Fine mapping of an immunodominant domain in the transmembrane glycoprotein of human immunodeficiency virus.
Sera from virtually all individuals infected with human immunodeficiency virus contain antibodies against the viral envelope glycoproteins. By using a series of synthetic peptide antigens, we identified an immunodominant domain at amino acid position 598-609 of gp41. The minimal essential epitope is a 7-amino-acid sequence (amino acids 603-609) containing two cysteine residues. Both cysteine residues are required for the antigenic conformation of the sequence, possibly due to creation of a cyclic structure via disulfide bond formation.
D000163:Acquired Immunodeficiency Syndrome / Q000276:immunology; D000595:Amino Acid Sequence; D000914:Antibodies, Viral / Q000032:analysis; D000956:Antigens, Viral / Q000276:immunology*; D000939:Epitopes; D006023:Glycoproteins / Q000276:immunology*; D006678:HIV / Q000276:immunology*; D006801:Humans; D008565:Membrane Proteins / Q000276:immunology*; D010446:Peptide Fragments / Q000138:chemical synthesis / Q000276:immunology; D013329:Structure-Activity Relationship; D014764:Viral Proteins / Q000276:immunology*
D000914:Antibodies, Viral; D000956:Antigens, Viral; D000939:Epitopes; D006023:Glycoproteins; D008565:Membrane Proteins; D010446:Peptide Fragments; D014764:Viral Proteins