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The saliva of hematophagous insects contains a variety of pharmacologically active substances that counteract the normal hemostatic response to injury in vertebrate hosts. The yellow-fever mosquito, Aedes aegypti, secretes an apyrase that inhibits ADP-dependent platelet aggregation. Apyrase was purified as an active enzyme from adult female salivary glands and subjected to tryptic digestion, and the resulting peptides were sequenced. The amino acid sequences obtained match the conceptual translation product of a cDNA clone isolated from an adult female salivary gland library. Sequence comparisons indicate similarities with a ubiquitous family of 5'-nucleotidases. The mosquito protein differs from other members of the family by lacking a carboxyl-terminal hydrophobic domain. The apparent conversion of a gene encoding an enzyme involved in a common metabolic event at the cellular level to a gene involved in the antihemostatic response of mosquitoes illustrates one way this particular insect has adapted to the challenges of bloodfeeding.

Original publication




Journal article


Proc Natl Acad Sci U S A

Publication Date





694 - 698


5'-Nucleotidase, Aedes, Amino Acid Sequence, Animals, Apyrase, Base Sequence, Cloning, Molecular, DNA, Complementary, Female, Genes, Insect, Molecular Sequence Data, Salivary Glands, Sequence Analysis, Sequence Analysis, DNA, Sequence Homology, Amino Acid