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An interesting example is the opportunistic respiratory pathogen <jats:italic>Streptococcus pneumoniae<\/jats:italic> that normally resides in the nasopharynx, but belongs to the greater Mitis group of streptococci, most of which colonize the oral cavity. <jats:italic>Streptococcus pneumoniae<\/jats:italic> also expresses a serine\u2010rich repeat (<jats:styled-content style=\"fixed-case\">SRR<\/jats:styled-content>) adhesin, PsrP, which is a homologue to oral Mitis group <jats:styled-content style=\"fixed-case\">SRR<\/jats:styled-content> adhesins, such as Hsa of <jats:italic>Streptococcus gordonii<\/jats:italic> and SrpA of <jats:italic>Streptococcus sanguinis<\/jats:italic>. As the latter bind to salivary glycoproteins through recognition of terminal sialic acids, we wanted to determine whether <jats:italic>S.\u00a0pneumoniae<\/jats:italic> also binds to salivary proteins through possibly the same mechanism. We found that only a capsule\u2010free mutant of <jats:italic>S.\u00a0pneumoniae <\/jats:italic><jats:styled-content style=\"fixed-case\">TIGR<\/jats:styled-content>4 binds to salivary proteins, most prominently to mucin <jats:styled-content style=\"fixed-case\">MUC<\/jats:styled-content>7, but that this binding was not mediated through PsrP or recognition of sialic acid. We also found, however, that PsrP is involved in agglutination of human red blood cells (<jats:styled-content style=\"fixed-case\">RBC<\/jats:styled-content>s). After removal of PsrP, an additional previously masked lectin\u2010like adhesin activity mediating agglutination of sialidase\u2010treated <jats:styled-content style=\"fixed-case\">RBC<\/jats:styled-content>s becomes revealed. Using a custom\u2010spotted glycoprotein and neoglycoprotein dot blot array, we identify candidate glycan motifs recognized by PsrP and by the putative <jats:italic>S.\u00a0pneumoniae<\/jats:italic> adhesin that could perhaps be responsible for pneumococcal binding to salivary <jats:styled-content style=\"fixed-case\">MUC<\/jats:styled-content>7 and glycoproteins on <jats:styled-content style=\"fixed-case\">RBC<\/jats:styled-content>s.<\/jats:p>","DOI":"10.1111\/omi.12113","type":"journal-article","created":{"date-parts":[[2015,7,14]],"date-time":"2015-07-14T13:15:52Z","timestamp":1436879752000},"page":"175-188","source":"Crossref","is-referenced-by-count":29,"title":["Absence of capsule reveals glycan\u2010mediated binding and recognition of salivary mucin MUC7 by <i>Streptococcus pneumoniae<\/i>"],"prefix":"10.1111","volume":"31","author":[{"given":"S.","family":"Thamadilok","sequence":"first","affiliation":[{"name":"Department of Oral Biology School of Dental Medicine University at Buffalo The State University of New York Buffalo NY USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"H.","family":"Roche\u2010H\u00e5kansson","sequence":"additional","affiliation":[{"name":"Department of Microbiology and Immunology School of Medicine and Biomedical Sciences University at Buffalo The State University of New York Buffalo NY USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"A.P.","family":"H\u00e5kansson","sequence":"additional","affiliation":[{"name":"Department of Microbiology and Immunology School of Medicine and Biomedical Sciences University at Buffalo The State University of New York Buffalo NY USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"S.","family":"Ruhl","sequence":"additional","affiliation":[{"name":"Department of Oral Biology School of Dental Medicine University at Buffalo The State University of New York Buffalo NY USA"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2015,8,17]]},"reference":[{"key":"e_1_2_6_2_1","doi-asserted-by":"publisher","DOI":"10.1084\/jem.158.2.559"},{"key":"e_1_2_6_3_1","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.66.4.1439-1444.1998"},{"key":"e_1_2_6_4_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M105448200"},{"key":"e_1_2_6_5_1","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.72.11.6528-6537.2004"},{"key":"e_1_2_6_6_1","doi-asserted-by":"publisher","DOI":"10.1128\/mBio.00745-13"},{"key":"e_1_2_6_7_1","doi-asserted-by":"publisher","DOI":"10.1006\/mpat.1994.1082"},{"key":"e_1_2_6_8_1","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.01125-09"},{"key":"e_1_2_6_9_1","doi-asserted-by":"publisher","DOI":"10.1371\/journal.ppat.1004540"},{"key":"e_1_2_6_10_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1365-2958.1994.tb01084.x"},{"key":"e_1_2_6_11_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1399-302X.1991.tb00466.x"},{"key":"e_1_2_6_12_1","unstructured":"Fukuda M.(2001)Chemical labeling of carbohydrates by oxidation and sodium borohydride reduction. 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