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Titolo:
The V410M mutation associated with pyrethroid resistance in Heliothis virescens reduces the pyrethroid sensitivity of house fly sodium channels expressed in Xenopus oocytes
Autore:
Lee, SH; Soderlund, DM;
Indirizzi:
Cornell Univ, New York State Agr Expt Stn, Dept Entomol, Geneva, NY 14456 USA Cornell Univ Geneva NY USA 14456 Stn, Dept Entomol, Geneva, NY 14456 USA
Titolo Testata:
INSECT BIOCHEMISTRY AND MOLECULAR BIOLOGY
fascicolo: 1, volume: 31, anno: 2001,
pagine: 19 - 29
SICI:
0965-1748(200101)31:1<19:TVMAWP>2.0.ZU;2-4
Fonte:
ISI
Lingua:
ENG
Soggetto:
COCKROACHES BLATTELLA-GERMANICA; KNOCKDOWN-RESISTANCE; POINT MUTATIONS; NA+ CHANNELS; MOLECULAR CHARACTERIZATION; INSECTICIDE RESISTANCE; BREVETOXIN RECEPTOR; MUSCA-DOMESTICA; GENE; KDR;
Keywords:
insecticide; resistance; pyrethroid; batrachotoxin; voltage-sensitive sodium channel; Musca domestica;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
47
Recensione:
Indirizzi per estratti:
Indirizzo: Soderlund, DM Cornell Univ, New York State Agr Expt Stn, Dept Entomol, Geneva, NY 14456 USA Cornell Univ Geneva NY USA 14456 omol, Geneva, NY 14456 USA
Citazione:
S.H. Lee e D.M. Soderlund, "The V410M mutation associated with pyrethroid resistance in Heliothis virescens reduces the pyrethroid sensitivity of house fly sodium channels expressed in Xenopus oocytes", INSEC BIO M, 31(1), 2001, pp. 19-29

Abstract

Some strains of Heliothis virescens carry a novel sodium channel mutation,corresponding to the replacement of Val410 by Met (designated V410M) in the house fly Vsscl sodium channel, that is genetically and physiologically associated with pyrethroid resistance. To test the functional significance of this mutation, we created a house fly Vsscl sodium channel containing theV410M mutation by site-directed mutagenesis, expressed wildtype and specifically mutated sodium channels in Xenopus laevis oocytes, and evaluated theeffects of the V410M mutation on the functional and pharmacological properties of the expressed channels by two-electrode voltage clamp. The V410M mutation caused depolarizing shifts of similar to9 mV and similar to5 mV in the voltage dependence of activation and steady-state inactivation, respectively, of Vsscl sodium channels. The V410M mutation also reduced the sensitivity of Vsscl sodium channels to the pyrethroid cismethrin at least 10-foldand accelerated the decay of cismethrin-induced sodium tail currents. The degree of resistance conferred by the V410M mutation in the present study is sufficient to account for the degree of pyrethroid resistance in H, virescens that is associated with this mutation. Although Va1410 is located in asodium channel segment identified as part of the binding site for batrachotoxin, the V410M mutation did not alter the sensitivity of house fly sodiumchannels to batrachotoxin. The effects of the V410M mutation on the voltage dependence and cismethrin sensitivity of Vsscl sodium channels were indistinguishable from those caused by another sodium channel point mutation, replacement of Leu1014 by Phe (L1014F), that is the cause of knockdown resistance to pyrethroids in the house fly. The positions of the V410M and L1014Fmutations in models of the tertiary structure of sodium channels suggest that the pyrethroid binding site on the sodium channel a subunit is located at the interface between sodium channel domains I and II. (C) 2001 ElsevierScience Ltd. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/01/20 alle ore 16:10:34