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Biomedical subjects

G H STOLLERMAN

Publications and source records attributed to G H STOLLERMAN.

At least 19 recordsLinked to original sources
PubMed1963

Accessory plasma factors involved in the bactericidal test for type-specific antibody to group A Streptococci. II. Human plasma cofactor (s) enhancing opsonization of encapsulated organisms.

A study was made of the nature of the thermolabile plasma factors in human blood which promote the phagocytosis of Group A streptococci in vitro in the presence of optimal amounts of type-specific M antibody. The plasmas of individuals with strong opsonic activity (normal) were compared with those of some individuals whose opsonic activity was consistently weak (deficient). A general relationship was established between encapsulation of streptococci and the opsonic requirement for thermolabile plasma factor(s). Marked differences in phagocytosis of Group A organisms by human bloods were demonstrated with encapsulated strains only. Human bloods deficient in the cofactor required for opsonization of encapsulated streptococci (coopsonin) showed a normal rate of phagocytosis against all other organisms and particles studied. Furthermore, coopsonin-deficient bloods contained normal levels of four components of complement, of properdin, of lysozyme, and of direct bactericidal activity against several species of Gram-negative organisms and of E. coli bacteriophage. The independence of the streptococcal coopsonin from complement was also demonstrated by absorption of plasma with bentonite and with zymosan. Under appropriate conditions, the coopsonin was reduced without significant loss of complement. The data support the concept that the capsule of the streptococcus imposes an opsonic requirement for a plasma factor(s) which is present in varying amounts in human bloods and which appears to be independent of the complement system. The possibility that it is accessory to the latter components has not been excluded.

Antibodies↗
PubMed1960

Factors affecting the chain length of group A streptococci. I. Demonstration of a metabolically active chain-splitting system.

Group A streptococci which grew in long chains in the presence of homologous anti-M antibody were split into their original length by the addition of an excess of homologous M protein to the culture. The chain-splitting reaction showed temperature and pH optima (37 degrees C., 7.5) and was completely inhibited at 0 degrees C. or by heat-killing the long chains at 56 degrees C. prior to the addition of M protein. Addition of sublethal doses of HgCl(2), or of penicillin, inhibited the chain-splitting reaction. Pneumococci behaved in entirely comparable fashion to streptococci in similar experiments. Virulent strains of streptococci formed the shortest chains when broth media was enriched with serum. The chain-shortening effect of serum enrichment of the media was most apparent with encapsulated strains and under cultural conditions that favored capsule formation. Loss of capsules by mutation or by unfavorable growth conditions resulted in increase in chain length. The activity of the chain-splitting mechanism seemed to be independent of M protein, however, since encapsulated M-negative variants also formed very short chain in serum-enriched media. The physical presence of the capsule was not essential for chain shortening since enzymatic removal of the capsule with hyaluronidase during growth did not affect chain length. These results strongly suggest that chain-splitting of streptococci and pneumococci occurs by an active metabolic mechanism, presumably enzymatic, which is inhibited by the union of surface antigens with specific antibody.

Antibodies↗
PubMed1960

Factors affecting the chain length of group A streptococci. II. Quantative M-anti-M relationships in the long chain test.

Minute amounts of M protein were detected in culture supernates of virulent Group A streptococci by type-specific inhibition of the long chain and the bactericidal tests for anti-M antibody. The amount of M protein that was detected by the inhibition of these biological systems was less than could be demonstrated by precipitation tests. All strains of streptococci rich in M protein which were studied formed long chains when grown in sufficient concentrations of anti-M antibody. Very low concentrations of anti-M antibody escaped detection by the long chain test when strains of excessive M protein content were employed. Under such conditions the bactericidal test detected anti-M antibody more sensitively than the long chain test owing to the smaller inoculum employed in the former method. The scission of streptococcal chains may be inhibited by union of antibodies with surface antigens other than M protein. Long chains were formed when M-negative, R-positive strains were grown in sera containing anti-R antibody.

Anti-Bacterial Agents↗