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A gut‐specific serine protease from the malaria vector Anopheles gambiae is downregulated after blood ingestion
Author(s) -
Shen Z.,
Edwards M. J.,
JacobsLorena M.
Publication year - 2000
Publication title -
insect molecular biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.955
H-Index - 93
eISSN - 1365-2583
pISSN - 0962-1075
DOI - 10.1046/j.1365-2583.2000.00188.x
Subject(s) - biology , trypsin , serine protease , chymotrypsin , blood meal , anopheles gambiae , biochemistry , microbiology and biotechnology , protease , complementary dna , messenger rna , recombinant dna , enzyme , gene , food science , immunology , malaria
A chymotrypsin‐like serine protease gene ( AgChyL ) was cloned from the mosquito Anopheles gambiae by a polymerase chain reaction (PCR)‐based subtractive cDNA cloning strategy. AgChyL messenger RNA (mRNA) is abundant in the adult female gut prior to, and for 8 h following, a blood meal. During the peak of digestion, from 12 to 24 h following a blood meal, AgChyL mRNA abundance decreased to barely detectable levels. AgChyL mRNA was abundant again by 48 h following a blood meal. Recombinant pro‐AgChyL was expressed in Escherichia coli . The pro‐enzyme can be activated by trypsin. Activated AgChyL cleaves the synthetic chymotrypsin substrate succinyl‐ l ‐Ala‐Ala‐Pro‐Phe‐nitroanilide, but not two other synthetic chymotrypsin substrates or synthetic trypsin and elastase substrates. The potential role of AgChyL in the coordination of An. gambiae digestion is discussed.