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

Research output: Contribution to journalArticle

Authors

  • 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

Colleges, School and Institutes

Abstract

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.

Details

Original languageEnglish
Pages (from-to)18255
JournalScientific Reports
Volume5
Publication statusPublished - 17 Dec 2015

Keywords

  • 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