diphtheria toxin. Nature. 1992 May 21;357(6375):216–222. doi: 10.1038/357216a0. [DOI] [PubMed] [Google Scholar]
  11. Cieplak W., Hasemann C., Eidels L. Specific cleavage of diphtheria toxin by human urokinase. Biochem Biophys Res Commun. 1988 Dec 15;157(2):747–754. doi: 10.1016/s0006-291x(88)80313-9. [DOI] [PubMed] [Google Scholar]
  12. Collier R. J., Kandel J. Structure and activity of diphtheria toxin. I. Thiol-dependent dissociation of a fraction of toxin into enzymically active and inactive fragments. J Biol Chem. 1971 Mar 10;246(5):1496–1503. [PubMed] [Google Scholar]
  13. DasGupta B. R. Activation of Clostridium botulinum type B toxin by an endogenous enzyme. J Bacteriol. 1971 Dec;108(3):1051–1057. doi: 10.1128/jb.108.3.1051-1057.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. DasGupta B. R., Dekleva M. L. Botulinum neurotoxin type A: sequence of amino acids at the N-terminus and around the nicking site. Biochimie. 1990 Sep;72(9):661–664. doi: 10.1016/0300-9084(90)90048-l. [DOI] [PubMed] [Google Scholar]
  15. Dekleva M. L., Dasgupta B. R. Purification and characterization of a protease from Clostridium botulinum type A that nicks single-chain type A botulinum neurotoxin into the di-chain form. J Bacteriol. 1990 May;172(5):2498–2503. doi: 10.1128/jb.172.5.2498-2503.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Draper R. K., Chin D., Eurey-Owens D., Scheffler I. E., Simon M. I. Biochemical and genetic characterization of three hamster cell mutants resistant to diphtheria toxin. J Cell Biol. 1979 Oct;83(1):116–125. doi: 10.1083/jcb.83.1.116. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Drazin R., Kandel J., Collier R. J. Structure and activity of diphtheria toxin. II. Attack by trypsin at a specific site within the intact toxin molecule. J Biol Chem. 1971 Mar 10;246(5):1504–1510. [PubMed] [Google Scholar]
  18. Endo Y., Tsurugi K., Yutsudo T., Takeda Y., Ogasawara T., Igarashi K. Site of action of a Vero toxin (VT2) from Escherichia coli O157:H7 and of Shiga toxin on eukaryotic ribosomes. RNA N-glycosidase activity of the toxins. Eur J Biochem. 1988 Jan 15;171(1-2):45–50. doi: 10.1111/j.1432-1033.1988.tb13756.x. [DOI] [PubMed] [Google Scholar]
  19. Ezzell J. W., Jr, Abshire T. G. Serum protease cleavage of Bacillus anthracis protective antigen. J Gen Microbiol. 1992 Mar;138(3):543–549. doi: 10.1099/00221287-138-3-543. [DOI] [PubMed] [Google Scholar]
  20. Friedlander A. M. Macrophages are sensitive to anthrax lethal toxin through an acid-dependent process. J Biol Chem. 1986 Jun 5;261(16):7123–7126. [PubMed] [Google Scholar]
  21. Fryling C., Ogata M., FitzGerald D. Characterization of a cellular protease that cleaves Pseudomonas exotoxin. Infect Immun. 1992 Feb;60(2):497–502. doi: 10.1128/iai.60.2.497-502.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Giménez J. A., DasGupta B. R. Botulinum neurotoxin type E fragmented with endoproteinase Lys-C reveals the site trypsin nicks and homology with tetanus neurotoxin. Biochimie. 1990 Apr;72(4):213–217. doi: 10.1016/0300-9084(90)90075-r. [DOI] [PubMed] [Google Scholar]
