作者: Kimberly W. Schuenke , Richard G. Cook , Robert R. Rich
DOI: 10.1016/S0198-8859(98)00072-X
关键词: HBsAg 、 Hepatitis B 、 Peptide binding 、 Major histocompatibility complex 、 Hepatitis B vaccine 、 Human leukocyte antigen 、 Epitope 、 Virology 、 Antibody 、 Biology
摘要: Abstract A small but significant proportion of people who receive the hepatitis B vaccine do not produce anti-hepatitis antibodies, a phenomenon associated with certain human leukocyte antigen (HLA) class II haplotypes. We were interested in determining whether natural allelic differences between two HLA-DR4 molecules responder versus nonresponder subtypes differed respect to binding an immunodominant surface (HBsAg) peptide as measured using resonant mirror biosensor. In contrast our original hypothesis, we found ten-fold difference affinity favor DRB1∗0401 allele, K D 6.89 × 10 −8 M 6.71 −7 for DRB1∗0404 allele. Half-times dissociation 1.3 min and 7.7 min, respectively, although association rate constants both HLA similar (approximately 4 −1 s ). Of particular interest was observation different on-rates during phase, suggesting that stoichiometry 1:1 or structural forms HLA-peptide complex exist. Our observations indicate whereas HBsAg is influenced by polymorphism, nonresponse this subtype result failure processed bind molecules.