Homology model of the DNA gyrase enzyme of Helicobacter pylori, a target of quinolone-based eradication therapy

Juntaro Matsuzaki, Hidekazu Suzuki, Hitoshi Tsugawa, Toshihiro Nishizawa, Toshifumi Hibi

研究成果: Article査読

15 被引用数 (Scopus)

抄録

Background and Aims: Resistance of Helicobacter pylori to the standard therapeutic antimicrobial agents has been demonstrated. Although quinolones are an alternative candidate for third-line eradication therapy, quinolone resistance of H. pylori is also increasing. Quinolone resistance of H. pylori is caused by a point mutation of the DNA gyrase subunit A (GyrA) protein, especially on amino acids 87 and 91. The aim of this study is to surmise the structure of H. pylori GryA. Methods: The modeling of the 3-D structure of H. pylori GyrA was performed by an automated homology modeling program: SWISS-MODEL. The position of amino acids 87 and 91 in H. pylori GyrA was plotted on the homology model. To estimate the function of quinolone resistance-determining region (QRDR), the structure of H. pylori GyrA was compared with Escherichia coli GyrA. Results: A molecular model of H. pylori GyrA could be predicted using SWISS-MODEL. The GyrA N- and C-terminal domains closely resembled those of E. coli. The position of amino acids 87 and 91 in H. pylori GyrA was part of the DNA binding region (head dimer interface) on the GyrA N-terminal domain. Conclusion: Our homology model of H. pylori GryA suggests that the quinolone resistance-determining region is on the head dimer interface of the GyrA N-terminal domain.

本文言語English
ページ(範囲)S7-S10
ジャーナルJournal of Gastroenterology and Hepatology (Australia)
25
SUPPL. 1
DOI
出版ステータスPublished - 2010 5月

ASJC Scopus subject areas

  • 肝臓学
  • 消化器病学

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