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Bothropstoxin-I: amino acid sequence and function

A C Cintra1, S Marangoni, B Oliveira

  • 1Departamento de Bioquímica, Faculdade de Medicina de Ribeirão Preto, Universidade de São Paulo, Brasil.

Journal of Protein Chemistry
|February 1, 1993
PubMed
Summary
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Bothropstoxin-I (BthTX-I) from Bothrops jararacussu snake venom is a Lys49 phospholipase A2 (PLA2)-like protein lacking detectable PLA2 activity due to specific amino acid mutations.

Area of Science:

  • Biochemistry
  • Toxicology
  • Molecular Biology

Background:

  • Snake venom contains various toxins, including phospholipase A2 (PLA2) enzymes.
  • Myotoxins are a class of toxins found in snake venom that specifically target muscle tissue.
  • Bothropstoxin-I (BthTX-I) is a component of Bothrops jararacussu snake venom.

Purpose of the Study:

  • To determine the complete amino acid sequence of bothropstoxin-I (BthTX-I).
  • To investigate the structural basis for the lack of phospholipase A2 (PLA2) activity in BthTX-I.
  • To compare the sequence of BthTX-I with other related myotoxins.

Main Methods:

  • Amino acid sequencing of bothropstoxin-I.
  • Sequence homology analysis with known phospholipase A2 (PLA2) enzymes and myotoxins.

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  • Identification of critical amino acid substitutions.

    • Main Results:

    • BthTX-I is a Lys49 phospholipase A2 (PLA2)-like protein with 121 amino acid residues.
    • BthTX-I lacks detectable PLA2 activity.
    • Sequence analysis revealed several critical mutations, including Lys49 for Asp49, correlating with the loss of PLA2 activity.
    • BthTX-I shares sequence homology with Asp49-PLA2s and other Lys49-myotoxins.

    Conclusions:

    • The absence of PLA2 activity in BthTX-I is attributed to specific amino acid substitutions.
    • BthTX-I represents a Lys49 myotoxin variant of PLA2 enzymes.
    • Comparative analysis provides insights into the structure-function relationships of snake venom toxins.