ArticleBMC microbiology2009
Identification of salivary mucin MUC7 binding proteins from Streptococcus gordonii.
Article in BMC microbiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 56 citations in OpenAlex.
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- Role of Salivary Biomarkers in Diagnosis and Detection of Dental Caries: A Systematic Review.Diagnostics (Basel, Switzerland) · 2022Review
- Enolase ofFrontiers in microbiology · 2022Article
- Assembly and organization of the N-terminal region of mucin MUC5AC: Indications for structural and functional distinction from MUC5B.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- FBPAII and rpoBC, the Two Novel Secreted Proteins Identified by the Proteomic Approach from a Comparative Study between Antibiotic-Sensitive and Antibiotic-Resistant Helicobacter pylori-Associated Gastritis Strains.Infection and immunity · 2021Article
- A journey through thePeerJ · 2021Article
- Deciphering Additional Roles for the EF-Tu, l-Asparaginase II and OmpT Proteins of Shiga Toxin-ProducingMicroorganisms · 2020Article
- Bacterial bug-out bags: outer membrane vesicles and their proteins and functions.Journal of microbiology (Seoul, Korea) · 2020Review
- An enzyme in the test tube, and a transcription factor in the cell: Moonlighting proteins and cellular factors that affect their behavior.Protein science : a publication of the Protein Society · 2019Review
- Exploring the Potential Role of Moonlighting Function of the Surface-Associated Proteins FromFrontiers in immunology · 2019Article
- The Diverse Functional Roles of Elongation Factor Tu (EF-Tu) in Microbial Pathogenesis.Frontiers in microbiology · 2019Review
- Protein moonlighting: what is it, and why is it important?Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018Review
- Intracellular proteins moonlighting as bacterial adhesion factors.AIMS microbiology · 2018Review
- Laminin-111-derived peptide conjugated fibrin hydrogel restores salivary gland function.PloS one · 2017Article
- Low-dose irradiation affects the functional behavior of oral microbiota in the context of mucositis.Experimental biology and medicine (Maywood, N.J.) · 2016Article
- Article
- Salivary mucins in host defense and disease prevention.Journal of oral microbiology · 2015Article
Corrections and comments
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Authors and funding
5 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe 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.
resultsWe 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.
conclusionOur data demonstrated that S. gordonii expressed a number of putative MUC7 recognizing proteins and these contribute to MUC7 mucin binding of this streptococcal strain.
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