{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,22]],"date-time":"2026-06-22T23:49:57Z","timestamp":1782172197058,"version":"3.54.5"},"reference-count":48,"publisher":"American Society for Microbiology","issue":"15","license":[{"start":{"date-parts":[[2014,8,1]],"date-time":"2014-08-01T00:00:00Z","timestamp":1406851200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Bacteriol"],"published-print":{"date-parts":[[2014,8]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            Expression of the surface protein Cnm has been directly implicated in the ability of certain strains of\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Streptococcus mutans<\/jats:named-content>\n            to bind to collagen and to invade human coronary artery endothelial cells (HCAEC) and in the killing of\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Galleria mellonella<\/jats:named-content>\n            . Sequencing analysis of Cnm\n            <jats:sup>+<\/jats:sup>\n            strains revealed that\n            <jats:italic>cnm<\/jats:italic>\n            is located between the core genes SMU.2067 and SMU.2069. Reverse transcription-PCR (RT-PCR) analysis showed that\n            <jats:italic>cnm<\/jats:italic>\n            is cotranscribed with SMU.2067, encoding a putative glycosyltransferase referred to here as PgfS (\n            <jats:underline>p<\/jats:underline>\n            rotein\n            <jats:underline>g<\/jats:underline>\n            lycosyltrans\n            <jats:underline>f<\/jats:underline>\n            erase of\n            <jats:underline>s<\/jats:underline>\n            treptococci). Notably, Cnm contains a threonine-rich domain predicted to undergo\n            <jats:italic>O<\/jats:italic>\n            -linked glycosylation. The previously shown abnormal migration pattern of Cnm, the presence of the threonine-rich domain, and the molecular linkage of\n            <jats:italic>cnm<\/jats:italic>\n            with\n            <jats:italic>pgfS<\/jats:italic>\n            lead us to hypothesize that PgfS modifies Cnm. A \u0394\n            <jats:italic>pgfS<\/jats:italic>\n            strain showed defects in several traits associated with Cnm expression, including collagen binding, HCAEC invasion, and killing of\n            <jats:named-content xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">G. mellonella<\/jats:named-content>\n            . Western blot analysis revealed that Cnm from the \u0394\n            <jats:italic>pgfS<\/jats:italic>\n            mutant migrated at a lower molecular weight than that from the parent strain. In addition, Cnm produced by \u0394\n            <jats:italic>pgfS<\/jats:italic>\n            was highly susceptible to proteinase K degradation, in contrast to the high-molecular-weight Cnm version found in the parent strain. Lectin-binding analyses confirmed the glycosylated nature of Cnm and strongly suggested the presence of\n            <jats:italic>N<\/jats:italic>\n            -acetylglucosamine residues attached to Cnm. Based on these findings, the phenotypes observed in \u0394\n            <jats:italic>pgfS<\/jats:italic>\n            are most likely associated with defects in Cnm glycosylation that affects protein function, stability, or both. In conclusion, this study demonstrates that Cnm is a glycoprotein and that posttranslational modification mediated by PgfS contributes to the virulence-associated phenotypes linked to Cnm.\n          <\/jats:p>","DOI":"10.1128\/jb.01783-14","type":"journal-article","created":{"date-parts":[[2014,5,17]],"date-time":"2014-05-17T03:35:01Z","timestamp":1400297701000},"page":"2789-2797","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":42,"title":["Modification of Streptococcus mutans Cnm by PgfS Contributes to Adhesion, Endothelial Cell Invasion, and Virulence"],"prefix":"10.1128","volume":"196","author":[{"given":"Alejandro","family":"Avil\u00e9s-Reyes","sequence":"first","affiliation":[{"name":"Center for Oral Biology, University of Rochester School of Medicine and Dentistry, Rochester, New York, USA"},{"name":"Department of Microbiology and Immunology, University of Rochester School of Medicine and Dentistry, Rochester, New York, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"James H.","family":"Miller","sequence":"additional","affiliation":[{"name":"Center for Oral Biology, University of Rochester School of Medicine and Dentistry, Rochester, New York, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Patricia J.","family":"Simpson-Haidaris","sequence":"additional","affiliation":[{"name":"Department of Microbiology and Immunology, University of Rochester School of Medicine and Dentistry, Rochester, New York, USA"},{"name":"Department of Medicine\/Hematology-Oncology Division, University of Rochester School of Medicine and Dentistry, Rochester, New York, USA"},{"name":"Department of Pathology and Laboratory Medicine, University of Rochester School of Medicine and Dentistry, Rochester, New York, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Fred K.","family":"Hagen","sequence":"additional","affiliation":[{"name":"Department of Biochemistry and Biophysics, University of Rochester School of Medicine and Dentistry, Rochester, New York, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jacqueline","family":"Abranches","sequence":"additional","affiliation":[{"name":"Center for Oral Biology, University of Rochester School of Medicine and Dentistry, Rochester, New York, USA"},{"name":"Department of Microbiology and Immunology, University of Rochester School of Medicine and Dentistry, Rochester, New York, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jos\u00e9 A.","family":"Lemos","sequence":"additional","affiliation":[{"name":"Center for Oral Biology, University of Rochester School of Medicine and Dentistry, Rochester, New York, USA"},{"name":"Department of Microbiology and Immunology, University of Rochester School of Medicine and Dentistry, Rochester, New York, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_3_2_2","doi-asserted-by":"publisher","DOI":"10.1128\/mr.50.4.353-380.1986"},{"key":"e_1_3_3_3_2","doi-asserted-by":"publisher","DOI":"10.1159\/000324598"},{"key":"e_1_3_3_4_2","doi-asserted-by":"publisher","DOI":"10.1254\/jphs.09R24FM"},{"key":"e_1_3_3_5_2","doi-asserted-by":"publisher","DOI":"10.1128\/JCM.02343-06"},{"key":"e_1_3_3_6_2","doi-asserted-by":"publisher","DOI":"10.1099\/jmm.0.47051-0"},{"key":"e_1_3_3_7_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.jdsr.2007.09.001"},{"key":"e_1_3_3_8_2","doi-asserted-by":"publisher","DOI":"10.1038\/nrcardio.2011.43"},{"key":"e_1_3_3_9_2","doi-asserted-by":"publisher","DOI":"10.2741\/1305"},{"key":"e_1_3_3_10_2","first-page":"1","article-title":"Deaths: final data for 2008","volume":"59","author":"Minino AM","year":"2011","unstructured":"MininoAMMurphySLXuJKochanekKD. 2011. 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