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A family of fibrinogen-binding MSCRAMMs from Enterococcus faecalis

¹ UT Medical School, Houston;
² Texas A&M Health Science Center

ABSTRACT

We report that three (EF0089, EF2505 and EF1896, renamed here Fss1, Fss2 and Fss3, respectively, for E. faecalis surface protein) of the recently predicted MSCRAMMs in Enterococcus faecalis strain V583 bind fibrinogen. Despite an absence of extensive primary sequence homology, the three proteins appear to be structurally related. Within the N-terminal regions of the three enterococcal proteins, we identified pairs of putative IgG-like modules with a high degree of predicted structural similarity to the fibrinogen-binding N2 and N3 domains of the staphylococcal MSCRAMMs ClfA and SdrG. A second N2N3-like segment was predicted in Fss1. Far-UV circular dichroism spectroscopy revealed that all four predicted N2N3-like regions are mainly composed of β-sheets with only a minor proportion of -helices, which is characteristic of immunoglobulin folded domains. Three of the four identified enterococcal N2N3-like regions showed potent dose-dependent binding to fibrinogen. However, the specificity of the fibrinogen-binding MSCRAMMs differs as indicated by far-Western blots which showed that recombinant segments of the MSCRAMMs bound different fibrinogen polypeptide chains. Enterococci, grown in serum-supplemented broth, adhere to fibrinogen-coated surfaces and inactivation in strain OG1RF of the gene encoding Fss2 resulted in reduced adherence, while complementation of the mutant restored full fibrinogen adherence. Thus, E. faecalis contains a family of MSCRAMMs that structurally and functionally resembles the fibrinogen-binding MSCRAMMs of staphylococci.

³ E-mail: mhook{at}ibt.tamhsc.edu

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