  23. Gordon V. M., Leppla S. H., Hewlett E. L. Inhibitors of receptor-mediated endocytosis block the entry of Bacillus anthracis adenylate cyclase toxin but not that of Bordetella pertussis adenylate cyclase toxin. Infect Immun. 1988 May;56(5):1066–1069. doi: 10.1128/iai.56.5.1066-1069.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Grodberg J., Dunn J. J. ompT encodes the Escherichia coli outer membrane protease that cleaves T7 RNA polymerase during purification. J Bacteriol. 1988 Mar;170(3):1245–1253. doi: 10.1128/jb.170.3.1245-1253.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Habermann E., Weller U., Hudel M. Limited proteolysis of single-chain tetanus toxin by tissue enzymes, in cultured brain tissue and during retrograde axonal to the spinal cord. Naunyn Schmiedebergs Arch Pharmacol. 1991 Mar;343(3):323–329. doi: 10.1007/BF00251134. [DOI] [PubMed] [Google Scholar]
  26. Hallenberger S., Bosch V., Angliker H., Shaw E., Klenk H. D., Garten W. Inhibition of furin-mediated cleavage activation of HIV-1 glycoprotein gp160. Nature. 1992 Nov 26;360(6402):358–361. doi: 10.1038/360358a0. [DOI] [PubMed] [Google Scholar]
  27. Helting T. B., Parschat S., Engelhardt H. Structure of tetanus toxin. Demonstration and separation of a specific enzyme converting intracellular tetanus toxin to the extracellular form. J Biol Chem. 1979 Nov 10;254(21):10728–10733. [PubMed] [Google Scholar]
  28. Hirst T. R., Holmgren J. Conformation of protein secreted across bacterial outer membranes: a study of enterotoxin translocation from Vibrio cholerae. Proc Natl Acad Sci U S A. 1987 Nov;84(21):7418–7422. doi: 10.1073/pnas.84.21.7418. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Hosaka M., Nagahama M., Kim W. S., Watanabe T., Hatsuzawa K., Ikemizu J., Murakami K., Nakayama K. Arg-X-Lys/Arg-Arg motif as a signal for precursor cleavage catalyzed by furin within the constitutive secretory pathway. J Biol Chem. 1991 Jul 5;266(19):12127–12130. [PubMed] [Google Scholar]
  30. Jacewicz M., Clausen H., Nudelman E., Donohue-Rolfe A., Keusch G. T. Pathogenesis of shigella diarrhea. XI. Isolation of a shigella toxin-binding glycolipid from rabbit jejunum and HeLa cells and its identification as globotriaosylceramide. J Exp Med. 1986 Jun 1;163(6):1391–1404. doi: 10.1084/jem.163.6.1391. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. Jinno Y., Ogata M., Chaudhary V. K., Willingham M. C., Adhya S., FitzGerald D., Pastan I. Domain II mutants of Pseudomonas exotoxin deficient in translocation. J Biol Chem. 1989 Sep 25;264(27):15953–15959. [PubMed] [Google Scholar]
  32. Kitamura M., Iwamori M., Nagai Y. Interaction between Clostridium botulinum neurotoxin and gangliosides. Biochim Biophys Acta. 1980 Mar 20;628(3):328–335. doi: 10.1016/0304-4165(80)90382-7. [DOI] [PubMed] [Google Scholar]
  33. Klimpel K. R., Molloy S. S., Thomas G., Leppla S. H. Anthrax toxin protective antigen is activated by a cell surface protease with the sequence specificity and catalytic properties of furin. Proc Natl Acad Sci U S A. 1992 Nov 1;89(21):10277–10281. doi: 10.1073/pnas.89.21.10277. [DOI] [PMC free article] [PubMed] [Google Scholar]
  34. Koehler T. M., Collier R. J. Anthrax toxin protective antigen: low-pH-induced hydrophobicity and channel formation in liposomes. Mol Microbiol. 1991 Jun;5(6):1501–1506. doi: 10.1111/j.1365-2958.1991.tb00796.x. [DOI] [PubMed] [Google Scholar]
