Identification of salivary mucin MUC7 binding proteins from Streptococcus gordonii Public Deposited

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Creator
  • Kesimer, Mehmet
    • Affiliation: School of Medicine, Department of Biochemistry and Biophysics
    • Other Affiliation: Department of Biochemistry, Faculty of Medicine, University of Gazi, 06510 Besevler, Ankara, Turkey
  • Thornton, David J
    • Other Affiliation: Wellcome Trust Centre for Cell-Matrix Research, Faculty of Life Sciences, University of Manchester, Manchester, M13 9PT, UK
  • Mehrotra, Ravi
    • Other Affiliation: Wellcome Trust Centre for Cell-Matrix Research, Faculty of Life Sciences, University of Manchester, Manchester, M13 9PT, UK
  • Kiliç, Nedret
    • Other Affiliation: Department of Biochemistry, Faculty of Medicine, University of Gazi, 06510 Besevler, Ankara, Turkey
  • Sheehan, John K
    • Affiliation: School of Medicine, Department of Biochemistry and Biophysics
    • Other Affiliation: Wellcome Trust Centre for Cell-Matrix Research, Faculty of Life Sciences, University of Manchester, Manchester, M13 9PT, UK
Abstract
  • Abstract Background The salivary mucin MUC7 (previously known as MG2) can adhere to various strains of streptococci that are primary colonizers and predominant microorganisms of the oral cavity. Although there is a growing interest in interaction between oral pathogens and salivary mucins, studies reporting the specific binding sites on the bacteria are rather limited. Identification and characterization of the specific interacting proteins on the bacterial cell surface, termed adhesins, are crucial to further understand host-pathogen interactions. Results We demonstrate here, using purified MUC7 to overlay blots of SDS-extracts of Streptococcus gordonii cell surface proteins, 4 MUC7-binding bands, with apparent molecular masses of 62, 78, 84 and 133 kDa from the Streptococcus gordonii strain, PK488. Putative adhesins were identified by in-gel digestion and subsequent nanoLC-tandem mass spectrometry analysis of resultant peptides. The 62 kDa and 84 kDa bands were identified as elongation factor (EF) Tu and EF-G respectively. The 78 kDa band was a hppA gene product; the 74 kDa oligopeptide-binding lipoprotein. The 133 kDa band contained two proteins; alpha enolase and DNA-directed RNA polymerase, beta' subunit. Some of these proteins, for example alpha enolase are expected to be intracellular, however, flow cytometric analysis confirmed its location on the bacterial surface. Conclusion Our data demonstrated that S. gordonii expressed a number of putative MUC7 recognizing proteins and these contribute to MUC7 mucin binding of this streptococcal strain.
Date of publication
Identifier
  • 19671172
  • doi:10.1186/1471-2180-9-163
Resource type
  • Article
Rights statement
  • In Copyright
Rights holder
  • Mehmet Kesimer et al.; licensee BioMed Central Ltd.
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Journal title
  • BMC Microbiology
Journal volume
  • 9
Journal issue
  • 1
Page start
  • 163
Language
  • English
Is the article or chapter peer-reviewed?
  • Yes
ISSN
  • 1471-2180
Bibliographic citation
  • BMC Microbiology. 2009 Aug 11;9(1):163
Access
  • Open Access
Publisher
  • BioMed Central Ltd
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