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The salivary gland proteins of adult female Anopheles darlingi were fractionated by reverse-phase HPLC and the five major peaks were submitted for amino-terminal sequencing using automated Edman degradation. The amino acid sequence of one of the purified salivary gland proteins showed similarity with the D7r3 protein of An. gambiae. Cloning and sequencing of two cDNAs allowed the prediction of the complete sequence of the An. darlingi D7 protein. The D7r3 protein is present specifically in adult female salivary glands of An. darlingi and despite being one of the major salivary gland proteins its function is not known. Predictions of secondary and tertiary structures revealed the similarity of the An. darlingi D7 protein to insect odorant binding proteins. This suggests that D7 proteins may act as carriers of hydrophobic molecules in mosquito saliva.

Original publication




Journal article


Insect Biochem Mol Biol

Publication Date





1419 - 1427


Amino Acid Sequence, Animals, Anopheles, Base Sequence, Chromatography, High Pressure Liquid, Female, Hydrogen-Ion Concentration, Insect Proteins, Models, Molecular, Molecular Sequence Data, Peptide Fragments, Protein Conformation, Salivary Proteins and Peptides, Sequence Alignment, Sequence Homology, Amino Acid, Sequence Homology, Nucleic Acid, Solubility, Tenebrio