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

A. M. Edwards, T. J. Grossman, J. D. Rudney

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21 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)217-224
Number of pages8
JournalOral Microbiology and Immunology
Volume22
Issue number4
DOIs
StatePublished - Aug 2007

Keywords

  • Autotransporter
  • Coaggregation
  • Fusobacterium nucleatum
  • Immunoglobulin binding
  • Streptococcus cristatus

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