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

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Walker S. G., Carnu O. I., Tuter G., Ryan M. E.

FEMS IMMUNOLOGY AND MEDICAL MICROBIOLOGY, vol.48, no.2, pp.218-222, 2006 (SCI-Expanded) identifier identifier identifier

  • Publication Type: Article / Article
  • Volume: 48 Issue: 2
  • Publication Date: 2006
  • Doi Number: 10.1111/j.1574-695x.2006.00148.x
  • Journal Name: FEMS IMMUNOLOGY AND MEDICAL MICROBIOLOGY
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Page Numbers: pp.218-222
  • Keywords: Streptococcus pneumoniae, IgA1 proteinase, chemically modified tetracycline, doxycycline, metalloproteinase, TERM-CARE FACILITY, FLUOROQUINOLONE-RESISTANT, METALLOPROTEINASES, IDENTIFICATION, COLONIZATION, EMERGENCE, VIRULENCE, PROTEASES, IGA
  • Gazi University Affiliated: Yes

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.