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Infect Immun. 2015 Mar;83(3):1104-13. doi: 10.1128/IAI.02838-14. Epub 2015 Jan 5.

Fap2 of Fusobacterium nucleatum is a galactose-inhibitable adhesin involved in coaggregation, cell adhesion, and preterm birth.

Author information

1
Institute of Dental Sciences, The Hebrew University Hadassah School of Dental Medicine, Jerusalem, Israel.
2
Department of Periodontics, School of Dental Medicine, Case Western Reserve University, Cleveland, Ohio, USA.
3
Division of Periodontics, College of Dental Medicine, Columbia University Medical Center, New York, New York, USA Department of Microbiology & Immunology, Columbia University Medical Center, New York, New York, USA Herbert Irving Comprehensive Cancer Center, Columbia University Medical Center, New York, New York, USA ywh2@case.edu giladba@ekmd.huji.ac.il.
4
Institute of Dental Sciences, The Hebrew University Hadassah School of Dental Medicine, Jerusalem, Israel ywh2@case.edu giladba@ekmd.huji.ac.il.

Abstract

Fusobacterium nucleatum is a common oral anaerobe involved in periodontitis that is known to translocate and cause intrauterine infections. In the oral environment, F. nucleatum adheres to a large diversity of species, facilitating their colonization and creating biological bridges that stabilize the multispecies dental biofilm. Many of these interactions (called coadherences or coaggregations) are galactose sensitive. Galactose-sensitive interactions are also involved in the binding of F. nucleatum to host cells. Hemagglutination of some F. nucleatum strains is also galactose sensitive, suggesting that a single galactose-sensitive adhesin might mediate the interaction of fusobacteria with many partners and targets. In order to identify the fusobacterial galactose-sensitive adhesin, a system for transposon mutagenesis in fusobacteria was created. The mutant library was screened for hemagglutination deficiency, and three clones were isolated. All three clones were found to harbor the transposon in the gene coding for the Fap2 outer membrane autotransporter. The three fap2 mutants failed to show galactose-inhibitable coaggregation with Porphyromonas gingivalis and were defective in cell binding. A fap2 mutant also showed a 2-log reduction in murine placental colonization compared to that of the wild type. Our results suggest that Fap2 is a galactose-sensitive hemagglutinin and adhesin that is likely to play a role in the virulence of fusobacteria.

PMID:
25561710
PMCID:
PMC4333458
DOI:
10.1128/IAI.02838-14
[Indexed for MEDLINE]
Free PMC Article

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