Characterization of Aedes Dredd: a novel initiator caspase from the yellow fever mosquito, Aedes aegypti. 2007

Dawn M Cooper, and Frederic Pio, and Emily P Thi, and Dave Theilmann, and Carl Lowenberger
Department of Biological Sciences, Simon Fraser University, Burnaby, BC, Canada. dmcooper@sfu.ca

Caspases play an essential role during programmed cell death in all metazoans. These enzymes are cysteine proteases and comprise a multi-gene family with more than a dozen mammalian family members. Although caspases have been characterized in many animals, including Drosophila melanogaster, little is known about the caspases that exist in mosquitoes. Here we describe the identification and characterization of Aedes Dredd (AeDredd), a novel caspase in the yellow fever mosquito, Aedes aegypti. AeDredd contains two N-terminal death effector domains and the well conserved caspase catalytic domain. Multiple sequence alignments and functional substrate assays of recombinant protein suggest that AeDredd is an orthologue of Drosophila Dredd and human caspase-8, both central effectors of the death receptor-mediated apoptotic pathway. AeDredd exhibits substrate specificity most similar to human caspase-8. AeDredd transcripts were found in all developmental stages with highest expression in early pupae. Within adults, AeDredd was found in all the tissues examined, with the highest transcript levels detected in fat body tissues. This is the first functional characterization of a death domain-containing caspase in an insect vector of human disease, and will initiate studies on the role of apoptosis in the innate immune response of vectors towards intracellular parasites such as viruses.

UI MeSH Term Description Entries
D008958 Models, Molecular Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures. Molecular Models,Model, Molecular,Molecular Model
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D009928 Organ Specificity Characteristic restricted to a particular organ of the body, such as a cell type, metabolic response or expression of a particular protein or antigen. Tissue Specificity,Organ Specificities,Specificities, Organ,Specificities, Tissue,Specificity, Organ,Specificity, Tissue,Tissue Specificities
D011487 Protein Conformation The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain). Conformation, Protein,Conformations, Protein,Protein Conformations
D004440 Ecdysone A steroid hormone that regulates the processes of MOLTING or ecdysis in insects. Molting Hormone
D000330 Aedes A genus of mosquitoes (CULICIDAE) frequently found in tropical and subtropical regions. YELLOW FEVER and DENGUE are two of the diseases that can be transmitted by species of this genus. Aede
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D013379 Substrate Specificity A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts. Specificities, Substrate,Specificity, Substrate,Substrate Specificities
D014466 Ultraviolet Rays That portion of the electromagnetic spectrum immediately below the visible range and extending into the x-ray frequencies. The longer wavelengths (near-UV or biotic or vital rays) are necessary for the endogenous synthesis of vitamin D and are also called antirachitic rays; the shorter, ionizing wavelengths (far-UV or abiotic or extravital rays) are viricidal, bactericidal, mutagenic, and carcinogenic and are used as disinfectants. Actinic Rays,Black Light, Ultraviolet,UV Light,UV Radiation,Ultra-Violet Rays,Ultraviolet Light,Ultraviolet Radiation,Actinic Ray,Light, UV,Light, Ultraviolet,Radiation, UV,Radiation, Ultraviolet,Ray, Actinic,Ray, Ultra-Violet,Ray, Ultraviolet,Ultra Violet Rays,Ultra-Violet Ray,Ultraviolet Black Light,Ultraviolet Black Lights,Ultraviolet Radiations,Ultraviolet Ray

Related Publications

Dawn M Cooper, and Frederic Pio, and Emily P Thi, and Dave Theilmann, and Carl Lowenberger
May 2002, Histochemistry and cell biology,
Dawn M Cooper, and Frederic Pio, and Emily P Thi, and Dave Theilmann, and Carl Lowenberger
August 1997, Insect molecular biology,
Dawn M Cooper, and Frederic Pio, and Emily P Thi, and Dave Theilmann, and Carl Lowenberger
September 2004, Die Naturwissenschaften,
Dawn M Cooper, and Frederic Pio, and Emily P Thi, and Dave Theilmann, and Carl Lowenberger
April 1992, The Journal of experimental biology,
Dawn M Cooper, and Frederic Pio, and Emily P Thi, and Dave Theilmann, and Carl Lowenberger
October 2001, Insect biochemistry and molecular biology,
Dawn M Cooper, and Frederic Pio, and Emily P Thi, and Dave Theilmann, and Carl Lowenberger
January 1979, Fortschritte der Zoologie,
Dawn M Cooper, and Frederic Pio, and Emily P Thi, and Dave Theilmann, and Carl Lowenberger
July 2010, Insect biochemistry and molecular biology,
Dawn M Cooper, and Frederic Pio, and Emily P Thi, and Dave Theilmann, and Carl Lowenberger
January 1972, The Journal of heredity,
Dawn M Cooper, and Frederic Pio, and Emily P Thi, and Dave Theilmann, and Carl Lowenberger
January 2015, Scientific reports,
Dawn M Cooper, and Frederic Pio, and Emily P Thi, and Dave Theilmann, and Carl Lowenberger
August 2007, Insect biochemistry and molecular biology,
Copied contents to your clipboard!