Shpp. Karunaratne et al., THE CROSS-REACTIVITY SPECTRUM OF A POLYCLONAL ANTISERUM RAISED AGAINST THE NATIVE AMPLIFIED A(2) ESTERASE INVOLVED IN INSECTICIDE RESISTANCE, Pesticide biochemistry and physiology, 53(2), 1995, pp. 75-83
Broad-spectrum insecticide resistance in the mosquito Culex quinquefas
ciatus is usually due to the overproduction of A- and B-type carboxyle
sterases (EC 3.1.1.1). Antiserum was raised against the carboxylestera
se A(2) purified from an organophosphate-resistant Culex strain. This
antiserum was used to show that, contrary to earlier reports, the A(2)
esterase is immunologically related to other A- and B-type carboxyles
terases from resistant and susceptible Culex strains. Dot-blot immunoa
ssays revealed that the purified esterase B-2 is about 50-fold less re
active with the antiserum than the purified esterase A(2). A strong im
munological relationship was observed between the A(2) antiserum and t
he organophosphate and carbamate target site acetylcholinesterase. A l
ower cross-reactivity with Anopheles stephensi esterases and no reacti
vity with resistance-associated esterases from grain beetles, planthop
pers, and cockroaches were observed. The antiserum cross-reacted with
some commercially available vertebrate esterases indicating its affini
ties with these enzymes. The observed cross-reactivity is not due to t
he antiserum cross-reacting with glycosylated residues, as the A(2) es
terase to which the antiserum was raised is unglycosylated. The utilit
y of this antiserum in future esterase cDNA cloning programs is discus
sed. (C) 1995 Academic Press, Inc.