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, cilt.48, sa.2, ss.218-222, 2006 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 48 Sayı: 2
  • Basım Tarihi: 2006
  • Doi Numarası: 10.1111/j.1574-695x.2006.00148.x
  • Dergi Adı: FEMS IMMUNOLOGY AND MEDICAL MICROBIOLOGY
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.218-222
  • Anahtar Kelimeler: Streptococcus pneumoniae, IgA1 proteinase, chemically modified tetracycline, doxycycline, metalloproteinase, TERM-CARE FACILITY, FLUOROQUINOLONE-RESISTANT, METALLOPROTEINASES, IDENTIFICATION, COLONIZATION, EMERGENCE, VIRULENCE, PROTEASES, IGA
  • Gazi Üniversitesi Adresli: Evet

Özet

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.