The N-terminal domain of the thermo-regulated surface protein PrpA of Enterococcus faecium binds to fibrinogen, fibronectin and platelets

Ana M Guzmán Prieto, Rolf T Urbanus, Xinglin Zhang, Damien Bierschenk, C Arnold Koekman, Miranda van Luit-Asbroek, Janneke P Ouwerkerk, Marieke Pape, Fernanda L Paganelli, Dominique Wobser, Johannes Huebner, Antoni P A Hendrickx, Marc J M Bonten, Rob J L Willems, Willem van Schaik

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Enterococcus faecium is a commensal of the mammalian gastrointestinal tract, but is also found in non-enteric environments where it can grow between 10 °C and 45 °C. E. faecium has recently emerged as a multi-drug resistant nosocomial pathogen. We hypothesized that genes involved in the colonization and infection of mammals exhibit temperature-regulated expression control and we therefore performed a transcriptome analysis of the clinical isolate E. faecium E1162, during mid-exponential growth at 25 °C and 37 °C. One of the genes that exhibited differential expression between 25 °C and 37 °C, was predicted to encode a peptidoglycan-anchored surface protein. The N-terminal domain of this protein is unique to E. faecium and closely related enterococci, while the C-terminal domain is homologous to the Streptococcus agalactiae surface protein BibA. This region of the protein contains proline-rich repeats, leading us to name the protein PrpA for proline-rich protein A. We found that PrpA is a surface-exposed protein which is most abundant during exponential growth at 37 °C in E. faecium E1162. The heterologously expressed and purified N-terminal domain of PrpA was able to bind to the extracellular matrix proteins fibrinogen and fibronectin. In addition, the N-terminal domain of PrpA interacted with both non-activated and activated platelets.

Original languageEnglish
Pages (from-to)18255
JournalScientific Reports
Publication statusPublished - 17 Dec 2015


  • Bacterial Proteins
  • Base Sequence
  • Binding Sites
  • Blood Platelets
  • Cross Infection
  • Enterococcus faecium
  • Fibrinogen
  • Fibronectins
  • Gene Expression Regulation, Bacterial
  • Gram-Positive Bacterial Infections
  • Humans
  • Membrane Proteins
  • Microscopy, Electron, Transmission
  • Molecular Sequence Data
  • Peptidoglycan
  • Promoter Regions, Genetic
  • Protein Binding
  • Reverse Transcriptase Polymerase Chain Reaction
  • Sequence Homology, Nucleic Acid
  • Temperature
  • Journal Article
  • Research Support, Non-U.S. Gov't


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