Moraxella-Dependent {alpha}1-Antichymotrypsin Neutralization - A Unique Virulence Mechanism.
(2008) In American Journal of Respiratory Cell and Molecular Biology 38(5). p.609-617- Abstract
- The acute phase reactant and protease inhibitor alpha1-antichymotrypsin is considered to play a protective role in the airways, but it is not known. Objectives: We analyzed whether the common respiratory pathogens Streptococcus pneumoniae, Haemophilus influenzae and Moraxella catarrhalis interact with antichymotrypsin. Methods: We compared a series of clinical isolates in addition to wild type and ubiquitous surface protein-deficient Moraxella to study the nature of antichymotrypsin binding by the bacteria. Measurements and Main Results: M. catarrhalis was the only species that bound antichymotrypsin among 25 bacterial species tested by flow cytometry and a direct binding assay. Experiments with Moraxella mutants revealed that ubiquitous... (More)
- The acute phase reactant and protease inhibitor alpha1-antichymotrypsin is considered to play a protective role in the airways, but it is not known. Objectives: We analyzed whether the common respiratory pathogens Streptococcus pneumoniae, Haemophilus influenzae and Moraxella catarrhalis interact with antichymotrypsin. Methods: We compared a series of clinical isolates in addition to wild type and ubiquitous surface protein-deficient Moraxella to study the nature of antichymotrypsin binding by the bacteria. Measurements and Main Results: M. catarrhalis was the only species that bound antichymotrypsin among 25 bacterial species tested by flow cytometry and a direct binding assay. Experiments with Moraxella mutants revealed that ubiquitous surface proteins A1 and A2 were responsible for the interaction, and using recombinant fragments, a consensus sequence within ubiquitous surface proteins A1 and A2 was defined. Binding of iodine labeled antichymotrypsin was dose dependent and strong (d (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1143594
- author
- Manolov, Taras LU ; Tan, Thuan Tong LU ; Forsgren, Arne LU and Riesbeck, Kristian LU
- organization
- publishing date
- 2008
- type
- Contribution to journal
- publication status
- published
- subject
- in
- American Journal of Respiratory Cell and Molecular Biology
- volume
- 38
- issue
- 5
- pages
- 609 - 617
- publisher
- American Thoracic Society
- external identifiers
-
- wos:000255692700015
- scopus:42949175646
- pmid:18096871
- ISSN
- 1535-4989
- DOI
- 10.1165/rcmb.2007-0289OC
- language
- English
- LU publication?
- yes
- id
- 2c4b249f-0fb9-4e37-b91c-e178ed1a5bad (old id 1143594)
- date added to LUP
- 2016-04-01 12:24:31
- date last changed
- 2022-04-29 05:35:30
@article{2c4b249f-0fb9-4e37-b91c-e178ed1a5bad, abstract = {{The acute phase reactant and protease inhibitor alpha1-antichymotrypsin is considered to play a protective role in the airways, but it is not known. Objectives: We analyzed whether the common respiratory pathogens Streptococcus pneumoniae, Haemophilus influenzae and Moraxella catarrhalis interact with antichymotrypsin. Methods: We compared a series of clinical isolates in addition to wild type and ubiquitous surface protein-deficient Moraxella to study the nature of antichymotrypsin binding by the bacteria. Measurements and Main Results: M. catarrhalis was the only species that bound antichymotrypsin among 25 bacterial species tested by flow cytometry and a direct binding assay. Experiments with Moraxella mutants revealed that ubiquitous surface proteins A1 and A2 were responsible for the interaction, and using recombinant fragments, a consensus sequence within ubiquitous surface proteins A1 and A2 was defined. Binding of iodine labeled antichymotrypsin was dose dependent and strong (d}}, author = {{Manolov, Taras and Tan, Thuan Tong and Forsgren, Arne and Riesbeck, Kristian}}, issn = {{1535-4989}}, language = {{eng}}, number = {{5}}, pages = {{609--617}}, publisher = {{American Thoracic Society}}, series = {{American Journal of Respiratory Cell and Molecular Biology}}, title = {{Moraxella-Dependent {alpha}1-Antichymotrypsin Neutralization - A Unique Virulence Mechanism.}}, url = {{http://dx.doi.org/10.1165/rcmb.2007-0289OC}}, doi = {{10.1165/rcmb.2007-0289OC}}, volume = {{38}}, year = {{2008}}, }