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PMID: 6995311 Published · ppublish English Journal Article

Protein antigens of Streptococcus mutans: purification and properties of a double antigen and its protease-resistant component.

Infection and immunity ·Vol. 28 ·No. 2 ·1980-05-00 ·Pages 486-93

Russell MW, Bergmeier LA, Zanders ED, Lehner T

Abstract

A surface protein antigen of Streptococcus mutans having two sets of antigenic determinants (antigens I and II) was purified by column chromatography from culture supernatants of S. mutans serotype c. The protease-resistant component, antigen II, was purified from pronase-digested antigen I/II. The antigens were analyzed chemically and immunologically, and their physicochemical properties were investigated. Antigen I/II consisted of more than 80% protein, and its peptide chain molecular weight was estimated to be 185,000. Antigen II consisted of approximately 60% protein, with a peptide chain molecular weight of 48,000. Antisera to antigens I/II and II were raised in rabbits and used to investigate the presence of the antigens in cells of other streptococci. This indicated that not only serotype c but also serotypes e and f possessed antigen I and II determinants, whereas serotypes a, d, and g possessed a determinant related to antigen I but not one related to antigen II.

MeSH Terms
Amino Acids/analysis Animals Antigens, Bacterial/analysis,isolation & purification Electrophoresis, Polyacrylamide Gel Fluorescent Antibody Technique Immune Sera Molecular Weight Peptide Hydrolases/analysis Rabbits Serotyping Streptococcus mutans/immunology
Chemicals
Amino Acids Antigens, Bacterial Immune Sera Peptide Hydrolases
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Russell M W
Bergmeier L A
Zanders E D
Lehner T
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22 references, click to expand
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Article Info
Journal
Infection and immunity
Abbr.
Infect Immun
ISSN
0019-9567
Published
1980-05-00
Pages
486-93
Language
English
Region
United States
NLM ID
0246127
PMCID
PMC550961
Subset
IM
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