title: Inhibition of Enterococcus faecium adherence to collagen by antibodies against high-affinity binding subdomains of Acm.
abstract: 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.
authors: Division of Infectious Diseases, Department of Internal Medicine, University of Texas Medical School at Houston, 6431 Fannin Street, MSB 2.112, Houston, TX 77030, USA.
authors: Sreedhar R
authors: SR
authors: Nallapareddy
authors: Jouko
authors: J
authors: Sillanpää
authors: Vannakambadi K
authors: VK
authors: Ganesh
authors: Magnus
authors: M
authors: Höök
authors: Barbara E
authors: BE
authors: Murray
mesh_terms: D018829:Adhesins, Bacterial / Q000276:immunology*; D000907:Antibodies, Bacterial / Q000276:immunology / Q000494:pharmacology*; D001422:Bacterial Adhesion / Q000187:drug effects*; D003094:Collagen / Q000378:metabolism*; D016984:Enterococcus faecium / Q000276:immunology / Q000378:metabolism*
chemical_list: C473793:Acm protein, Enterococcus faecium; D018829:Adhesins, Bacterial; D000907:Antibodies, Bacterial; D003094:Collagen