Identification of two abundant Aerococcus urinae cell wall-anchored proteins
(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
- Senneby, Erik LU ; Sunnerhagen, Torgny LU ; Hallström, Björn LU ; Lood, Rolf LU ; Malmström, Johan LU ; Karlsson, Christofer LU and Rasmussen, Magnus LU
- organization
- publishing date
- 2019-06-24
- 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
- 2024-09-18 06:19:54
@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}}, }