Antigenic structure of the hexacosapeptide melittin: evidence for three determinants, one with a helical conformation.
ELISA-based epitope analysis was performed using rabbit polyclonal antisera against melittin. Antigenic sites were found at the C-terminus, in the middle section and within the N-terminal helix. Antibodies against the helical segment could discriminate between two faces of the amphiphilic helix. The antigenic sites include the bulk of the melittin hexacosapeptide, which is synonymous with a very high epitope density.
von Grünigen
R
R
University of Bern, Inselspital, Switzerland.
Schneider
C H
CH
D000595:Amino Acid Sequence; D000818:Animals; D001514:Bee Venoms / Q000276:immunology*; D004797:Enzyme-Linked Immunosorbent Assay; D000939:Epitopes / Q000302:isolation & purification*; D008555:Melitten / Q000276:immunology*; D008968:Molecular Conformation; D008969:Molecular Sequence Data
D001514:Bee Venoms; D000939:Epitopes; D008555:Melitten