Filamentous capsulated streptococci from the human respiratory tract: chemical and immunochemical characterization of a glycoprotein capsular antigen of provisional binary capsular type 87.

A filamentous alpha-hemolytic streptococcus of provisional capsular type 87 isolated from the human respiratory tract has been shown to be binary capsulated. One of the capsular antigens appears to be a glycoprotein; the other appears to be a polysaccharide. Transformation reactions with deoxyribonucleic acid from streptococcus type 87 and a number of noncapsulated pneumococci yielded transformed pneumococci with either a glycoprotein capsule or a polysaccharide capsule, but not with both. Capsular precipitin (quellung) reactions were observed when streptococcus type 87 was treated with homologous antiserum or with antisera to either of the two distinct capsular transformants. Each of the transformed pneumococci gave a quellung reaction with its homologous antiserum or with antiserum to streptococcus type 87, but neither reacted with antiserum to the heterologous transformant. Chemical analysis showed the glycoprotein antigen of streptococcus type 87 to contain, in addition to amino acids, glucose, galactose, glucosamine, and phosphate. The amino acid composition of the glycoprotein capsular antigens from streptococcus type 87 and of those from transformed pneumococci were similar, showing only minor differences. The glycoprotein capsular antigen from streptococcus type 87 gave two closely associated precipitin bands with homologous antiserum or antisera to transformed pneumococci with the glycoprotein capsule. That the two precipitin bands represent two unrelated proteins is precluded largely on the basis of the unlikely probability of 100% cotransformation of the genes coding for both proteins in the pneumococcal transformants that were isolated. Chemical analyses of the various fractions of the glycoprotein indicate that the two precipitin bands may represent a glycoprotein and its corresponding apoprotein.