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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{triangledown}

Sreedhar R. Nallapareddy,1,2 Jouko Sillanpää,1,2 Vannakambadi K. Ganesh,4 Magnus Höök,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, 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.

* Corresponding author. Mailing address: Division of Infectious Diseases, Department of Internal Medicine, University of Texas Medical School at Houston, 6431 Fannin Street, MSB 2.112, Houston, TX 77030. Phone: (713) 500-6745. Fax: (713) 500-6766. E-mail: bem.asst{at}uth.tmc.edu

{triangledown} Published ahead of print on 16 April 2007.

Editor: F. C. Fang

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.



This article has been cited by other articles:

  • Sillanpaa, J., Nallapareddy, S. R., Qin, X., Singh, K. V., Muzny, D. M., Kovar, C. L., Nazareth, L. V., Gibbs, R. A., Ferraro, M. J., Steckelberg, J. M., Weinstock, G. M., Murray, B. E. (2009). A Collagen-Binding Adhesin, Acb, and Ten Other Putative MSCRAMM and Pilus Family Proteins of Streptococcus gallolyticus subsp. gallolyticus (Streptococcus bovis Group, Biotype I). J. Bacteriol. 191: 6643-6653 [Abstract] [Full Text]  
  • Sillanpaa, J., Nallapareddy, S. R., Prakash, V. P., Qin, X., Hook, M., Weinstock, G. M., Murray, B. E. (2008). Identification and phenotypic characterization of a second collagen adhesin, Scm, and genome-based identification and analysis of 13 other predicted MSCRAMMs, including four distinct pilus loci, in Enterococcus faecium. Microbiology 154: 3199-3211 [Abstract] [Full Text]  
  • Nallapareddy, S. R., Singh, K. V., Okhuysen, P. C., Murray, B. E. (2008). A Functional Collagen Adhesin Gene, acm, in Clinical Isolates of Enterococcus faecium Correlates with the Recent Success of This Emerging Nosocomial Pathogen. Infect. Immun. 76: 4110-4119 [Abstract] [Full Text]  
  • Nallapareddy, S. R., Singh, K. V., Murray, B. E. (2008). Contribution of the Collagen Adhesin Acm to Pathogenesis of Enterococcus faecium in Experimental Endocarditis. Infect. Immun. 76: 4120-4128 [Abstract] [Full Text]  


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