Association of a high-molecular weight arginine-binding protein of Fusobacterium nucleatum ATCC 10953 with adhesion to secretory immunoglobulin A and coaggregation with Streptococcus cristatus

被引:26
作者
Edwards, A. M. [1 ]
Grossman, T. J. [1 ]
Rudney, J. D. [1 ]
机构
[1] Univ Minnesota, Sch Dent, Dept Diagnost & Biol Sci, Minneapolis, MN 55455 USA
来源
ORAL MICROBIOLOGY AND IMMUNOLOGY | 2007年 / 22卷 / 04期
关键词
autotransporter; coaggregation; Fusobacterium nucleatum; immunoglobulin binding; Streptococcus cristatus; ORAL MICROBIAL COMMUNITIES; HUMAN EPITHELIAL-CELLS; PORPHYROMONAS-GINGIVALIS; ACTINOBACILLUS-ACTINOMYCETEMCOMITANS; AUTOTRANSPORTER PROTEINS; HUMAN-ERYTHROCYTES; GENETIC SYSTEMS; BUCCAL CELLS; IDENTIFICATION; BACTERIA;
D O I
10.1111/j.1399-302X.2006.00343.x
中图分类号
R78 [口腔科学];
学科分类号
1003 ;
摘要
Introduction: Fusobacterium nucleatum coaggregates with a diverse range of bacterial species, and binds to host tissues and proteins such as immunoglobulin. These interactions may support the attachment of a variety of organisms to oral surfaces and can facilitate the invasion of soft tissues. We hypothesized that coaggregation with streptococci and immunoglobulin binding may occur by a common adhesin sensitive to L-arginine. Methods: Repeated mixing of F. nucleatum with non-immune secretory immunoglobulin A (S-IgA) and recovery of non-agglutinating cells isolated a spontaneous mutant (isolate 21) of F. nucleatum that was defective in S-IgA binding. Wild-type and mutant F. nucleatum were compared by coaggregation and adhesion assays. Results: Isolate 21 exhibited significantly reduced S-IgA binding and coaggregation with oral streptococci but not with Porphyromonas gingivalis. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed that the mutant was deficient compared to wild-type for a single protein of approximately 360 kilodaltons. The corresponding protein was isolated from wild-type F. nucleatum protein preparations by coprecipitation with arginine-agarose beads. This protein was able to bind both Streptococcus cristatus and S-IgA. Mass spectrometry analysis indicated that this protein was closely related to putative autotransporter proteins in other F. nucleatum strains and was a 100% match to the deduced amino acid sequence of a 10,638-base-pair open reading frame in the incomplete genome sequence of F. nucleatum ATCC 10953. Peptides identified by MS-MS analysis spanned most of the predicted amino acid sequence, suggesting that the mature protein is not subject to postsecretory cleavage. Conclusion: Coaggregation represents a novel function within the autotransporter class of proteins, which are often associated with virulence.
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收藏
页码:217 / 224
页数:8
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