Characteristics of a High Molecular Weight Extracellular Protein of Streptococcus mutans

• Published in: Journal of general microbiology Vol. 129; no. 9; pp. 2779 - 2788
• Main Authors: Forester, Henry, Hunter, Neil, Knox, Kenneth W
• Format: Journal Article
• Language: English
• Published: London Soc General Microbiol 01.09.1983; New York, NY Cambridge University Press
• Subjects: Amino Acids - analysis; Animals; Antigens, Bacterial - analysis; Antigens, Bacterial - immunology; Antigens, Bacterial - isolation & purification; Bacteriology; Biological and medical sciences; Cross Reactions; Electrophoresis, Polyacrylamide Gel; Fundamental and applied biological sciences. Psychology; Immune Sera; Immunodiffusion; Metabolism. Enzymes; Microbiology; Molecular Weight; Myocardium - immunology; Rabbits; Streptococcus mutans; Streptococcus mutans - immunology; Proteins; Antigenicity; Extracellular; Physicochemical properties; Production; Streptococcus mutans
• ISSN: 0022-1287; 1350-0872; 1465-2080
• DOI: 10.1099/00221287-129-9-2779

Institute of Dental Research, United Dental Hospital, Chalmers Street, Sydney NSW 2010, Australia ABSTRACT Summary: A high molecular weight protein antigen, designated P1, has been isolated from the culture fluid of chemostat-grown Streptococcus mutans strain Ingbritt and shown to be free of other antigens including glucosyltransferase. Antiserum against the protein was used in rocket immunoelectro-phoresis to confirm and extend the previous observation that there were major differences in the amount of the protein produced under different growth conditions. Physico-chemical and serological studies indicated that protein P1 was indistinguishable from antigens B, I II and IF isolated in other laboratories. Mammalian tissue cross-reactivity of protein P1 was demonstrated by binding of antiserum to P1 to sections of normal rabbit tissues, particularly heart. There was also a statistically significant increase in the number of mononuclear leucocytes in heart tissue of rabbits which had been injected with protein P1, when compared with the levels in control uninjected rabbits; injection with whole cells of S. mutans Ingbritt did not produce this effect.