TITLE

Secretory Immunoglobulin A Heavy Chain Presents Ga1β1-3Ga1NAc Binding Structures For Actinomyces naeslundii genospecies 1

AUTHOR(S)
Bratt, P.; Borén, D.; Borén, T.; Stromberg, N.
PUB. DATE
June 1999
SOURCE
Journal of Dental Research;Jun1999, Vol. 78 Issue 6, p1238
SOURCE TYPE
Academic Journal
DOC. TYPE
Article
ABSTRACT
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 Ga1NAcβ1-3Ga1α-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 Ga1β1-3Ga1NAc residues on these molecules. Both salivary and colostrum S-IgA aggregated with strain ATCC 12104 in a Ga1NAcβ-3Ga1α-O-ethyl-inhibitable fashion. Further separation of high-molecular-weight salivary proteins on S-500 HR columns showed Ga1NAcβ-3Ga1α-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 Ga1NAcβ-3Ga1α-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.
ACCESSION #
36489429

 

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