Immunogenicity of mastoparan B, a cationic tetradecapeptide isolated from the hornet (Vespa basaus) venom, and its structural requirements

Ho Chewn-Lang, Lin Yah-Luen, Chen Wan-Chen, Yu Hui-Ming, Wang Kung-Tsung, Hwang Ling-Ling, Chen Chiung-Tong

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Abstract

Mastoparan B (MP-B) is a cationic tetradecapeptide (LKLKSIVSWAKKVL-CONH2, mol. wt 1611) isolated from the black-bellied hornet (Vespa basalis) venom. The small peptide itself was capable of inducing antibodies without prior conjugation to a protein carrier in rabbits and mice. The mouse antibody was found to be of IgG1 isotype with κ-type light chain. The peptide antigen was able to form insoluble complexes with the specific antibody, suggesting that MP-B possessed more than one epitope in its molecule. The finding that MP-B was able to bind with both mouse and rabbit antibodies in sandwich ELISA supports this contention. Synthetic MP-B analogues in which lysine at position 2, 4, 11 or 12 was replaced by neutral amino acids such as asparagine or leucine showed a significant decrease in their antibody-binding activities. Substitution of lysine at position 4 (Lys4) caused the most marked inhibition in its binding activity. However, replacing tryptophan at position 9 by tyrosine caused a relatively small reduction in its binding activity. Replacing both Lys2,4 by asparagine or removing Lys-containing segments at amino or carboxyl terminus in MP-B sequence caused a remarkable decrease in the antibody-binding and immunogenic activities of the peptide. The Lys residues located at amino and carboxyl terminal segments of MP-B, especially Lys4, appear to play a critical role in the binding interaction and the immunogenicity of the peptide.

Original languageEnglish
Pages (from-to)1443-1451
Number of pages9
JournalToxicon
Volume33
Issue number11
DOIs
Publication statusPublished - 1995
Externally publishedYes

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ASJC Scopus subject areas

  • Toxicology

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