  35. Kounnas M. Z., Morris R. E., Thompson M. R., FitzGerald D. J., Strickland D. K., Saelinger C. B. The alpha 2-macroglobulin receptor/low density lipoprotein receptor-related protein binds and internalizes Pseudomonas exotoxin A. J Biol Chem. 1992 Jun 25;267(18):12420–12423. [PubMed] [Google Scholar]
  36. Krieglstein K. G., Henschen A. H., Weller U., Habermann E. Limited proteolysis of tetanus toxin. Relation to activity and identification of cleavage sites. Eur J Biochem. 1991 Nov 15;202(1):41–51. doi: 10.1111/j.1432-1033.1991.tb16342.x. [DOI] [PubMed] [Google Scholar]
  37. Leppla S. H. Anthrax toxin edema factor: a bacterial adenylate cyclase that increases cyclic AMP concentrations of eukaryotic cells. Proc Natl Acad Sci U S A. 1982 May;79(10):3162–3166. doi: 10.1073/pnas.79.10.3162. [DOI] [PMC free article] [PubMed] [Google Scholar]
  38. Lindberg A. A., Brown J. E., Strömberg N., Westling-Ryd M., Schultz J. E., Karlsson K. A. Identification of the carbohydrate receptor for Shiga toxin produced by Shigella dysenteriae type 1. J Biol Chem. 1987 Feb 5;262(4):1779–1785. [PubMed] [Google Scholar]
  39. Madshus I. H., Stenmark H., Sandvig K., Olsnes S. Entry of diphtheria toxin-protein A chimeras into cells. J Biol Chem. 1991 Sep 15;266(26):17446–17453. [PubMed] [Google Scholar]
  40. Mekalanos J. J., Swartz D. J., Pearson G. D., Harford N., Groyne F., de Wilde M. Cholera toxin genes: nucleotide sequence, deletion analysis and vaccine development. Nature. 1983 Dec 8;306(5943):551–557. doi: 10.1038/306551a0. [DOI] [PubMed] [Google Scholar]
  41. Milne J. C., Collier R. J. pH-dependent permeabilization of the plasma membrane of mammalian cells by anthrax protective antigen. Mol Microbiol. 1993 Nov;10(3):647–653. doi: 10.1111/j.1365-2958.1993.tb00936.x. [DOI] [PubMed] [Google Scholar]
  42. Misumi Y., Oda K., Fujiwara T., Takami N., Tashiro K., Ikehara Y. Functional expression of furin demonstrating its intracellular localization and endoprotease activity for processing of proalbumin and complement pro-C3. J Biol Chem. 1991 Sep 5;266(25):16954–16959. [PubMed] [Google Scholar]
  43. Moehring J. M., Inocencio N. M., Robertson B. J., Moehring T. J. Expression of mouse furin in a Chinese hamster cell resistant to Pseudomonas exotoxin A and viruses complements the genetic lesion. J Biol Chem. 1993 Feb 5;268(4):2590–2594. [PubMed] [Google Scholar]
  44. Moehring J. M., Moehring T. J. Characterization of the diphtheria toxin-resistance system in Chinese hamster ovary cells. Somatic Cell Genet. 1979 Jul;5(4):453–468. doi: 10.1007/BF01538880. [DOI] [PubMed] [Google Scholar]
  45. Moehring J. M., Moehring T. J. Strains of CHO-K1 cells resistant to Pseudomonas exotoxin A and cross-resistant to diphtheria toxin and viruses. Infect Immun. 1983 Sep;41(3):998–1009. doi: 10.1128/iai.41.3.998-1009.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  46. Molloy S. S., Bresnahan P. A., Leppla S. H., Klimpel K. R., Thomas G. Human furin is a calcium-dependent serine endoprotease that recognizes the sequence Arg-X-X-Arg and efficiently cleaves anthrax toxin protective antigen. J Biol Chem. 1992 Aug 15;267(23):16396–16402. [PubMed] [Google Scholar]
  47. Moskaug J. O., Sletten K., Sandvig K., Olsnes S. Translocation of diphtheria toxin A-fragment to the cytosol. Role of the site of interfragment cleavage. J Biol Chem. 1989 Sep 15;264(26):15709–15713. [PubMed] [Google Scholar]
