title: Influence of N-terminal amino acids & conjugation position to carrier on specificities of antibodies elicited by malaria peptides.
abstract: The specificity of murine antibodies raised against structurally related peptides derived from a malaria parasite membrane protein was studied. The peptides were conjugated to bovine serum albumin (BSA) with 6-maleimido caproic acyl N-hydroxysuccinimide ester before immunization. Conjugation to BSA through a C-terminal or an internal cysteine residue elicited antibodies with noticeably different specificities. An N-terminal tripeptide sequence arginine-asparagine-asparagine had a dominant influence on the immunogenicity of the peptides. Such factors need to be taken into consideration while designing peptide-based immunogens.
authors.affiliation: Division of Life Sciences, Institute of Fundamental Studies, Kandy, Sri Lanka.
authors.forename: R
authors.initials: R
authors.lastname: Ramasamy
authors.forename: C
authors.initials: C
authors.lastname: Wickremaratne
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D000913:Antibodies, Protozoan / Q000276:immunology*; D000918:Antibody Specificity; D004797:Enzyme-Linked Immunosorbent Assay; D008288:Malaria / Q000378:metabolism*; D051379:Mice; D008807:Mice, Inbred BALB C; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000235:genetics* / Q000276:immunology*; D015800:Protozoan Proteins / Q000235:genetics* / Q000276:immunology*
chemical_list: D000913:Antibodies, Protozoan; D010446:Peptide Fragments; D015800:Protozoan Proteins