The browser you are using is not supported by this website. All versions of Internet Explorer are no longer supported, either by us or Microsoft (read more here: https://www.microsoft.com/en-us/microsoft-365/windows/end-of-ie-support).

Please use a modern browser to fully experience our website, such as the newest versions of Edge, Chrome, Firefox or Safari etc.

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

På svenska

Author

Summary, in English

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

Publishing year

2008

Language

English

Pages

609-617

Publication/Series

American Journal of Respiratory Cell and Molecular Biology

Volume

38

Issue

5

Document type

Journal article

Publisher

American Thoracic Society

Topic

  • Cell and Molecular Biology

Status

Published

Research group

  • Clinical Microbiology, Malmö

ISBN/ISSN/Other

  • ISSN: 1535-4989