  48. Naglich J. G., Metherall J. E., Russell D. W., Eidels L. Expression cloning of a diphtheria toxin receptor: identity with a heparin-binding EGF-like growth factor precursor. Cell. 1992 Jun 12;69(6):1051–1061. doi: 10.1016/0092-8674(92)90623-k. [DOI] [PubMed] [Google Scholar]
  49. Nakayama K., Watanabe T., Nakagawa T., Kim W. S., Nagahama M., Hosaka M., Hatsuzawa K., Kondoh-Hashiba K., Murakami K. Consensus sequence for precursor processing at mono-arginyl sites. Evidence for the involvement of a Kex2-like endoprotease in precursor cleavages at both dibasic and mono-arginyl sites. J Biol Chem. 1992 Aug 15;267(23):16335–16340. [PubMed] [Google Scholar]
  50. O'Brien A. D., LaVeck G. D. Purification and characterization of a Shigella dysenteriae 1-like toxin produced by Escherichia coli. Infect Immun. 1983 May;40(2):675–683. doi: 10.1128/iai.40.2.675-683.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  51. O'Brien A. D., Tesh V. L., Donohue-Rolfe A., Jackson M. P., Olsnes S., Sandvig K., Lindberg A. A., Keusch G. T. Shiga toxin: biochemistry, genetics, mode of action, and role in pathogenesis. Curr Top Microbiol Immunol. 1992;180:65–94. doi: 10.1007/978-3-642-77238-2_4. [DOI] [PubMed] [Google Scholar]
  52. O'Hare M., Brown A. N., Hussain K., Gebhardt A., Watson G., Roberts L. M., Vitetta E. S., Thorpe P. E., Lord J. M. Cytotoxicity of a recombinant ricin-A-chain fusion protein containing a proteolytically-cleavable spacer sequence. FEBS Lett. 1990 Oct 29;273(1-2):200–204. doi: 10.1016/0014-5793(90)81084-2. [DOI] [PubMed] [Google Scholar]
  53. Ogata M., Chaudhary V. K., Pastan I., FitzGerald D. J. Processing of Pseudomonas exotoxin by a cellular protease results in the generation of a 37,000-Da toxin fragment that is translocated to the cytosol. J Biol Chem. 1990 Nov 25;265(33):20678–20685. [PubMed] [Google Scholar]
  54. Ogata M., Fryling C. M., Pastan I., FitzGerald D. J. Cell-mediated cleavage of Pseudomonas exotoxin between Arg279 and Gly280 generates the enzymatically active fragment which translocates to the cytosol. J Biol Chem. 1992 Dec 15;267(35):25396–25401. [PubMed] [Google Scholar]
  55. Ohishi I. Activation of botulinum C2 toxin by trypsin. Infect Immun. 1987 Jun;55(6):1461–1465. doi: 10.1128/iai.55.6.1461-1465.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  56. Ohishi I., Iwasaki M., Sakaguchi G. Purification and characterization of two components of botulinum C2 toxin. Infect Immun. 1980 Dec;30(3):668–673. doi: 10.1128/iai.30.3.668-673.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  57. Ohishi I., Tsuyama S. ADP-ribosylation of nonmuscle actin with component I of C2 toxin. Biochem Biophys Res Commun. 1986 Apr 29;136(2):802–806. doi: 10.1016/0006-291x(86)90511-5. [DOI] [PubMed] [Google Scholar]
  58. Ohishi I., Yanagimoto A. Visualizations of binding and internalization of two nonlinked protein components of botulinum C2 toxin in tissue culture cells. Infect Immun. 1992 Nov;60(11):4648–4655. doi: 10.1128/iai.60.11.4648-4655.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  59. Olsnes S., Reisbig R., Eiklid K. Subunit structure of Shigella cytotoxin. J Biol Chem. 1981 Aug 25;256(16):8732–8738. [PubMed] [Google Scholar]
  60. Pappenheimer A. M., Jr Diphtheria toxin. Annu Rev Biochem. 1977;46:69–94. doi: 10.1146/annurev.bi.46.070177.000441. [DOI] [PubMed] [Google Scholar]
