Cloning and characterization of midgut-specific gene/gene products in the mosquito Aedes aegypti

Persistent Link:
http://hdl.handle.net/10150/282179
Title:
Cloning and characterization of midgut-specific gene/gene products in the mosquito Aedes aegypti
Author:
Jiang, Qijiao
Issue Date:
1996
Publisher:
The University of Arizona.
Rights:
Copyright © is held by the author. Digital access to this material is made possible by the University Libraries, University of Arizona. Further transmission, reproduction or presentation (such as public display or performance) of protected items is prohibited except with permission of the author.
Abstract:
The yellow fever and dengue fever carrying mosquito, Aedes aegypti, requires blood feeding for egg production. The blood proteins are digested in the midgut to yield amino acids which are the nutritional source for oogenesis. Serine proteases are important enzymes that participate in the process of blood protein digestion. The identification of the corresponding genes may have significant implications in the control of mosquito-borne diseases. A gut-specific chymotrypsin-like cDNA was isolated and sequenced. The 938 bp clone encodes a preproenzyme with a putative 18 amino acid signal peptide sequence, a 7 amino acid activation peptide sequence rich in serine and charged residues, and a mature enzyme of 268 amino acids. The deduced amino acid sequence has a typical catalytic triad region for serine proteases (His 57, Asp 102 and Ser 195 in bovine chymotrypsin numbering system), and the hydrophobic substrate binding pocket with most features of chymotrypsins. Six cysteine residues are present in the sequence which are characteristically involved in disulfide bond formation in invertebrate serine proteases. Characterization of the gene expression and the protein synthesis, as well as the enzymatic activity in the midgut, clearly demonstrated that (1) the chymotrypsin gene is newly transcribed after eclosion and the mRNA is present almost steadily during the digestion of a meal; (2) the chymotrypsin synthesis and its corresponding activity are induced and increased significantly by the ingestion of a meal. In vitro studies of the recombinant protease derived from the cDNA clone indicated several unique properties of the mosquito chymotrypsin compared with its bovine analog.
Type:
text; Dissertation-Reproduction (electronic)
Keywords:
Biology, Molecular.; Biology, Entomology.
Degree Name:
Ph.D.
Degree Level:
doctoral
Degree Program:
Graduate College; Biochemistry
Degree Grantor:
University of Arizona
Advisor:
Wells, Michael A.

Full metadata record

DC FieldValue Language
dc.language.isoen_USen_US
dc.titleCloning and characterization of midgut-specific gene/gene products in the mosquito Aedes aegyptien_US
dc.creatorJiang, Qijiaoen_US
dc.contributor.authorJiang, Qijiaoen_US
dc.date.issued1996en_US
dc.publisherThe University of Arizona.en_US
dc.rightsCopyright © is held by the author. Digital access to this material is made possible by the University Libraries, University of Arizona. Further transmission, reproduction or presentation (such as public display or performance) of protected items is prohibited except with permission of the author.en_US
dc.description.abstractThe yellow fever and dengue fever carrying mosquito, Aedes aegypti, requires blood feeding for egg production. The blood proteins are digested in the midgut to yield amino acids which are the nutritional source for oogenesis. Serine proteases are important enzymes that participate in the process of blood protein digestion. The identification of the corresponding genes may have significant implications in the control of mosquito-borne diseases. A gut-specific chymotrypsin-like cDNA was isolated and sequenced. The 938 bp clone encodes a preproenzyme with a putative 18 amino acid signal peptide sequence, a 7 amino acid activation peptide sequence rich in serine and charged residues, and a mature enzyme of 268 amino acids. The deduced amino acid sequence has a typical catalytic triad region for serine proteases (His 57, Asp 102 and Ser 195 in bovine chymotrypsin numbering system), and the hydrophobic substrate binding pocket with most features of chymotrypsins. Six cysteine residues are present in the sequence which are characteristically involved in disulfide bond formation in invertebrate serine proteases. Characterization of the gene expression and the protein synthesis, as well as the enzymatic activity in the midgut, clearly demonstrated that (1) the chymotrypsin gene is newly transcribed after eclosion and the mRNA is present almost steadily during the digestion of a meal; (2) the chymotrypsin synthesis and its corresponding activity are induced and increased significantly by the ingestion of a meal. In vitro studies of the recombinant protease derived from the cDNA clone indicated several unique properties of the mosquito chymotrypsin compared with its bovine analog.en_US
dc.typetexten_US
dc.typeDissertation-Reproduction (electronic)en_US
dc.subjectBiology, Molecular.en_US
dc.subjectBiology, Entomology.en_US
thesis.degree.namePh.D.en_US
thesis.degree.leveldoctoralen_US
thesis.degree.disciplineGraduate Collegeen_US
thesis.degree.disciplineBiochemistryen_US
thesis.degree.grantorUniversity of Arizonaen_US
dc.contributor.advisorWells, Michael A.en_US
dc.identifier.proquest9713425en_US
dc.identifier.bibrecord.b34434951en_US
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