In the female mosquito, Aedes aegypti, neurohormones are released from
the brain in response to a blood meal and stimulate the ovaries to se
crete ecdysteroid hormones, which modulate yolk protein synthesis in t
he fat body. Neuropeptides with this bioactivity were isolated from he
ad extracts, and partial sequences from these peptides when aligned ga
ve a 31-residue sequence at the amino terminus. Oligonucleotide primer
s for this sequence were used to amplify with the polymerase chain rea
ction a genomic DNA product that hybridized to a clone from a head cDN
A library. The cDNA encodes a 149-residue preprohormone that is proces
sed into an 86-residue peptide, as indicated by the mass value obtaine
d from the native peptide, with the expected amino-terminal sequence,
After modification, the cDNA for the putative neurohormone was express
ed in a bacterial system, and the purified peptide had high specific a
ctivity in bioassays, thus confirming that it is a steroidogenic gonad
otropin, the first to be identified for invertebrates.