Impact of actin on adhesion and translocation of Enterococcus faecalis
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Original Paper
Impact of actin on adhesion and translocation of Enterococcus faecalis Zhen Peng · Viktoria Krey · Hua Wei · Qianglai Tan · Roger Vogelmann · Matthias A. Ehrmann · Rudi F. Vogel
Received: 15 April 2013 / Revised: 15 November 2013 / Accepted: 23 November 2013 / Published online: 21 December 2013 © Springer-Verlag Berlin Heidelberg 2013
Abstract This study focuses on the impact of actin on adhesion and translocation of Enterococcus (E.) faecalis OG1RF, E. faecalis Symbioflor®, and E. faecalis V583. Insight into the role of actin aggregation in the mediation of bacterial adhesion and translocation was provided by a two-chamber translocation assay, which employed Ptk6 cells. Determination of translocation rates, cytochalasin D treatment, and laser scanning confocal microscopic observation revealed actin as a predominant brace for enterococci to pass through the epithelial cell layer. As the three enterococci had moderate adhesion ability to actin, actin-binding proteins were isolated and characterized by LC–MS/MS. The isolated proteins were identified as pyruvate formate lyase, enolase, glyceraldehyde-3-phosphate dehydrogenase, and GroEL. All these proteins belong to two major groups of moonlighting proteins, i.e., proteins, which display additional functions other than their described major biochemical catalysis. Both groups of moonlight proteins were determined to be associated with epithelial cell binding.
Communicated by Wolfgang Bucek. Z. Peng · M. A. Ehrmann · R. F. Vogel (*) Lehrstuhl für Technische Mikrobiologie, Technische Universität München, Weihenstephaner Steig 16, 85350 Freising, Germany e-mail: [email protected] V. Krey Lehrstuhl für Mikrobielle Ökologie, Technische Universität München, Freising, Germany H. Wei · Q. Tan Nanchang University, Nanchang, China R. Vogelmann Second Department of Internal Medicine, Universitätsmedizin Mannheim, University Heidelberg, 68167 Mannheim, Germany
Keywords Enterococcus faecalis · Actin · Ptk6 cell monolayer · Adhesion · Translocation · Cytochalasin D
Introduction Enterococcus (E.) faecalis is well known as a common inhabitant in the human and animal large intestine and vagina and plays ambiguous roles in organismal health (Domann et al. 2007). Versatile and contradictory as it is, some E. faecalis strains (Symbioflor®, UGRA10) manifest beneficial activities such as the competitive exclusion of pathogens and potentiation of immunity, while some other E. faecalis strains (V583, MMH594) are notorious for their pathogenicity, which may lead to urinary tract infections, meningitis, and endocarditis (Mason et al. 2011). E. faecalis is one of the leading three causes of nosocomial infections, is the most clinically abundant species, and poses a severe threat to clinical illness. However, the origin of isolation and presence or absence of virulence genes alone cannot be used to assess the behavior of Enterococcus strains (Lindenstrauss et al. 2011). For example, collagen-binding protein ace was reported to be a virulence factor existing in E. fae
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