Identification of monoclonal antibody-binding domains within antigen P1 of Streptococcus mutans and cross-reactivity with related surface antigens of oral streptococci.
AUTOR(ES)
Brady, L J
RESUMO
Eleven monoclonal antibodies (MAbs) specific for P1, the major protein surface antigen of Streptococcus mutans serotype c, were characterized by Western blot (immunoblot) analysis and by radioimmunoassay using whole bacterial cells. The approximate binding domains of the MAbs were determined by using full-length and truncated P1 polypeptides. The accessibility of these binding sites on the surfaces of intact bacteria was determined by radioimmunoassay. The ability of each MAb to cross-react with related proteins from strains of S. mutans serotypes e and f, S. sanguis, and S. sobrinus serotype g is also reported.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=259059Documentos Relacionados
- Cross-reactivity of Streptococcus mutans antigens and human heart tissue.
- Characterization of serological cross-reactivity between polysaccharide antigens of Streptococcus mutans serotypes c and d.
- Specificity and Cross-Reactivity of Plasmodium falciparum Variant Surface Antigen-Specific Antibody Responses
- Cross-reactivity between the immunodominant determinant of the antigen I component of Streptococcus sobrinus SpaA protein and surface antigens from other members of the Streptococcus mutans group.
- Identification of a salivary agglutinin-binding domain within cell surface adhesin P1 of Streptococcus mutans.