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Moraxella-Dependent {alpha}1-Antichymotrypsin Neutralization - A Unique Virulence Mechanism.

Manolov, Taras LU ; Tan, Thuan Tong LU ; Forsgren, Arne LU and Riesbeck, Kristian LU (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)
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author
organization
publishing date
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
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
2008-07-29 16:06:05
date last changed
2017-01-01 05:07:05
@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},
  volume       = {38},
  year         = {2008},
}