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A group of salivary-gland-specific proteins, designated gp65, were identified in the mosquito Anopheles albimanus. Two-dimensional gel electrophoresis resolved this group into at least four molecules with pI 6.4-6.5. The N-terminal amino acid sequence was determined for the major species, gp65-1, and degenerate oligonucleotide primers were used to amplify a specific probe for library screening. A 1312 bp cDNA clone encoding a predicted translation product of 386 amino acids was recovered. gp65-1 is expressed abundantly in the medial and distal-lateral lobes of the adult female glands, and is secreted in the saliva. The amino acid sequence has potential sites for N-glycosylation, phosphorylation and myristylation, and is similar to a number of proteins of unknown function from other mosquito species.

Original publication




Journal article


Insect Mol Biol

Publication Date





155 - 164


Amino Acid Sequence, Animals, Anopheles, Base Sequence, DNA Primers, Electrophoresis, Gel, Two-Dimensional, Electrophoresis, Polyacrylamide Gel, Female, Gene Library, Immunoblotting, Molecular Sequence Data, Saliva, Salivary Glands, Salivary Proteins and Peptides, Sequence Analysis, DNA, Sex Characteristics