TY - JOUR
T1 - Immunogenicity of mastoparan B, a cationic tetradecapeptide isolated from the hornet (Vespa basaus) venom, and its structural requirements
AU - Chewn-Lang, Ho
AU - Yah-Luen, Lin
AU - Wan-Chen, Chen
AU - Hui-Ming, Yu
AU - Kung-Tsung, Wang
AU - Ling-Ling, Hwang
AU - Chiung-Tong, Chen
PY - 1995
Y1 - 1995
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0029190870&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0029190870&partnerID=8YFLogxK
U2 - 10.1016/0041-0101(95)00093-2
DO - 10.1016/0041-0101(95)00093-2
M3 - Article
C2 - 8744984
AN - SCOPUS:0029190870
VL - 33
SP - 1443
EP - 1451
JO - Toxicon
JF - Toxicon
SN - 0041-0101
IS - 11
ER -