Abstract
M protein of group A streptococci was extracted by mild peptic digestion. Optimal amounts of type-specific M protein were released after 20 min of digestion with 0.02 mg of pepsin per ml at pH 5.8. Immunological analysis revealed that, unlike conventional HCl extracts, pepsin extracts lacked the surface C carbohydrate antigen and contained less non-type-specific, heat-stable cellular antigens; they also lacked detectable heat-labile T protein. Similar to HCl extracts, however, the pepsin-extracted M protein precipitated homologous-type M antisera and inhibited type-specific opsonization of homologous group A streptococci. Furthermore, the pepsin extract was capable of inducing type-specific opsonic M antibody in rabbits. This method may provide a useful initial step in the purification of M protein by reducing contaminating antigens.
MeSH Terms
Agglutination Tests
Animals
Antibody Specificity
Antigens, Bacterial/isolation & purification
Complement Fixation Tests
Epitopes
Hemagglutination Tests
Immune Sera
Immunization
Immunodiffusion
Methods
Opsonin Proteins/analysis
Pepsin A/pharmacology
Rabbits/immunology
Streptococcus pyogenes/immunology
Chemicals
Antigens, Bacterial
Epitopes
Immune Sera
Opsonin Proteins
Pepsin A
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Beachey E H
Campbell G L
Ofek I
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13 references, click to expand
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