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Infection and Immunity, June 2007, p. 3192-3196, Vol. 75, No. 6
0019-9567/07/$08.00+0     doi:10.1128/IAI.02016-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Inhibition of Enterococcus faecium Adherence to Collagen by Antibodies against High-Affinity Binding Subdomains of Acm

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, University of Texas Medical School,³ Center for Extracellular Matrix Biology, Institute of Biosciences and Technology, Texas A&M University Health Science Center, Houston, Texas 77030⁴

Received 22 December 2006/ Returned for modification 5 March 2007/ Accepted 3 April 2007

Strains of Enterococcus faecium express a cell wall-anchored protein, Acm, which mediates adherence to collagen. Here, we (i) identify the minimal and high-affinity binding subsegments of Acm and (ii) show that anti-Acm immunoglobulin Gs (IgGs) purified against these subsegments reduced E. faecium TX2535 strain collagen adherence up to 73 and 50%, respectively, significantly more than the total IgGs against the full-length Acm A domain (28%) (P < 0.0001). Blocking Acm adherence with functional subsegment-specific antibodies raises the possibility of their use as therapeutic or prophylactic agents.

Published ahead of print on 16 April 2007.

Editor: F. C. Fang

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