Linked Life Data

10371247

Source:http://linkedlifedata.com/resource/pubmed/id/10371247

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1999-6-29
pubmed:abstractText
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 GalNAcbeta1-3Galalpha-O-ethyl-inhibitable binding to high-molecular-weight proteins (Strömberg 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 lactose-inhibitable 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. Lactose-inhibitable 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 Galbeta1-3GalNAc residues on these molecules. Both salivary and colostrum S-IgA aggregated with strain ATCC 12104 in a GalNAcbeta1-3Galalpha-O-ethyl-inhibitable fashion. Further separation of high-molecular-weight salivary proteins on S-500 HR columns showed GalNAcbeta1-3Galalpha-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 GalNAcbeta1-3Galalpha-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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
D
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0022-0345
pubmed:author
pubmed:issnType
Print
pubmed:volume
78
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1238-44
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:10371247-Actinomyces, pubmed-meshheading:10371247-Antigens, Bacterial, pubmed-meshheading:10371247-Antigens, Tumor-Associated, Carbohydrate, pubmed-meshheading:10371247-Bacterial Adhesion, pubmed-meshheading:10371247-Blotting, Western, pubmed-meshheading:10371247-Colostrum, pubmed-meshheading:10371247-Dental Deposits, pubmed-meshheading:10371247-Dental Pellicle, pubmed-meshheading:10371247-Humans, pubmed-meshheading:10371247-Immunoglobulin A, Secretory, pubmed-meshheading:10371247-Immunoglobulin Heavy Chains, pubmed-meshheading:10371247-Isoantigens, pubmed-meshheading:10371247-Lactose, pubmed-meshheading:10371247-Molecular Weight, pubmed-meshheading:10371247-Mucins, pubmed-meshheading:10371247-Parotid Gland, pubmed-meshheading:10371247-Peanut Agglutinin, pubmed-meshheading:10371247-Protein Binding, pubmed-meshheading:10371247-Salivary Proteins and Peptides
pubmed:year
1999
pubmed:articleTitle
Secretory immunoglobulin A heavy chain presents Galbeta1-3GalNAc binding structures for Actinomyces naeslundii genospecies 1.
pubmed:affiliation
Department of Cariology, Umeå University, Sweden.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't