Journal article
Multiple glucan-binding proteins of Streptococcus sobrinus
Journal of bacteriology, Vol.178(6), pp.1572-1577
03/1996
DOI: 10.1128/jb.178.6.1572-1577.1996
PMCID: PMC177840
PMID: 8626283
Abstract
Several proteins from culture supernatants of Streptococcus sobrinus were able to bind avidly to Sephadex G-75. The proteins could be partially eluted from the Sephadex by low-molecular-weight alpha-1,6 glucan or fully eluted by 4 M guanidine hydrochloride. Elution profiles were complex, yielding proteins of 16, 45, 58 to 60, 90, 135, and 145 kDa, showing that the wild-type strain possessed multiple glucan-binding proteins. Two mutants of Streptococcus sobrinus incapable of aggregation by high-molecular-weight alpha-1,6 glucan were isolated. One mutant was spontaneous, from a cell suspension to which glucan had been added, whereas the other was induced by ethyl methanesulfonate. Both mutants were devoid of a 60-kDa protein, as shown by gel electrophoresis of culture supernatants and whole cells. Amino acid analysis showed that the 58- to 60-kDa protein and the 90-kDa protein were distinct, although both were N-terminally blocked. Both mutants retained their ability to adhere to glass in the presence of sucrose and to ferment mannitol and sorbitol. Both mutants retained their glucosytransferase activities, as shown by activity gels. Western blots (immunoblots), employing antibody against a glucan-binding protein of Streptococcus mutans, failed to reveal cross-reactivity with S. sobrinus proteins. The results show that even though S. sobrinus produces several proteins capable of binding alpha-1,6 glucans, the 60-kDa protein is probably the lectin needed for glucan-dependent cellular aggregation.
Details
- Title: Subtitle
- Multiple glucan-binding proteins of Streptococcus sobrinus
- Creators
- Y Ma - Department of Microbiology and Immunology, Academic Health Center, University of Louisville, Kentucky 40292, USAM O LassiterJ A BanasM Y GalperínK G TaylorR J Doyle
- Resource Type
- Journal article
- Publication Details
- Journal of bacteriology, Vol.178(6), pp.1572-1577
- DOI
- 10.1128/jb.178.6.1572-1577.1996
- PMID
- 8626283
- PMCID
- PMC177840
- NLM abbreviation
- J Bacteriol
- ISSN
- 0021-9193
- eISSN
- 1098-5530
- Publisher
- United States
- Grant note
- DE-05102 / NIDCR NIH HHS DE-10058 / NIDCR NIH HHS DE-07199 / NIDCR NIH HHS
- Language
- English
- Date published
- 03/1996
- Academic Unit
- Pediatric Dentistry; Dental Research
- Record Identifier
- 9984066085702771
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