NDLI: Functional and Immunogenic Characterization of Two Cloned Regions of Streptococcus mutans Glucosyltransferase I

Content Provider	PubMed Central
Author	Christina, Jespersgaard George, Hajishengallis Greenway, Terrence E. Smith, Daniel J. Russell, Michael W. Michalek, Suzanne M.
Editor	Burns, D. L.
Copyright Year	1999
Abstract	Glucosyltransferase (GTF) enzymes of mutans streptococci are considered virulence factors due to their ability to synthesize adhesive glucans, which facilitate cell-to-cell adherence and accumulation. In this study we report the cloning, expression, and characterization of the catalytic (CAT) and glucan-binding (GLU) domains of S. mutans GTF-I encoded by gtfB. The CAT and GLU polypeptides represent amino acid residues 253 to 628 and 1183 to 1473, respectively, of S. mutans GTF-I. Antibodies to recombinant CAT and GLU were generated in rabbits and purified by affinity chromatography. Purified anti-CAT antibodies significantly inhibited water-insoluble glucan synthesis by S. mutans and S. sobrinus GTFs (P < 0.0001 and P < 0.05, respectively). The purified anti-GLU antibodies significantly inhibited both water-insoluble and water-soluble glucan synthesis by S. mutans GTFs (P < 0.0001 and P < 0.05, respectively). These results demonstrate that anti-CAT and anti-GLU antibodies are capable of inhibiting a variety of GTF activities. Since antibodies to S. mutans in saliva are implicated in protection against disease, we next assessed the ability of CAT and GLU polypeptides to induce mucosal antibody responses in mice. Intranasal (i.n.) immunization of mice with CAT showed significantly (P < 0.005) elevated levels of specific immunoglobulin G (IgG) antibody activity in serum and specific IgA antibody activity in serum, saliva, vaginal washes, and fecal samples. GLU immunized animals showed significantly (P < 0.005) elevated levels of specific IgA antibody activity in serum and vaginal secretions. Taken together, these results demonstrate that the recombinant CAT and GLU polypeptides are effective in inducing both mucosal and systemic immune responses. The ability of these polypeptides to induce a mucosal IgA immune response in mice after i.n. immunization supports their use as subunit vaccine candidates in the development of an anticaries vaccine.
Starting Page	810
File Format	PDF
ISSN	10985522
e-ISSN	10985522
Journal	Infection and Immunity
Issue Number	2
Volume Number	67
Language	English
Publisher	American Society for Microbiology
Publisher Date	1999-02-01
Access Restriction	Open
Rights Holder	American Society for Microbiology
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Infectious Diseases Parasitology Immunology Microbiology

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Mapping of a cloned glucosyltransferase gene in Streptococcus mutans.

Characterization of glucosyltransferase-deficient, plasmid-containing mutants of Streptococcus mutans LM-7.

Characterization of the Streptococcus mutans plasmid pva318 cloned into Escherichia coli.

Glucosyltransferase gene polymorphism among Streptococcus mutans strains.

Pyridine analogs inhibit the glucosyltransferase of Streptococcus mutans.

Antigenic relatedness of glucosyltransferase enzymes from streptococcus mutans.

Molecular cloning and characterization of the glucosyltransferase C gene (gtfC) from Streptococcus mutans LM7.

Characterization of an anti-glucosyltransferase serum specific for insoluble glucan synthesis by Streptococcus mutans.

Identification and Characterization of a Nonimmunoglobulin Factor in Human Saliva That Inhibits Streptococcus mutans Glucosyltransferase

Functional and Immunogenic Characterization of Two Cloned Regions of Streptococcus mutans Glucosyltransferase I

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