Intriguing olfactory proteins from the yellow fever mosquito,<Emphasis Type="Italic"> Aedes aegypti</Emphasis>

Four antennae-specific proteins (AaegOBP1, AaegOBP2, AaegOBP3, and AaegASP1) were isolated from the yellow fever mosquito, Aedes aegypti and their full-length cDNAs were cloned. RT-PCR indicated that they are expressed in female and, to a lesser extent, in male antennae, but not in control tissues (legs). AaegOBP1 and AaegOBP3 showed significant similarity to previously identified mosquito odorant-binding proteins (OBPs) in cysteine spacing pattern and sequence. Two of the isolated proteins have a total of eight cysteine residues. The similarity of the spacing pattern of the cysteine residues and amino acid sequence to those of previously identified olfactory proteins suggests that one of the cysteine-rich proteins (AaegOBP2) is an OBP. The other (AaegASP1) did not belong to any group of known OBPs. Structural analyses indicate that six of the cysteine residues in AaegOBP2 are linked in a similar pattern to the previously known cysteine pairing in OBPs, i.e., Cys-24–Cys-55, Cys-51–Cys-104, Cys-95–Cys-113. The additional disulfide bridge, Cys-38–Cys-125, knits the extended C-terminal segment of the protein to a predicted 2-helix. As indicated by circular dichroism (CD) spectra, the extra rigidity seems to prevent the predicted formation of a C-terminal -helix at low pH.Electronic Supplementary Material  Supplementary material is available for this article if you access the article at . A link in the frame on the left on that page takes you directly to the supplementary material.