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TitleImportance of the Cysteine-Rich Domain of Snake Venom Prothrombin Activators: Insights Gained from Synthetic Neutralizing Antibodies.
Journal, issue, pagesToxins (Basel), Vol. 16, Issue 8, Year 2024
Publish dateAug 15, 2024
AuthorsLaetitia E Misson Mindrebo / Jeffrey T Mindrebo / Quoc Tran / Mark C Wilkinson / Jessica M Smith / Megan Verma / Nicholas R Casewell / Gabriel C Lander / Joseph G Jardine /
PubMed AbstractSnake venoms are cocktails of biologically active molecules that have evolved to immobilize prey, but can also induce a severe pathology in humans that are bitten. While animal-derived polyclonal ...Snake venoms are cocktails of biologically active molecules that have evolved to immobilize prey, but can also induce a severe pathology in humans that are bitten. While animal-derived polyclonal antivenoms are the primary treatment for snakebites, they often have limitations in efficacy and can cause severe adverse side effects. Building on recent efforts to develop improved antivenoms, notably through monoclonal antibodies, requires a comprehensive understanding of venom toxins. Among these toxins, snake venom metalloproteinases (SVMPs) play a pivotal role, particularly in viper envenomation, causing tissue damage, hemorrhage and coagulation disruption. One of the current challenges in the development of neutralizing monoclonal antibodies against SVMPs is the large size of the protein and the lack of existing knowledge of neutralizing epitopes. Here, we screened a synthetic human antibody library to isolate monoclonal antibodies against an SVMP from saw-scaled viper (genus ) venom. Upon characterization, several antibodies were identified that effectively blocked SVMP-mediated prothrombin activation. Cryo-electron microscopy revealed the structural basis of antibody-mediated neutralization, pinpointing the non-catalytic cysteine-rich domain of SVMPs as a crucial target. These findings emphasize the importance of understanding the molecular mechanisms of SVMPs to counter their toxic effects, thus advancing the development of more effective antivenoms.
External linksToxins (Basel) / PubMed:39195771 / PubMed Central
MethodsEM (single particle)
Resolution3.43 Å
Structure data

45728

9clp

EMDB-45728, PDB-9clp:
Structure of ecarin from the venom of Kenyan saw-scaled viper in complex with the Fab of neutralizing antibody H11
Method: EM (single particle) / Resolution: 3.43 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-CA:
Unknown entry

Source
  • Echis pyramidum leakeyi (Leakey's carpet viper)
  • echis carinatus (saw-scaled viper)
  • homo sapiens (human)
KeywordsHYDROLASE / Snake venom metalloproteinase / neutralizing antibody

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