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Identification of two abundant Aerococcus urinae cell wall-anchored proteins

Senneby, Erik LU ; Sunnerhagen, Torgny LU orcid ; Hallström, Björn LU ; Lood, Rolf LU ; Malmström, Johan LU orcid ; Karlsson, Christofer LU and Rasmussen, Magnus LU (2019) In International Journal of Medical Microbiology 309(7).
Abstract

Aerococcus urinae is an emerging pathogen that causes urinary tract infections, bacteremia and infective endocarditis. The mechanisms through which A. urinae cause infection are largely unknown. The aims of this study were to describe the surface proteome of A. urinae and to analyse A. urinae genomes in search for genes encoding surface proteins. Two proteins, denoted Aerococcal surface protein (Asp) 1 and 2, were through the use of mass spectrometry based proteomics found to quantitatively dominate the aerococcal surface. The presence of these proteins on the surface was also shown using ELISA with serum from rabbits immunized with the recombinant Asp. These proteins had a signal sequence in the amino-terminal end and a cell... (More)

Aerococcus urinae is an emerging pathogen that causes urinary tract infections, bacteremia and infective endocarditis. The mechanisms through which A. urinae cause infection are largely unknown. The aims of this study were to describe the surface proteome of A. urinae and to analyse A. urinae genomes in search for genes encoding surface proteins. Two proteins, denoted Aerococcal surface protein (Asp) 1 and 2, were through the use of mass spectrometry based proteomics found to quantitatively dominate the aerococcal surface. The presence of these proteins on the surface was also shown using ELISA with serum from rabbits immunized with the recombinant Asp. These proteins had a signal sequence in the amino-terminal end and a cell wall-sorting region in the carboxy-terminal end, which contained an LPATG-motif, a hydrophobic domain and a positively charged tail. Twenty-three additional A. urinae genomes were sequenced using Illumina HiSeq technology. Six different variants of asp genes were found (denoted asp1-6). All isolates had either one or two of these asp-genes located in a conserved locus, designated Locus encoding Aerococcal Surface Proteins (LASP). The 25 genomes had in median 13 genes encoding LPXTG-proteins (range 6-24). For other Gram-positive bacteria, cell wall-anchored surface proteins with an LPXTG-motif play a key role for virulence. Thus, it will be of great interest to explore the function of the Asp proteins of A. urinae to establish a better understanding of the molecular mechanisms by which A. urinae cause disease.

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author
; ; ; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
International Journal of Medical Microbiology
volume
309
issue
7
article number
151325
publisher
Elsevier
external identifiers
  • pmid:31257068
  • scopus:85067916457
ISSN
1618-0607
DOI
10.1016/j.ijmm.2019.06.005
project
Infections caused by Aerococcus and other endocarditis-causing pathogens
language
English
LU publication?
yes
additional info
Copyright © 2019. Published by Elsevier GmbH.
id
bb0532c2-67d9-4721-a4a3-4f862a576f0d
date added to LUP
2019-07-04 01:52:56
date last changed
2024-03-03 19:50:21
@article{bb0532c2-67d9-4721-a4a3-4f862a576f0d,
  abstract     = {{<p>Aerococcus urinae is an emerging pathogen that causes urinary tract infections, bacteremia and infective endocarditis. The mechanisms through which A. urinae cause infection are largely unknown. The aims of this study were to describe the surface proteome of A. urinae and to analyse A. urinae genomes in search for genes encoding surface proteins. Two proteins, denoted Aerococcal surface protein (Asp) 1 and 2, were through the use of mass spectrometry based proteomics found to quantitatively dominate the aerococcal surface. The presence of these proteins on the surface was also shown using ELISA with serum from rabbits immunized with the recombinant Asp. These proteins had a signal sequence in the amino-terminal end and a cell wall-sorting region in the carboxy-terminal end, which contained an LPATG-motif, a hydrophobic domain and a positively charged tail. Twenty-three additional A. urinae genomes were sequenced using Illumina HiSeq technology. Six different variants of asp genes were found (denoted asp1-6). All isolates had either one or two of these asp-genes located in a conserved locus, designated Locus encoding Aerococcal Surface Proteins (LASP). The 25 genomes had in median 13 genes encoding LPXTG-proteins (range 6-24). For other Gram-positive bacteria, cell wall-anchored surface proteins with an LPXTG-motif play a key role for virulence. Thus, it will be of great interest to explore the function of the Asp proteins of A. urinae to establish a better understanding of the molecular mechanisms by which A. urinae cause disease.</p>}},
  author       = {{Senneby, Erik and Sunnerhagen, Torgny and Hallström, Björn and Lood, Rolf and Malmström, Johan and Karlsson, Christofer and Rasmussen, Magnus}},
  issn         = {{1618-0607}},
  language     = {{eng}},
  month        = {{06}},
  number       = {{7}},
  publisher    = {{Elsevier}},
  series       = {{International Journal of Medical Microbiology}},
  title        = {{Identification of two abundant Aerococcus urinae cell wall-anchored proteins}},
  url          = {{https://lup.lub.lu.se/search/files/119473383/Identification_of_two_abundant_Aerococcus_urinae_cell_wall_anchored_proteins.pdf}},
  doi          = {{10.1016/j.ijmm.2019.06.005}},
  volume       = {{309}},
  year         = {{2019}},
}