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. 2011 Mar 22;3(3):309–344. doi: 10.3390/toxins3030309

Table 1.

An overview of toxin families in Loxosceles genus.

Toxins MW (kDa) Characteristics and actions described No. Seq *
Phospholipases-D (SicTox family members, such as LiRecDTs) 30–35 Several isoforms with variant features such as: 335
Insecticidal peptides 5–8
  • - LiTx family members [23,27] and Magi 3-related peptides [23,27,51]

  • - LiTx: Lethal to S. frugiperda (flaccid paralysis) [23]

  • - LiTx3: appears to act upon Na+ channels [23]

8
Metalloproteases 28–35
  • - Astacin-like Metalloprotease (LALPs) [29,52]

  • - Present in the venom of different species of Loxosceles genus [12,13,27,51,53]

  • - Activity upon gelatin, fibronectin, fibrinogen and entactin [18,52,53,54]

4
Hyaluronidases 41–43
  • - Classified as endo-beta-N-acetyl-d-hexosaminidases hydrolases [14]

  • - Activity upon hyaluronic acid and chondroitin sulphate [13,14]

  • - Present in the venom of different species of Loxosceles genus [12,13,14,24,27,51,55]

-
Serine-proteases 85–95
  • - Gelatinolytic activity [19]

  • - Activated in vitro by trypsin [19]

  • - Present in the venom of L. intermedia and L. laeta [27,51]

-
Serine/Cysteine protease inhibitors N.D.
  • - Belongs to Serpin superfamily [27]

  • - Identified in Loxosceles spp. transcriptomes and proteome [24,27,51]

  • - May be related to coagulation processes, fibrinolysis and inflammation [51]

-
TCTP (translationally controlled tumour protein) ~46
  • - Identified in Loxosceles spp. transcriptomes [27,51]

  • - Putative functions: Histamine releasing factor in extracellular environment; several intracellular roles such as embryonic development, cell proliferation, stabilization of microtubules [56]

-
Lectin-like N.D. - Putative features: carbohydrate-binding molecules; involved in extracellular matrix organization, endocytosis, complement activation, etc. [51] -
Alkaline-phosphatase N.D. - Degrades the synthetic substrate p-nitrophenyl phosphate[10] -
ATPase N.D - ATP hydrolysis [10] -

N.D.: not determined. *Number of sequences deposited in PUBMED protein database.