Immunisation With a Purified Protein From Streptococcus Mutans Against Dental Caries in Rhesus Monkeys

Lehner, Thomas; Russell, Michael W.; Caldwell, J. D.

doi:10.1016/s0140-6736(80)91437-3

Cited by 77 publications

(53 citation statements)

References 18 publications

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“…SpaA is highly immunogenic in rabbits, mice, and monkeys (46,56). Found among serotypes a, c, d, e, f, g, and h of S. mutans but not in b (34,51,57,60), its widespread occurrence suggests that SpaA may serve an important function for bacteria in the S. mutans group.…”

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confidence: 99%

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Regions of the Streptococcus sobrinus spaA gene encoding major determinants of antigen I

1990

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Surface protein antigen A (SpaA), also called antigen B, antigen I/II, or antigen P1, is an abundant cell envelope protein that is the major antigenic determinant of Streptococcus sobrinus and other members of the Streptococcus mutans group of cariogenic bacteria. This laboratory has previously reported the cloning and expression in Escherichia coli of a BamHI restriction fragment of S. sobrinus DNA containing most of the spaA gene (pYA726) and encoding antigen I. Regions of spaA encoding immunodeterminants of antigen I were analyzed by either deletion mapping or expressing selected restriction fragments from the trc promoter. SpaA proteins produced by mutants harboring nested deletions, constructed by BAL 31 exonuclease treatment at a unique SstI site located towards the 3' end of the gene, were examined by Western immunoblot with rabbit serum against SpaA from S. sobrinus. Only SpaA polypeptides larger than 56 kilodaltons reacted with anti-SpaA serum. Various restriction fragments of the region of spaA encoding the antigenic determinants were cloned into an expression vector. The immunoreactive properties of the polypeptides encoded by those fragments indicated that expression of the immunodominant determinant required topographically assembled residues specified by noncontiguous regions located within 0.48-kilobase PvuH-to-SstI and 1.2-kilobase SstI-to-HindHI fragments which were adjacent on the spaA map.

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confidence: 99%

“…From a practical perspective, the high immunogenicity of SpaA and its ubiquity among the S. mutans group of bacteria make this protein an attractive candidate for the development of vaccines against S. mutans-induced dental caries (19,20,46). SpaA can induce protective immunity against dental caries in monkeys (46).…”

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confidence: 99%

Regions of the Streptococcus sobrinus spaA gene encoding major determinants of antigen I

1990

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“…Immunization with protein antigen I or I/II (17,29) or antigen A or B (33) significantly reduces dental caries in monkeys. These results suggest that our PAg may be useful for an effective vaccine in experimental dental caries.…”

Section: Resultsmentioning

confidence: 99%

“…185,000 and are physico-chemically and serologically indistinguishable. It has been shown that immunization with antigen I/II, I, or II, and antigen A or B results in a significant reduction of experimental dental caries in monkeys (17,18,33). Protein antigens of serotypes e and f S. mutans have been demonstrated to be serologically identical, with the antigen of the serotype c organism (32).…”

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Purification and Immunochemical Properties of a Protein Antigen from Serotype g Streptococcus mutans

Okahashi

Kinoshita

Hamada

1986

Microbiology and Immunology

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“…S. mutans produces a surface-protein antigen, which has a molecular mass of 190 kDa which has been previously designated to antigen I/II [4], B [5], P1 [6], or PAc [3]. The protein interacts with salivary components including lysozyme [7,8], amylase and proline-rich proteins of 18 000 and 38 000 Da [7] and is an antigen candidate inducing inhibitory antibodies against dental caries [9,10]. The antibodies have been reported as effective in the passive immunization against dental caries [11±13].…”

Section: Introductionmentioning

confidence: 99%

Inhibitory Effects of MoAbs against a Surface Protein Antigen in Real‐Time Adherence In vitro and Recolonization In vivo of Streptococcus mutans

et al. 2001

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A surface protein antigen (PAc) of Streptococcus mutans, particularly the A-region of the molecule, has been reported to interact with salivary components on the tooth surface. It might be a candidate antigen inducing the production of antibodies against the adherence of S. mutans to the tooth surface. We investigated the effects of monoclonal antibodies (MoAbs) obtained by immunization of synthetic PAc peptides that completely correspond to the amino acid sequence of part of the A-region. These MoAbs recognize several core B-cell epitopes in the sequence. Two (KH5 and SH2) of these antibodies reacted with both S. mutans and Streptococcus sobrinus, but not with Streptococcus sanguis, Streptococcus salivarius, Porphyromonas gingivalis or Lactobacillus casei. They clearly inhibited the real-time adherence of S. mutans to salivary components in a biosensor. KH5, which showed a real-time inhibition (71%), also significantly prevented the recolonization of S. mutans on the tooth surface in rats. These results suggested that the core B-cell epitope (-Y---L--Y----) recognized by KH5 was the essential sequence in the antigenic epitopes of PAc protein recognized specifically by the inhibitory antibody. Therefore, the amino acid residues were found to be important in the initial attachment of S. mutans to the tooth surface. These results provide for the mechanism of PAc molecule in the initial attachment of S. mutans on the tooth surface and more effective designs for the removal of S. mutans and S. sobrinus from the oral cavity.

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Immunisation With a Purified Protein From Streptococcus Mutans Against Dental Caries in Rhesus Monkeys

Cited by 77 publications

References 18 publications

Regions of the Streptococcus sobrinus spaA gene encoding major determinants of antigen I

Regions of the Streptococcus sobrinus spaA gene encoding major determinants of antigen I

Purification and Immunochemical Properties of a Protein Antigen from Serotype g Streptococcus mutans

Inhibitory Effects of MoAbs against a Surface Protein Antigen in Real‐Time Adherence In vitro and Recolonization In vivo of Streptococcus mutans

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