1887

Abstract

Interbacterial binding is considered an important colonization mechanism for many of the organisms that inhabit dental plaque. , a periodontal pathogen, can adhere to species that comprise early plaque, such as . In this study, the molecules of G9B that mediate binding to were investigated. Biotinylated surface molecules of were extracted and mixed with cells. Interactive streptococcal components were identified by SDS-PAGE of the cells followed by electroblotting, and visualization of the adsorbed streptococcal molecules with streptavidin-alkaline phosphatase. molecules of 45 kDa and a doublet of 62/60 kDa were observed to bind to . Polyclonal antibodies raised to the 62/60 kDa proteins inhibited the binding interaction. These antibodies demonstrated an antigenic relationship between the 62/60 kDa molecules and the 45 kDa protein. Both molecules were also antigenically related to, and may be breakdown products of, a larger molecule of 170 kDa which is antigenically related to the P1 antigen of . Cloning and expression in of the gene for the P1-like molecule from M5 resulted in a phenotype that expressed the 62/60 kDa and 45 kDa antigens and was capable of binding to . These results suggest that a P1-like molecule in is involved in adherence to . Processing of the P1-like molecule into smaller fragments of 62/60 kDa and 45 kDa may be required for binding activity.

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/content/journal/micro/10.1099/00221287-140-4-867
1994-04-01
2019-12-10
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http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-140-4-867
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