Moraxella catarrhalis Evades Host Innate Immunity via Targeting Cartilage Oligomeric Matrix Protein.
(2016) In Journal of Immunology 196(3). p.1249-1258- Abstract
- Moraxella catarrhalis is a respiratory tract pathogen commonly causing otitis media in children and acute exacerbations in patients suffering from chronic obstructive pulmonary disease. Cartilage oligomeric matrix protein (COMP) functions as a structural component in cartilage, as well as a regulator of complement activity. Importantly, COMP is detected in resident macrophages and monocytes, alveolar fluid, and the endothelium of blood vessels in lung tissue. We show that the majority of clinical isolates of M. catarrhalis (n = 49), but not other tested bacterial pathogens, bind large amounts of COMP. COMP interacts directly with the ubiquitous surface protein A2 of M. catarrhalis. Binding of COMP correlates with survival of M. catarrhalis... (More)
- Moraxella catarrhalis is a respiratory tract pathogen commonly causing otitis media in children and acute exacerbations in patients suffering from chronic obstructive pulmonary disease. Cartilage oligomeric matrix protein (COMP) functions as a structural component in cartilage, as well as a regulator of complement activity. Importantly, COMP is detected in resident macrophages and monocytes, alveolar fluid, and the endothelium of blood vessels in lung tissue. We show that the majority of clinical isolates of M. catarrhalis (n = 49), but not other tested bacterial pathogens, bind large amounts of COMP. COMP interacts directly with the ubiquitous surface protein A2 of M. catarrhalis. Binding of COMP correlates with survival of M. catarrhalis in human serum by inhibiting bactericidal activity of the complement membrane attack complex. Moreover, COMP inhibits phagocytic killing of M. catarrhalis by human neutrophils. We further observed that COMP reduces bacterial adhesion and uptake by human lung epithelial cells, thus protecting M. catarrhalis from intracellular killing by epithelial cells. Taken together, our findings uncover a novel mechanism that M. catarrhalis uses to evade host innate immunity. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/8500256
- author
- organization
-
- Protein Chemistry, Malmö (research group)
- Clinical Microbiology, Malmö (research group)
- Clinical pathology, Malmö (research group)
- BioCARE: Biomarkers in Cancer Medicine improving Health Care, Education and Innovation
- Pathology, Malmö (research group)
- Rheumatology
- Department of Translational Medicine
- publishing date
- 2016
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Immunology
- volume
- 196
- issue
- 3
- pages
- 1249 - 1258
- publisher
- American Association of Immunologists
- external identifiers
-
- pmid:26712944
- wos:000368596600032
- scopus:84957707373
- pmid:26712944
- ISSN
- 1550-6606
- DOI
- 10.4049/jimmunol.1502071
- language
- English
- LU publication?
- yes
- id
- 65fd8491-9e31-41ad-a1b4-ff1a6de48ba4 (old id 8500256)
- alternative location
- http://www.ncbi.nlm.nih.gov/pubmed/26712944?dopt=Abstract
- date added to LUP
- 2016-04-01 09:53:20
- date last changed
- 2025-04-04 15:11:48
@article{65fd8491-9e31-41ad-a1b4-ff1a6de48ba4, abstract = {{Moraxella catarrhalis is a respiratory tract pathogen commonly causing otitis media in children and acute exacerbations in patients suffering from chronic obstructive pulmonary disease. Cartilage oligomeric matrix protein (COMP) functions as a structural component in cartilage, as well as a regulator of complement activity. Importantly, COMP is detected in resident macrophages and monocytes, alveolar fluid, and the endothelium of blood vessels in lung tissue. We show that the majority of clinical isolates of M. catarrhalis (n = 49), but not other tested bacterial pathogens, bind large amounts of COMP. COMP interacts directly with the ubiquitous surface protein A2 of M. catarrhalis. Binding of COMP correlates with survival of M. catarrhalis in human serum by inhibiting bactericidal activity of the complement membrane attack complex. Moreover, COMP inhibits phagocytic killing of M. catarrhalis by human neutrophils. We further observed that COMP reduces bacterial adhesion and uptake by human lung epithelial cells, thus protecting M. catarrhalis from intracellular killing by epithelial cells. Taken together, our findings uncover a novel mechanism that M. catarrhalis uses to evade host innate immunity.}}, author = {{Liu, Guanghui and Gradstedt, Henrik and Ermert, David and Englund, Emelie and Singh, Birendra and Su, Yu-Ching and Johansson, Martin and Aspberg, Anders and Agarwal, Vaibhav and Riesbeck, Kristian and Blom, Anna}}, issn = {{1550-6606}}, language = {{eng}}, number = {{3}}, pages = {{1249--1258}}, publisher = {{American Association of Immunologists}}, series = {{Journal of Immunology}}, title = {{Moraxella catarrhalis Evades Host Innate Immunity via Targeting Cartilage Oligomeric Matrix Protein.}}, url = {{http://dx.doi.org/10.4049/jimmunol.1502071}}, doi = {{10.4049/jimmunol.1502071}}, volume = {{196}}, year = {{2016}}, }