Dengue-2-virus-interacting polypeptides involved in mosquito cell infection

For the design of effective antiviral strategies, understanding the fundamental steps of the virus life cycle, including virus-host interactions, is essential. We performed a virus overlay protein binding assay followed by proteomics for identification of proteins from membrane fractions of A7 (Aede...

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Bibliographic Details
Published in:Archives of virology 2010-09, Vol.155 (9), p.1453-1461
Main Authors: Paingankar, Mandar S, Gokhale, Mangesh D, Deobagkar, Dileep N
Format: Article
Language:English
Subjects:
Aedes - genetics
Aedes - metabolism
Aedes - virology
Aedes aegypti
Aedes albopictus
Animals
Biological and medical sciences
Biomedical and Life Sciences
Biomedicine
Cell Line
Dengue
Dengue fever
Dengue Virus - genetics
Dengue Virus - physiology
Dengue virus type 2
Exocrine glands
Fundamental and applied biological sciences. Psychology
Glycoproteins
Infections
Infectious Diseases
Insect Proteins - genetics
Insect Proteins - metabolism
Insect Vectors - genetics
Insect Vectors - metabolism
Insect Vectors - virology
Medical Microbiology
Microbiology
Miscellaneous
Molecular Sequence Data
Mosquitoes
Original Article
Peptides - genetics
Peptides - metabolism
Polypeptides
Proteins
Proteomics
Virology
Virulence
Virus Internalization
Zoology
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Summary:For the design of effective antiviral strategies, understanding the fundamental steps of the virus life cycle, including virus-host interactions, is essential. We performed a virus overlay protein binding assay followed by proteomics for identification of proteins from membrane fractions of A7 (Aedes aegypti) cells, C6/36 (Aedes albopictus) cells and the midgut brush border membrane fraction of Ae. aegypti mosquito that bind to dengue-2 virus. Actin, ATP synthase β subunit, HSc 70, orisis, prohibitin, tubulin β chain, and vav-1 were identified as dengue-2-virus-binding proteins. Our results suggest that dengue-2 virus exploits an array of housekeeping proteins for its entry in mosquito cells.
ISSN:0304-8608
1432-8798
DOI:10.1007/s00705-010-0728-7