This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Maeda, Y.
Right arrow Articles by Hikichi, Y.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Maeda, Y.
Right arrow Articles by Hikichi, Y.
Agricola
Right arrow Articles by Maeda, Y.
Right arrow Articles by Hikichi, Y.

 Previous Article  |  Next Article 

Applied and Environmental Microbiology, February 2007, p. 1114-1119, Vol. 73, No. 4
0099-2240/07/$08.00+0     doi:10.1128/AEM.02400-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Amino Acid Substitutions in GyrA of Burkholderia glumae Are Implicated in Not Only Oxolinic Acid Resistance but Also Fitness on Rice Plants{triangledown}

Yukiko Maeda,1 Akinori Kiba,1 Kouhei Ohnishi,2 and Yasufumi Hikichi1*

Laboratory of Plant Pathology and Biotechnology,1 Institute of Molecular Genetics, Kochi University, 200 Monobe, Nankoku, Kochi 783-8502, Japan2

Received 12 October 2006/ Accepted 18 December 2006

Oxolinic acid (OA) resistance in field isolates of Burkholderia glumae, a causal agent of bacterial grain rot, is dependent on an amino acid substitution at position 83 in GyrA (GyrA83). In the present study, among spontaneous in vitro mutants from the OA-sensitive B. glumae strain Pg-10, we selected OA-resistant mutants that emerged at a rate of 5.7 x 10–10. Nucleotide sequence analysis of the quinolone resistance-determining region in GyrA showed that Gly81Cys, Gly81Asp, Asp82Gly, Ser83Arg, Asp87Gly, and Asp87Asn are observed in these OA-resistant mutants. The introduction of each amino acid substitution into Pg-10 resulted in OA resistance, similar to what was observed for mutants with the responsible amino acid substitution. In vitro growth of recombinants with Asp82Gly was delayed significantly compared to that of Pg-10; however, that of the other recombinants did not differ significantly. The inoculation of each recombinant into rice spikelets did not result in disease. In inoculated rice spikelets, recombinants with Ser83Arg grew less than Pg-10 during flowering, and growth of the other recombinants was reduced significantly. On the other hand, the reduced growth of recombinants with Ser83Arg in spikelets was compensated for under OA treatment, resulting in disease. These results suggest that amino acid substitutions in GyrA of B. glumae are implicated in not only OA resistance but also fitness on rice plants. Therefore, GyrA83 substitution is thought to be responsible for OA resistance in B. glumae field isolates.


* Corresponding author. Mailing address: Laboratory of Plant Pathology and Biotechnology, Kochi University, 200 Monobe, Nankoku, Kochi 783-8502, Japan. Phone: 81-88-864-5218. Fax: 81-88-864-5200. E-mail: yhikichi{at}cc.kochi-u.ac.jp.

{triangledown} Published ahead of print on 28 December 2006.


Applied and Environmental Microbiology, February 2007, p. 1114-1119, Vol. 73, No. 4
0099-2240/07/$08.00+0     doi:10.1128/AEM.02400-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.