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Multicomponent Moraxella catarrhalis outer membrane vesicles induce an inflammatory response and are internalized by human epithelial cells.

Schaar, Viveka LU ; De Vries, Stefan P W; Perez Vidakovics, Maria Laura A; Bootsma, Hester J; Larsson, Lennart LU ; Hermans, Peter W M; Bjartell, Anders LU ; Mörgelin, Matthias LU and Riesbeck, Kristian LU (2011) In Cellular Microbiology Dec. p.432-449
Abstract
Moraxella catarrhalis is an emerging human respiratory pathogen in patients with chronic obstructive pulmonary disease (COPD) and in children with acute otitis media. The specific secretion machinery known as outer membrane vesicles (OMVs) is a mechanism by which Gram-negative pathogens interact with host cells during infection. We identified 57 proteins in M. catarrhalis OMVs using a proteomics approach combining two-dimensional SDS-PAGE and MALDI-TOF mass spectrometry analysis. The OMVs contained known surface proteins such as ubiquitous surface proteins (Usp) A1/A2, and Moraxella IgD-binding protein (MID). Most of the proteins are adhesins/virulence factors triggering the immune response, but also aid bacteria to evade the host defence.... (More)
Moraxella catarrhalis is an emerging human respiratory pathogen in patients with chronic obstructive pulmonary disease (COPD) and in children with acute otitis media. The specific secretion machinery known as outer membrane vesicles (OMVs) is a mechanism by which Gram-negative pathogens interact with host cells during infection. We identified 57 proteins in M. catarrhalis OMVs using a proteomics approach combining two-dimensional SDS-PAGE and MALDI-TOF mass spectrometry analysis. The OMVs contained known surface proteins such as ubiquitous surface proteins (Usp) A1/A2, and Moraxella IgD-binding protein (MID). Most of the proteins are adhesins/virulence factors triggering the immune response, but also aid bacteria to evade the host defence. FITC-stained OMVs bound to lipid raft domains in alveolar epithelial cells and were internalized after interaction with Toll-like receptor 2 (TLR2), suggesting a delivery to the host tissue of a large and complex group of OMV-attributed proteins. Interestingly, OMVs modulated the pro-inflammatory response in epithelial cells, and UspA1-bearing OMVs were found to specifically downregulate the reaction. When mice were exposed to OMVs, a pulmonary inflammation was clearly seen. Our findings indicate that Moraxella OMVs are highly biologically active, transport main bacterial virulence factors and may modulate the epithelial pro-inflammatory response. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Cellular Microbiology
volume
Dec
pages
432 - 449
publisher
Wiley-Blackwell
external identifiers
  • wos:000287317100010
  • pmid:21044239
  • scopus:79951507158
ISSN
1462-5814
DOI
10.1111/j.1462-5822.2010.01546.x
language
English
LU publication?
yes
id
ae04eeeb-749a-4bb0-92ab-51b1a080791c (old id 1732390)
alternative location
http://www.ncbi.nlm.nih.gov/pubmed/21044239?dopt=Abstract
date added to LUP
2010-12-01 10:24:07
date last changed
2017-11-12 04:06:38
@article{ae04eeeb-749a-4bb0-92ab-51b1a080791c,
  abstract     = {Moraxella catarrhalis is an emerging human respiratory pathogen in patients with chronic obstructive pulmonary disease (COPD) and in children with acute otitis media. The specific secretion machinery known as outer membrane vesicles (OMVs) is a mechanism by which Gram-negative pathogens interact with host cells during infection. We identified 57 proteins in M. catarrhalis OMVs using a proteomics approach combining two-dimensional SDS-PAGE and MALDI-TOF mass spectrometry analysis. The OMVs contained known surface proteins such as ubiquitous surface proteins (Usp) A1/A2, and Moraxella IgD-binding protein (MID). Most of the proteins are adhesins/virulence factors triggering the immune response, but also aid bacteria to evade the host defence. FITC-stained OMVs bound to lipid raft domains in alveolar epithelial cells and were internalized after interaction with Toll-like receptor 2 (TLR2), suggesting a delivery to the host tissue of a large and complex group of OMV-attributed proteins. Interestingly, OMVs modulated the pro-inflammatory response in epithelial cells, and UspA1-bearing OMVs were found to specifically downregulate the reaction. When mice were exposed to OMVs, a pulmonary inflammation was clearly seen. Our findings indicate that Moraxella OMVs are highly biologically active, transport main bacterial virulence factors and may modulate the epithelial pro-inflammatory response.},
  author       = {Schaar, Viveka and De Vries, Stefan P W and Perez Vidakovics, Maria Laura A and Bootsma, Hester J and Larsson, Lennart and Hermans, Peter W M and Bjartell, Anders and Mörgelin, Matthias and Riesbeck, Kristian},
  issn         = {1462-5814},
  language     = {eng},
  pages        = {432--449},
  publisher    = {Wiley-Blackwell},
  series       = {Cellular Microbiology},
  title        = {Multicomponent Moraxella catarrhalis outer membrane vesicles induce an inflammatory response and are internalized by human epithelial cells.},
  url          = {http://dx.doi.org/10.1111/j.1462-5822.2010.01546.x},
  volume       = {Dec},
  year         = {2011},
}