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. Author manuscript; available in PMC: 2011 Mar 14.
Published in final edited form as: Biochem J. 2009 Apr 15;419(2):377–385. doi: 10.1042/BJ20082082

Figure 2. Identification of four new residues in IIIS6 that contribute to sodium channel interaction with deltamethrin.

Figure 2

The amino acid sequence of the 20 residues flanking Phe1519 in IIIS6 of BgNav1-1A is shown. The boxed Phe1519 was identified previously to be critical for the binding and action of pyrethroids [11]. The four residues identified in the present study to be required for normal pyrethroid action are marked in bold. Responses to deltamethrin of wild-type channels and the four mutant channels (I1514A, G1516A, F1518A and N1522A) with altered sensitivities to pyrethroids are shown. The percentage of channel modification by deltamethrin was determined using the method described in the Experimental section. G1516A, F1518A and N1522A reduced channel sensitivity to deltamethrin 5-, 20- and 20-fold respectively, whereas I1514A increased channel sensitivity to deltamethrin 10-fold.