Identification of salivary mucin MUC7 binding proteins from <it>Streptococcus gordonii</it>
<p>Abstract</p> <p>Background</p> <p>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 betwee...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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BMC
2009-08-01
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| Series: | BMC Microbiology |
| Online Access: | http://www.biomedcentral.com/1471-2180/9/163 |
| _version_ | 1818760325328011264 |
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| author | Thornton David J Mehrotra Ravi Kiliç Nedret Kesimer Mehmet Sheehan John K |
| author_facet | Thornton David J Mehrotra Ravi Kiliç Nedret Kesimer Mehmet Sheehan John K |
| author_sort | Thornton David J |
| collection | DOAJ |
| description | <p>Abstract</p> <p>Background</p> <p>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.</p> <p>Results</p> <p>We demonstrate here, using purified MUC7 to overlay blots of SDS-extracts of <it>Streptococcus gordonii </it>cell surface proteins, 4 MUC7-binding bands, with apparent molecular masses of 62, 78, 84 and 133 kDa from the <it>Streptococcus gordonii </it>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 <it>hppA </it>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.</p> <p>Conclusion</p> <p>Our data demonstrated that <it>S. gordonii </it>expressed a number of putative MUC7 recognizing proteins and these contribute to MUC7 mucin binding of this streptococcal strain.</p> |
| first_indexed | 2024-12-18T06:56:49Z |
| format | Article |
| id | doaj.art-14df22b221db4df193b864a53b511110 |
| institution | Directory Open Access Journal |
| issn | 1471-2180 |
| language | English |
| last_indexed | 2024-12-18T06:56:49Z |
| publishDate | 2009-08-01 |
| publisher | BMC |
| record_format | Article |
| series | BMC Microbiology |
| spelling | doaj.art-14df22b221db4df193b864a53b5111102022-12-21T21:17:10ZengBMCBMC Microbiology1471-21802009-08-019116310.1186/1471-2180-9-163Identification of salivary mucin MUC7 binding proteins from <it>Streptococcus gordonii</it>Thornton David JMehrotra RaviKiliç NedretKesimer MehmetSheehan John K<p>Abstract</p> <p>Background</p> <p>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.</p> <p>Results</p> <p>We demonstrate here, using purified MUC7 to overlay blots of SDS-extracts of <it>Streptococcus gordonii </it>cell surface proteins, 4 MUC7-binding bands, with apparent molecular masses of 62, 78, 84 and 133 kDa from the <it>Streptococcus gordonii </it>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 <it>hppA </it>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.</p> <p>Conclusion</p> <p>Our data demonstrated that <it>S. gordonii </it>expressed a number of putative MUC7 recognizing proteins and these contribute to MUC7 mucin binding of this streptococcal strain.</p>http://www.biomedcentral.com/1471-2180/9/163 |
| spellingShingle | Thornton David J Mehrotra Ravi Kiliç Nedret Kesimer Mehmet Sheehan John K Identification of salivary mucin MUC7 binding proteins from <it>Streptococcus gordonii</it> BMC Microbiology |
| title | Identification of salivary mucin MUC7 binding proteins from <it>Streptococcus gordonii</it> |
| title_full | Identification of salivary mucin MUC7 binding proteins from <it>Streptococcus gordonii</it> |
| title_fullStr | Identification of salivary mucin MUC7 binding proteins from <it>Streptococcus gordonii</it> |
| title_full_unstemmed | Identification of salivary mucin MUC7 binding proteins from <it>Streptococcus gordonii</it> |
| title_short | Identification of salivary mucin MUC7 binding proteins from <it>Streptococcus gordonii</it> |
| title_sort | identification of salivary mucin muc7 binding proteins from it streptococcus gordonii it |
| url | http://www.biomedcentral.com/1471-2180/9/163 |
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