Impact of mutations in DNA gyrase genes on quinolone resistance in Campylobacter jejuni

Changkwanyeun, Ruchirada; Yamaguchi, Tomoyuki; Kongsoi, Siriporn et al.

Drug Testing and Analysis, 2016, 8(10), 1071-1076

Permalink : https://hdl.handle.net/2115/67280

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アクセス権
open access
URI
https://hdl.handle.net/2115/67280
タイトル
Impact of mutations in DNA gyrase genes on quinolone resistance in Campylobacter jejuni
著者
Changkwanyeun, Ruchirada ; Yamaguchi, Tomoyuki ; Kongsoi, Siriporn ; Changkaew, Kanjana ; Yokoyama, Kazumasa ; Kim, Hyun ; Suthienkul, Orasa ; Usui, Masaru ; Tamura, Yutaka ; Nakajima, Chie ; Suzuki, Yasuhiko
著者名
Changkwanyeun, Ruchirada
著者名
Yamaguchi, Tomoyuki
著者名
Kongsoi, Siriporn
著者名
Changkaew, Kanjana
著者名
Yokoyama, Kazumasa
著者名
Kim, Hyun
著者名
Suthienkul, Orasa
著者名
Usui, Masaru
e-Rad_Researcher
50382487
著者名
Tamura, Yutaka
e-Rad_Researcher
60435964
著者名
Nakajima, Chie
e-Rad_Researcher
90206540
著者名
Suzuki, Yasuhiko
言語
英語
キーワード
Campylobacter jejuni
quinolone resistance
DNA gyrase
mutation
発行日
2016-10
出版者
Wiley-Blackwell
収録物名
Drug Testing and Analysis
巻(号)
8(10)
ページ
1071-1076
抄録
Amino acid substitutions providing quinolone resistance to Campyloabcter jejuni have been found in the quinolone resistance-determining region of protein DNA gyrase subunit A (GyrA), with the highest frequency at position 86 followed by position 90. In this study, wild-type and mutant recombinant DNA gyrase subunits were expressed in Escherichia coli and purified using Ni-NTA agarose column chromatography. Soluble 97 kDa GyrA and 87 kDa DNA gyrase subunit B were shown to reconstitute ATP-dependent DNA supercoiling activity. A quinolone-inhibited supercoiling assay demonstrated the roles of Thr86Ile, Thr86Ala, Thr86Lys, Asp90Asn, and Asp90Tyr amino acid substitutions in reducing sensitivity to quinolones. The marked effect of Thr86Ile on all examined quinolones suggested the advantage of this substitution in concordance with recurring isolation of quinolone-resistant C. jejuni. An analysis of the structure-activity relationship showed the importance of the substituent at position 8 in quinolones to overcome the effect of Thr86Ile. Sitafloxacin (SIT), which has a fluorinate cyclopropyl ring at R-1 and a chloride substituent at R-8, a characteristic not found in other quinolones, showed the highest inhibitory activity against all mutant C. jejuni gyrases including ciprofloxacin-resistant mutants. The results suggest SIT as a promising drug for the treatment of campylobacteriosis caused by CIP-resistant C. jejuni. Copyright (C) 2016 John Wiley & Sons, Ltd.
資源タイプ
学術雑誌論文
出版タイプ
Accepted Manuscript
権利情報
This is the peer reviewed version of the following article: R. Changkwanyeun, T. Yamaguchi, S. Kongsoi, K. Changkaew, K. Yokoyama, H. Kim, O. Suthienkul, M. Usui, Y. Tamura, C. Nakajima, Y. Suzuki. Impact of mutations in DNA gyrase genes on quinolone resistance in Campylobacter jejuni. Drug Test. Anal. 2016, 8, 1071, which has been published in final form at http://dx.doi.org/10.1002/dta.1937. This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Self-Archiving.
PISSN
1942-7603
EISSN
1942-7611
NCID
AA12629829
関連情報
PMID
26857529
関連情報 (isVersionOf)
出版社版DOI
https://doi.org/10.1002/dta.1937