Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 421065
Title Low Temperature-Dependent Salmonid Alphavirus Glycoprotein Processing and Recombinant Virus-Like Particle Formation
Author(s) Metz, S.W.H.; Feenstra, F.; Villoing, S.; Hulten, M.C. van; Lent, J.W.M. van; Koumans, J.; Vlak, J.M.; Pijlman, G.P.
Source PLoS One 6 (2011)10. - ISSN 1932-6203 - 10 p.
DOI http://dx.doi.org/10.1371/journal.pone.0025816
Department(s) Laboratory of Virology
PE&RC
Publication type Refereed Article in a scientific journal
Publication year 2011
Keyword(s) semliki-forest-virus - equine encephalitis-virus - nuclear polyhedrosis-virus - swine-fever virus - pancreas disease - atlantic salmon - spodoptera-frugiperda - nucleocapsid protein - baculovirus vectors - sleeping-disease
Abstract Pancreas disease (PD) and sleeping disease (SD) are important viral scourges in aquaculture of Atlantic salmon and rainbow trout. The etiological agent of PD and SD is salmonid alphavirus (SAV), an unusual member of the Togaviridae (genus Alphavirus). SAV replicates at lower temperatures in fish. Outbreaks of SAV are associated with large economic losses of ~17 to 50 million $/year. Current control strategies rely on vaccination with inactivated virus formulations that are cumbersome to obtain and have intrinsic safety risks. In this research we were able to obtain non-infectious virus-like particles (VLPs) of SAV via expression of recombinant baculoviruses encoding SAV capsid protein and two major immunodominant viral glycoproteins, E1 and E2 in Spodoptera frugiperda Sf9 insect cells. However, this was only achieved when a temperature shift from 27°C to lower temperatures was applied. At 27°C, precursor E2 (PE2) was misfolded and not processed by host furin into mature E2. Hence, E2 was detected neither on the surface of infected cells nor as VLPs in the culture fluid. However, when temperatures during protein expression were lowered, PE2 was processed into mature E2 in a temperature-dependent manner and VLPs were abundantly produced. So, temperature shift-down during synthesis is a prerequisite for correct SAV glycoprotein processing and recombinant VLP production
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