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.
journal_name
Sci Repjournal_title
Scientific reportsauthors
Guzmán Prieto AM,Urbanus RT,Zhang X,Bierschenk D,Koekman CA,van Luit-Asbroek M,Ouwerkerk JP,Pape M,Paganelli FL,Wobser D,Huebner J,Hendrickx AP,Bonten MJ,Willems RJ,van Schaik Wdoi
10.1038/srep18255subject
Has Abstractpub_date
2015-12-17 00:00:00pages
18255issn
2045-2322pii
srep18255journal_volume
5pub_type
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