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.
Original language | English |
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Pages (from-to) | 18255 |
Journal | Scientific Reports |
Volume | 5 |
DOIs | |
Publication status | Published - 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