  61. Pastan I., Chaudhary V., FitzGerald D. J. Recombinant toxins as novel therapeutic agents. Annu Rev Biochem. 1992;61:331–354. doi: 10.1146/annurev.bi.61.070192.001555. [DOI] [PubMed] [Google Scholar]
  62. Sandvig K., Dubinina E., Garred O., Prydz K., Kozlov J. V., Hansen S. H., Van Deurs B. Entry of Shiga toxin into cells. Zentralbl Bakteriol. 1993 Apr;278(2-3):296–305. doi: 10.1016/s0934-8840(11)80846-7. [DOI] [PubMed] [Google Scholar]
  63. Sandvig K., Garred O., Prydz K., Kozlov J. V., Hansen S. H., van Deurs B. Retrograde transport of endocytosed Shiga toxin to the endoplasmic reticulum. Nature. 1992 Aug 6;358(6386):510–512. doi: 10.1038/358510a0. [DOI] [PubMed] [Google Scholar]
  64. Sandvig K., Olsnes S. Rapid entry of nicked diphtheria toxin into cells at low pH. Characterization of the entry process and effects of low pH on the toxin molecule. J Biol Chem. 1981 Sep 10;256(17):9068–9076. [PubMed] [Google Scholar]
  65. Schiavo G., Benfenati F., Poulain B., Rossetto O., Polverino de Laureto P., DasGupta B. R., Montecucco C. Tetanus and botulinum-B neurotoxins block neurotransmitter release by proteolytic cleavage of synaptobrevin. Nature. 1992 Oct 29;359(6398):832–835. doi: 10.1038/359832a0. [DOI] [PubMed] [Google Scholar]
  66. Schiavo G., Rossetto O., Santucci A., DasGupta B. R., Montecucco C. Botulinum neurotoxins are zinc proteins. J Biol Chem. 1992 Nov 25;267(33):23479–23483. [PubMed] [Google Scholar]
  67. Seetharam S., Chaudhary V. K., FitzGerald D., Pastan I. Increased cytotoxic activity of Pseudomonas exotoxin and two chimeric toxins ending in KDEL. J Biol Chem. 1991 Sep 15;266(26):17376–17381. [PubMed] [Google Scholar]
  68. Simpson L. L. Molecular pharmacology of botulinum toxin and tetanus toxin. Annu Rev Pharmacol Toxicol. 1986;26:427–453. doi: 10.1146/annurev.pa.26.040186.002235. [DOI] [PubMed] [Google Scholar]
  69. Simpson L. L., Stiles B. G., Zepeda H., Wilkins T. D. Production by Clostridium spiroforme of an iotalike toxin that possesses mono(ADP-ribosyl)transferase activity: identification of a novel class of ADP-ribosyltransferases. Infect Immun. 1989 Jan;57(1):255–261. doi: 10.1128/iai.57.1.255-261.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  70. Singh Y., Chaudhary V. K., Leppla S. H. A deleted variant of Bacillus anthracis protective antigen is non-toxic and blocks anthrax toxin action in vivo. J Biol Chem. 1989 Nov 15;264(32):19103–19107. [PubMed] [Google Scholar]
  71. Steiner D. F., Smeekens S. P., Ohagi S., Chan S. J. The new enzymology of precursor processing endoproteases. J Biol Chem. 1992 Nov 25;267(33):23435–23438. [PubMed] [Google Scholar]
  72. Stieneke-Gröber A., Vey M., Angliker H., Shaw E., Thomas G., Roberts C., Klenk H. D., Garten W. Influenza virus hemagglutinin with multibasic cleavage site is activated by furin, a subtilisin-like endoprotease. EMBO J. 1992 Jul;11(7):2407–2414. doi: 10.1002/j.1460-2075.1992.tb05305.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  73. Strauch K. L., Johnson K., Beckwith J. Characterization of degP, a gene required for proteolysis in the cell envelope and essential for growth of Escherichia coli at high temperature. J Bacteriol. 1989 May;171(5):2689–2696. doi: 10.1128/jb.171.5.2689-2696.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  74. Strom T. B., Anderson P. L., Rubin-Kelley V. E., Williams D. P., Kiyokawa T., Murphy J. R. Immunotoxins and cytokine toxin fusion proteins. Ann N Y Acad Sci. 1991 Dec 30;636:233–250. doi: 10.1111/j.1749-6632.1991.tb33455.x. [DOI] [PubMed] [Google Scholar]
