Biomedical subjects

W A PIERCE

Publications and source records attributed to W A PIERCE.

14 recordsLinked to original sources

PubMed1965

EFFECT OF PARTIALLY PURIFIED STREPTOCOCCAL M PROTEIN ON THE IN VITRO PHAGOCYTOSIS OF STREPTOCOCCUS PYOGENES.

Domingue, Gerald J. (Tulane University, New Orleans, La.), and William A. Pierce, Jr. Effect of partially purified streptococcal M protein on the in vitro phagocytosis of Streptococcus pyogenes. J. Bacteriol. 89:583-588. 1965.-M protein from Streptococcus pyogenes strain Bailey type 12 was adsorbed onto cells of a glossy mutant of this strain. Phagocytosis experiments were performed in vitro with rabbit peritoneal polymorphonuclear leukocytes. Direct microscopic counts suggested M protein-treated cells were more resistant to phagocytosis than were untreated cells. With the Cohn and Morse technique for evaluating quantitatively the fate of bacteria during phagocytosis, there was observed a more rapid drop in total and extracellular counts of treated, as compared with untreated, cells. Experiments with radioactively labeled streptococci showed that M-treated cells were more readily destroyed within leukocytes than were nontreated glossy streptococci, which suggested a reason for the scarcity of treated streptococci in direct microscopic counts.

Agglutination↗

PubMed1964

IN VITRO PHAGOCYTOSIS OF STAPHYLOCOCCUS AUREUS WITH SPECIAL REFERENCE TO A POSSIBLE ANTIPHAGOCYTIC FUNCTION OF COAGULASE.

Borchardt, Kenneth A. (Tulane University School of Medicine, New Orleans, La.), and William A. Pierce, Jr. In vitro phagocytosis of Staphylococcus aureus with special reference to a possible antiphagocytic function of coagulase. J. Bacteriol. 87:311-315. 1964.-Rabbit antisera were prepared to Staphylococcus aureus strains of bacteriophage types 81 and 42D with vaccines consisting of washed, heat-killed cells grown in media which either did or did not support coagulase formation. Partially purified coagulases were prepared, and were used to produce rabbit anticoagulase antisera. In vitro phagocytic studies, with the two staphylococcal strains plus rabbit polymorphonuclear peritoneal exudate cells and the various types of rabbit antisera, did not yield evidence that coagulase per se contributes to staphylococcal resistance to either ingestion or intracellular killing. The role of coagulase, if any, in the virulence of these organisms for rabbits (and probably for man) must therefore be attributed to some other mechanism.

Animals↗

PubMed1964

ELECTROPHORETIC SEPARATION OF CONSTITUENTS OF PARTIALLY PURIFIED M PROTEIN OF STREPTOCOCCUS PYOGENES.

Pierce, William A., Jr. (Tulane University, New Orleans, La.). Electrophoretic separation of constituents of partially purified M protein of Streptococcus pyogenes. J. Bacteriol. 88:912-921. 1964.-Partially purified M protein of a group A, type 12 strain of Streptococcus pyogenes was studied by use of chemical, electrophoretic, and immunological techniques. It was demonstrated in immunodiffusion tests that the antigen contains multiple precipitating components. The type-specific antigen was identified, and evidence was presented that, in some instances at least, the cross-reactions observed between this type 12 M protein and heterologous antisera in immunodiffusion tests involve contaminating antigens rather than the component which precipitates with adsorbed homologous-typing antiserum. In passive hemagglutination tests where M protein was adsorbed to tanned sheep erythrocytes, it was found that antisera suitably adsorbed to show good specificity in capillary precipitin tests nevertheless still contain cross-reactive antibodies which are detectable by this more sensitive technique. Electrophoresis on starch paste separates some of the components of partially purified M protein, so that a fraction can be obtained which has fewer precipitating antigens, as determined in immunodiffusion tests, and which is less cross-reactive in passive hemagglutination tests with heterologous unadsorbed antistreptococcal antisera.

Animals↗

PubMed1963