The immunoglobulin A1 proteinase from Streptococcus pneumoniae is inhibited by tetracycline compounds.
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.
Walker
Stephen G
SG
Department of Oral Biology and Pathology, School of Dental Medicine, State University of New York at Stony Brook, NY 11794-8702, USA. stephen.walker@stonybrook.edu
Carnu
Oana I
OI
Tüter
Gülay
G
Ryan
Maria E
ME
D004305:Dose-Response Relationship, Drug; D004318:Doxycycline / Q000494:pharmacology; D006801:Humans; D012697:Serine Endopeptidases / Q000378:metabolism*; D015842:Serine Proteinase Inhibitors / Q000494:pharmacology*; D013296:Streptococcus pneumoniae / Q000187:drug effects / Q000201:enzymology* / Q000302:isolation & purification; D013754:Tetracyclines / Q000494:pharmacology*
D015842:Serine Proteinase Inhibitors; D013754:Tetracyclines; C117155:tetracycline CMT-3; D012697:Serine Endopeptidases; C021433:IgA-specific serine endopeptidase; D004318:Doxycycline