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A complete amino acid sequence for the basic subunit of crotoxin.

S D Aird, I I Kaiser, R V Lewis

    Archives of Biochemistry and Biophysics
    |September 1, 1986
    PubMed
    Summary
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    The complete amino acid sequence of the basic subunit of crotoxin from Crotalus durissus terrificus venom was determined. This research clarifies sequence differences and allelic variations in this toxic protein.

    Area of Science:

    • Biochemistry
    • Toxicology
    • Protein Chemistry

    Background:

    • Crotoxin is a major neurotoxin found in the venom of Crotalus durissus terrificus.
    • The basic subunit of crotoxin is a phospholipase A2 enzyme, crucial for its toxic activity.
    • Previous sequence data for the basic subunit had some ambiguities and potential inaccuracies.

    Purpose of the Study:

    • To determine the complete and accurate amino acid sequence of the basic subunit of crotoxin.
    • To identify and resolve discrepancies with previously reported sequences.
    • To compare the sequence with other phospholipase A2 enzymes.

    Main Methods:

    • Protein fragmentation using cyanogen bromide.
    • Enzymatic digestion with arginine- and lysine-specific endoproteases.

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  • Amino acid sequencing and comparison with existing databases.

    • Main Results:

    • The complete amino acid sequence of the basic subunit was elucidated.
    • Specific differences were identified compared to prior reports, including corrections at positions 60-61 (Lys-Trp) and identification of Ser at position 99 and Tyr at position 105.
    • Allelic variations were observed at positions 33, 37, and 69, indicating natural diversity within the venom.
    • Structural similarity was found with other viperid and crotalid phospholipases A2.

    Conclusions:

    • The determined sequence provides a more accurate representation of the basic subunit of crotoxin.
    • The findings contribute to understanding the structural basis of crotoxin's toxicity and its evolutionary relationships with other snake venom phospholipases A2.
    • The identified allelic variations highlight the complexity of snake venom composition.