  75. Syuto B., Kubo S. Separation and characterization of heavy and light chains from Clostridium botulinum type C toxin and their reconstitution. J Biol Chem. 1981 Apr 25;256(8):3712–3717. [PubMed] [Google Scholar]
  76. Takao T., Tanabe T., Hong Y. M., Shimonishi Y., Kurazono H., Yutsudo T., Sasakawa C., Yoshikawa M., Takeda Y. Identity of molecular structure of Shiga-like toxin I (VT1) from Escherichia coli O157:H7 with that of Shiga toxin. Microb Pathog. 1988 Nov;5(5):57–69. doi: 10.1016/0882-4010(88)90036-8. [DOI] [PubMed] [Google Scholar]
  77. Theuer C. P., FitzGerald D., Pastan I. A recombinant form of Pseudomonas exotoxin directed at the epidermal growth factor receptor that is cytotoxic without requiring proteolytic processing. J Biol Chem. 1992 Aug 25;267(24):16872–16877. [PubMed] [Google Scholar]
  78. Vitetta E. S., Thorpe P. E. Immunotoxins containing ricin or its A chain. Semin Cell Biol. 1991 Feb;2(1):47–58. [PubMed] [Google Scholar]
  79. Wandersman C. Secretion, processing and activation of bacterial extracellular proteases. Mol Microbiol. 1989 Dec;3(12):1825–1831. doi: 10.1111/j.1365-2958.1989.tb00169.x. [DOI] [PubMed] [Google Scholar]
  80. Wasley L. C., Rehemtulla A., Bristol J. A., Kaufman R. J. PACE/furin can process the vitamin K-dependent pro-factor IX precursor within the secretory pathway. J Biol Chem. 1993 Apr 25;268(12):8458–8465. [PubMed] [Google Scholar]
  81. Watanabe T., Murakami K., Nakayama K. Positional and additive effects of basic amino acids on processing of precursor proteins within the constitutive secretory pathway. FEBS Lett. 1993 Apr 12;320(3):215–218. doi: 10.1016/0014-5793(93)80589-m. [DOI] [PubMed] [Google Scholar]
  82. Watson D. G., Moehring J. M., Moehring T. J. A mutant CHO-K1 strain with resistance to Pseudomonas exotoxin A and alphaviruses fails to cleave Sindbis virus glycoprotein PE2. J Virol. 1991 May;65(5):2332–2339. doi: 10.1128/jvi.65.5.2332-2339.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  83. Williams D. P., Wen Z., Watson R. S., Boyd J., Strom T. B., Murphy J. R. Cellular processing of the interleukin-2 fusion toxin DAB486-IL-2 and efficient delivery of diphtheria fragment A to the cytosol of target cells requires Arg194. J Biol Chem. 1990 Nov 25;265(33):20673–20677. [PubMed] [Google Scholar]
  84. Yoshida T., Chen C. C., Zhang M. S., Wu H. C. Disruption of the Golgi apparatus by brefeldin A inhibits the cytotoxicity of ricin, modeccin, and Pseudomonas toxin. Exp Cell Res. 1991 Feb;192(2):389–395. doi: 10.1016/0014-4827(91)90056-z. [DOI] [PubMed] [Google Scholar]
  85. van de Ven W. J., Voorberg J., Fontijn R., Pannekoek H., van den Ouweland A. M., van Duijnhoven H. L., Roebroek A. J., Siezen R. J. Furin is a subtilisin-like proprotein processing enzyme in higher eukaryotes. Mol Biol Rep. 1990 Nov;14(4):265–275. doi: 10.1007/BF00429896. [DOI] [PubMed] [Google Scholar]

Articles from Infection and Immunity are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES