4.7 Article

A novel Pro197Glu substitution in acetolactate synthase (ALS) confers broad-spectrum resistance across ALS inhibitors

Journal

PESTICIDE BIOCHEMISTRY AND PHYSIOLOGY
Volume 117, Issue -, Pages 31-38

Publisher

ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.pestbp.2014.10.005

Keywords

ALS inhibitor; ALS resistance mutation; Cross-resistance; (d)CAPS; Water chickweed (Myosoton aquaticum (L) Moench.)

Funding

  1. Special Fund for Agroscientific Research in the Public Interest [201303031]
  2. Ph.D. Programs Foundation of the Ministry of Education of China [20133702110017]

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Water chickweed (Myosoton aquaticum L.), a competitive broadleaf weed, is widespread in wheat fields in China. Tribenuron and pyroxsulam failed to control water chickweed in the same field in Qiaotian Village in 2011 and 2012, respectively. An initial tribenuron resistance confirmation test identified a resistant population (AH02). ALS gene sequencing revealed a previously unreported substitution of Glu for Pro at amino acid position 197 in resistant individuals. A purified subpopulation (WRR04) that was individually homozygous for the Pro197Glu substitution was generated and characterized in terms of its response to different classes of ALS inhibitors. A whole-plant experiment showed that the WRRO4 population exhibited broad-spectrum resistance to tribenuron (SU, 318-folds, pyrithiobac sodium (PTB, > 197-fold), pyroxsulam (TP, 81-fold), florasulam (TP, > 36-fold) and imazethapyr (IMI, 11-fold). An in vitro ALS assay confirmed that the ALS from WRRO4 showed high resistance to all the tested ALS inhibitors. These results established that the Pro197Glu substitution endows broad-spectrum resistance across ALS inhibitors in water chickweed. In addition, molecular markers were developed to rapidly identify the Pro197Glu mutation. Crown Copyright (C) 2014 Published by Elsevier Inc. All rights reserved.

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