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Infection and Immunity, September 2000, p. 5218-5224, Vol. 68, No. 9
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Enterococcus faecalis Adhesin, Ace, Mediates Attachment to Extracellular Matrix Proteins Collagen Type IV and Laminin as well as Collagen Type I

Sreedhar R. Nallapareddy,1,2 Xiang Qin,1,2,3 George M. Weinstock,2,3 Magnus Höök,3,4 and Barbara E. Murray1,2,3,*

Division of Infectious Diseases, Department of Internal Medicine,1 Center for the Study of Emerging and Re-emerging Pathogens,2 Department of Microbiology and Molecular Genetics,3 University of Texas Medical School, and Center for Extracellular Matrix Biology, Institute of Biosciences and Technology, Texas A&M University System Health Science Center,4 Houston, Texas 77030

Received 10 April 2000/Returned for modification 12 May 2000/Accepted 16 June 2000

Adhesin-mediated binding to extracellular matrix (ECM) proteins is thought to be a crucial step in the pathogenic process of many bacterial infections. We have previously reported conditional adherence of most Enterococcus faecalis isolates, after growth at 46°C, to ECM proteins collagen types I and IV and laminin; identified an E. faecalis-specific gene, ace, whose encoded protein has characteristics of a bacterial adhesin; and implicated Ace in binding to collagen type I. In this study, we constructed an ace disruption mutant from E. faecalis strain OG1RF that showed marked reduction in adherence to collagen types I and IV and laminin when compared to the parental OG1RF strain after growth at 46°C. Polyclonal immune serum raised against the OG1RF-derived recombinant Ace A domain reacted with a single ~105-kDa band of mutanolysin extracts from OG1RF grown at 46°C, while no band was detected in extracts from OG1RF grown at 37°C, nor from the OG1RF ace mutant grown at 37 or 46°C. IgGs purified from the anti-Ace A immune serum inhibited adherence of 46°C-grown E. faecalis OG1RF to immobilized collagen type IV and laminin as well as collagen type I, at a concentration as low as 1 µg/ml, and also inhibited the 46°C-evoked adherence of two clinical isolates tested. We also showed in vitro interaction of collagen type IV with Ace from OG1RF mutanolysin extracts on a far-Western blot. Binding of recombinant Ace A to immobilized collagen types I and IV and laminin was demonstrated in an enzyme-linked immunosorbent assay and was shown to be concentration dependent. These results indicate that Ace A mediates the conditional binding of E. faecalis OG1RF to collagen type IV and laminin in addition to collagen type I.

* Corresponding author. Mailing address: Center for the Study of Emerging and Re-emerging Pathogens, Division of Infectious Diseases, Department of Internal Medicine, University of Texas Medical School at Houston, 6431 Fannin St., Houston, TX 77030. Phone: (713) 500-6767. Fax: (713) 500-5495. E-mail: infdis{at}heart.med.uth.tmc.edu.

Infection and Immunity, September 2000, p. 5218-5224, Vol. 68, No. 9
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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