{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,3]],"date-time":"2026-05-03T12:22:16Z","timestamp":1777810936949,"version":"3.51.4"},"reference-count":37,"publisher":"SAGE Publications","issue":"6","license":[{"start":{"date-parts":[[1999,6,1]],"date-time":"1999-06-01T00:00:00Z","timestamp":928195200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.sagepub.com\/page\/policies\/text-and-data-mining-license"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["J Dent Res"],"published-print":{"date-parts":[[1999,6]]},"abstract":"<jats:p>Adherence of Actinomyces naeslundii ATCC 12104 to hydroxyapatite beads coated with protein fractions of parotid saliva, obtained by gel filtration on S-200 HR columns, showed GalNAc\u03b21-3Gal\u03b1-O-ethyl-inhibitable binding to high-molecular-weight proteins (Stromberg et al., 1992). The present study investigates the nature of these high-molecular-weight binding proteins and determines their specific ability to mediate adherence to representative strains of Actinomyces species. Strain ATCC 12104 bound specifically in a lactoseinhibitable manner to the heavy chain of secretory immunoglobulin A (S-IgA), contained within a high-molecular-weight parotid protein fraction separated on SDS-PAGE and transferred to a solid membrane support. Lactoseinhibitable binding to the heavy chain of S-IgA from human colostrum was also demonstrated. Peanut agglutinin bound to the heavy chain of parotid and colostrum S-IgAs contained on solid support membranes, confirming the presence of Gal\u03b21-3GalNAc residues on these molecules. Both salivary and colostrum S-IgA aggregated with strain ATCC 12104 in a GalNAc\u03b21-3Gal\u03b1-O-ethyl-inhibitable fashion. Further separation of high-molecular-weight salivary proteins on S-500 HR columns showed GalNAc\u03b21-3Gal\u03b1-O-ethyl-inhibitable binding to both mucin- and S-IgA-containing fractions. The presence of S-IgA in salivary pellicles formed in vivo on teeth was demonstrated by Western blot analysis of pellicle extracts with anti-IgA antibodies. Among strains representing A. naeslundii genospecies 1 and 2 and A. odontolyticus, only those of genospecies 1 with a particular adherence profile showed efficient GalNAc\u03b21-3Gal\u03b1-O-ethyl-inhibitable binding to S-IgA. Thus, oligosaccharides on S-IgA may promote bacterial aggregation (or adherence) and provide a mechanism by which S-IgA can interact with bacteria without prior immunological challenge.<\/jats:p>","DOI":"10.1177\/00220345990780060701","type":"journal-article","created":{"date-parts":[[2009,1,8]],"date-time":"2009-01-08T19:39:42Z","timestamp":1231443582000},"page":"1238-1244","source":"Crossref","is-referenced-by-count":7,"title":["Secretory Immunoglobulin A Heavy Chain Presents Gal\u03b21-3GalNAc Binding Structures for Actinomyces naeslundii genospecies 1"],"prefix":"10.1177","volume":"78","author":[{"given":"P.","family":"Bratt","sequence":"first","affiliation":[{"name":"Department of Cariology, Umea University, S-901 87 Umea, Sweden"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"D.","family":"Boren","sequence":"additional","affiliation":[{"name":"Department of Cariology, Umea University, S-901 87 Umea, Sweden"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"T.","family":"Boren","sequence":"additional","affiliation":[{"name":"Department of Cariology, Umea University, S-901 87 Umea, Sweden"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"N.","family":"Stromberg","sequence":"additional","affiliation":[{"name":"Department of Cariology, Umea University, S-901 87 Umea, Sweden"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"179","published-online":{"date-parts":[[1999,6,1]]},"reference":[{"key":"atypb1","doi-asserted-by":"crossref","first-page":"7260","DOI":"10.1016\/S0021-9258(19)42100-5","volume":"249","author":"Baenziger J.","year":"1974","journal-title":"J Biol Chem"},{"key":"atypb2","doi-asserted-by":"publisher","DOI":"10.1016\/S0021-9258(19)42101-7"},{"key":"atypb3","doi-asserted-by":"publisher","DOI":"10.1126\/science.8018146"},{"key":"atypb4","doi-asserted-by":"publisher","DOI":"10.1128\/IAI.52.3.840-845.1986"},{"key":"atypb5","doi-asserted-by":"publisher","DOI":"10.1177\/00220345980770011301"},{"key":"atypb6","unstructured":"Cisar JO (1986). 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