Cookies on this website

We use cookies to ensure that we give you the best experience on our website. If you click 'Accept all cookies' we'll assume that you are happy to receive all cookies and you won't see this message again. If you click 'Reject all non-essential cookies' only necessary cookies providing core functionality such as security, network management, and accessibility will be enabled. Click 'Find out more' for information on how to change your cookie settings.

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

DOI

10.1111/j.0962-1075.2004.00473.x

Type

Journal article

Journal

Insect Mol Biol

Publication Date

04/2004

Volume

13

Pages

155 - 164

Keywords

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