|Appears in Collections:||Aquaculture Journal Articles|
|Peer Review Status:||Refereed|
|Title:||Molecular cloning and characterisation of a novel P-glycoprotein in the salmon louse Lepeophtheirus salmonis|
Carmichael, Stephen N
|Citation:||Heumann J, Carmichael SN, Bron J, Tildesley A & Sturm A (2012) Molecular cloning and characterisation of a novel P-glycoprotein in the salmon louse Lepeophtheirus salmonis, Comparative Biochemistry and Physiology - Part C: Toxicology and Pharmacology, 155 (2), pp. 198-205.|
|Abstract:||The salmon louse, Lepeophtheirus salmonis, is a crustacean ectoparasite of salmonid fish. At present, sea louse control on salmon farms relies heavily upon chemical treatments. Drug efflux transport, mediated by ABC transporters such as P-glycoprotein (Pgp), represents a major mechanism for drug resistance in parasites. We report here the molecular cloning of a new Pgp from the salmon louse, called SL-PGY1. A partial Pgp sequence was obtained by searching sea louse ESTs, and extended by rapid amplification of cDNA ends (RACE). The open reading frame of SL-PGY1 encodes a protein of 1438 amino acids that possesses typical structural traits of P-glycoproteins, and shows a high degree of sequence homology to invertebrate and vertebrate P-glycoproteins. In the absence of drug exposure, SL-PGY1 mRNA expression levels did not differ between a drug-susceptible strain of L. salmonis and a strain showing a ~ 7-fold decrease in sensitivity against emamectin benzoate, the active component of the in-feed sea louse treatment SLICE® (Merck Animal Health). Aqueous exposure of the hyposensitive salmon louse strain to emamectin benzoate (24 h, 410 μg/L) provoked a 2.9-fold upregulation of SL-PGY1. Adult male lice of both strains showed a greater abundance of SL-PGY1 mRNA than adult females.|
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