The antigenic structure of HBsAg: study of the d/y subtype determinant by chemical modification and site directed mutagenesis.
Lysine residue 122 of the major protein of HBsAg/adw has been shown previously to be involved in the d subtype determinant. We demonstrate here that the corresponding residue of the HBsAg/ayw, arginine 122, does not play such a critical role the y site of this antigen subtype. Thus, conversion by site directed mutagenesis of arginine 122 to lysine 122 in HBsAg/ayw does not result in the loss of y activity nor gain of d activity. Moreover, chemical modification studies of both the adw and ayw antigens with the reagents o-methylisourea and cyclohexanedione, demonstrate that arginine 122 plays at most only a minor role in this subtype antigenic site.
Department of Immunology and Infectious Diseases, School of Hygiene and Public Health, Johns Hopkins University, Baltimore, MD 21205.
E
E
Guerrero
P D
PD
Swenson
P S
PS
Hu
D L
DL
Peterson
D000911:Antibodies, Monoclonal; D000918:Antibody Specificity; D001120:Arginine; D001483:Base Sequence; D003512:Cyclohexanones; D000939:Epitopes; D006514:Hepatitis B Surface Antigens / Q000235:genetics / Q000276:immunology*; D006801:Humans; D008239:Lysine; D008782:Methylurea Compounds; D008969:Molecular Sequence Data; D009154:Mutation; D010658:Phenylglyoxal; D012703:Serotyping
D000911:Antibodies, Monoclonal; D003512:Cyclohexanones; D000939:Epitopes; D006514:Hepatitis B Surface Antigens; D008782:Methylurea Compounds; C002249:O-methylisourea; D001120:Arginine; D008239:Lysine; D010658:Phenylglyoxal