title: Fine mapping of an immunodominant domain in the transmembrane glycoprotein of human immunodeficiency virus.
abstract: 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.
mesh_terms: 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*
chemical_list: D000914:Antibodies, Viral; D000956:Antigens, Viral; D000939:Epitopes; D006023:Glycoproteins; D008565:Membrane Proteins; D010446:Peptide Fragments; D014764:Viral Proteins