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

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...

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Bibliographic Details
Published in:FEMS immunology and medical microbiology 2006-11, Vol.48 (2), p.218-222
Main Authors: Walker, Stephen G., Carnu, Oana I., Tüter, Gülay, Ryan, Maria E.
Format: Article
Language:English
Subjects:
Antibiotics
Bacteriology
Biological and medical sciences
chemically modified tetracycline
Dose-Response Relationship, Drug
Doxycycline
Doxycycline - pharmacology
Enzymes
Fundamental and applied biological sciences. Psychology
Humans
IgA1 proteinase
Immunoglobulins
Metalloproteinase
Microbiology
Miscellaneous
Organic chemistry
Proteinase
Serine Endopeptidases - metabolism
Serine Proteinase Inhibitors - pharmacology
Streptococcus infections
Streptococcus pneumoniae
Streptococcus pneumoniae - drug effects
Streptococcus pneumoniae - enzymology
Streptococcus pneumoniae - isolation & purification
Tetracyclines - pharmacology
Virulence
Virulence factors
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Summary: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.
ISSN:0928-8244
1574-695X
2049-632X
DOI:10.1111/j.1574-695X.2006.00148.x