Inhibition of Enterococcus faecium adherence to collagen by antibodies against high-affinity binding subdomains of Acm. Academic Article

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

• Hook, Magnus

published proceedings

• Infect Immun

author list (cited authors)

• Nallapareddy, S. R., Sillanp, J., Ganesh, V. K., Hk, M., & Murray, B. E.

citation count

• 14

complete list of authors

• Nallapareddy, Sreedhar R||Sillanpää, Jouko||Ganesh, Vannakambadi K||Höök, Magnus||Murray, Barbara E

publication date

• June 2007

publisher

• American Society for Microbiology  Publisher

published in

• Infection and Immunity  Journal

keywords

• Adhesins, Bacterial
• Antibodies, Bacterial
• Bacterial Adhesion
• Collagen
• Enterococcus Faecium

Digital Object Identifier (DOI)

• 10.1128/IAI.02016-06

URI

• https://hdl.handle.net/1969.1/181812

start page

• 3192

end page

• 3196

volume

• 75

issue

• 6

URL

• http://dx.doi.org/10.1128/iai.02016-06