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ARS Home » Plains Area » Manhattan, Kansas » Center for Grain and Animal Health Research » ABADRU » Research » Publications at this Location » Publication #285640
Title: Rift Valley fever virus incorporates the 78kDa glycoprotein into virions matured in C6/36 2 mosquito cells

Author
item WEINGARTL, HANA - Canadian Food Inspection Agency
item ZHANG, SHUNZHEN - Canadian Food Inspection Agency
item MARSZAL, PETER - Canadian Food Inspection Agency
item MCVREEVY, ALAN - University Of Manitoba
item BURTON, LYNN - Canadian Food Inspection Agency
item Wilson, William

Submitted to: Journal of Virology
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 12/1/2014
Publication Date: 1/1/2014
Publication URL: http://doi:10.1371/journal.pone.0087385
Citation: Weingartl, H.M., Zhang, S., Marszal, P., Mcvreevy, A., Burton, L., Wilson, W.C. 2014. Rift Valley fever virus incorporates the 78kDa glycoprotein into virions matured in C6/36 2 mosquito cells. Journal of Virology. 9(1):e87385.

Interpretive Summary: The mosquito-borne virus, Rift Valley fever virus (RVFV) is able to transition between distant host species, causing potentially severe disease in humans and ruminants. This paper describes the first report of different protein composition between virus formed in insect versus mammalian cells. This difference may be important in the ability of the virus to replicate in the diverse hosts and/or be transmitted from the mosquito to the vertebrate host. Understanding this finding could lead to better control strategies for this pathogen of agricultural and public health concern.

Technical Abstract: Rift Valley fever virus (RVFV), genus Phlebovirus, family Bunyaviridae is a zoonotic arthropod-borne virus able to transition between distant host species, causing potentially severe disease in humans and ruminants. Viral proteins are encoded by three genomic segments, with the medium M segment coding for four proteins: nonstructural NSm protein, two glycoproteins Gn and Gc and large 78 kDa glycoprotein (LGp) of unknown function. Rabbit polyclonal antibody and mouse monoclonal antibody generated against a polypeptide unique to the LGp detected this protein in gradient purified RVFV ZH 501 virions harvested from mosquito C6/36 cells but not in virions harvested from the mammalian Vero E6 cells. The LGp was incorporated into the virions immediately during the first passage in C6/36 cells of Vero E6 derived virus, and the incorporation of LGp into the mosquito cell line generated virions was confirmed by immune-electron microscopy. Our data indicate that LGp is a structural protein in mosquito cell generated virions with a possible role in replication of RVFV in the mosquito host, and may aid the transmission from the mosquitoes to the ruminant host. To our knowledge, this is a first report of different protein composition between virions formed in insect versus mammalian cells.