Literature DB >> 16995879

The immunoglobulin A1 proteinase from Streptococcus pneumoniae is inhibited by tetracycline compounds.

Stephen G Walker1, Oana I Carnu, Gülay Tüter, Maria E Ryan.   

Abstract

Streptococcus pneumoniae produces a zinc-dependent proteinase that cleaves human immunoglobulin (Ig) A1 in the hinge region. This metalloproteinase is hypothesized to act as a virulence factor by allowing S. pneumoniae to evade the protection provided by IgA1, thus enhancing its ability to colonize the human nasopharyngeal region. No biologically compatible inhibitors of this enzyme have been identified. We determined that doxycycline and a chemically modified tetracycline inhibit this enzyme in vitro at low micromolar concentrations.

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Year:  2006        PMID: 16995879     DOI: 10.1111/j.1574-695X.2006.00148.x

Source DB:  PubMed          Journal:  FEMS Immunol Med Microbiol        ISSN: 0928-8244


  2 in total

1.  Development of a high-throughput screen and its use in the discovery of Streptococcus pneumoniae immunoglobulin A1 protease inhibitors.

Authors:  Amanda L Garner; Jessica L Fullagar; Joshua A Day; Seth M Cohen; Kim D Janda
Journal:  J Am Chem Soc       Date:  2013-06-28       Impact factor: 15.419

2.  Lower Density and Shorter Duration of Nasopharyngeal Carriage by Pneumococcal Serotype 1 (ST217) May Explain Its Increased Invasiveness over Other Serotypes.

Authors:  Dean B Everett; Aras Kadioglu; Laura Bricio-Moreno; Chrispin Chaguza; Reham Yahya; Rebecca K Shears; Jennifer E Cornick; Karsten Hokamp; Marie Yang; Daniel R Neill; Neil French; Jay C D Hinton
Journal:  mBio       Date:  2020-12-08       Impact factor: 7.867

  2 in total

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