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 431168
Title Correlation between structure, protein composition, morphogenesis and cytopathology of Glossina pallidipes salivary gland hypertrophy virus
Author(s) Kariithi, H.M.; Lent, J.W.M. van; Boeren, S.; Abd-Alla, A.M.M.; Ince, I.A.; Oers, M.M. van; Vlak, J.M.
Source Journal of General Virology 94 (2013)1. - ISSN 0022-1317 - p. 193 - 208.
DOI http://dx.doi.org/10.1099/vir.0.047423-0
Department(s) Laboratory of Virology
Biochemistry
PE&RC
Publication type Refereed Article in a scientific journal
Publication year 2013
Keyword(s) vesicular stomatitis-virus - sarcoma-associated herpesvirus - nuclear polyhedrosis-virus - occlusion-derived virus - cellular-proteins - musca-domestica - ns protein - human cytomegalovirus - transcription factor - proteomic analysis
Abstract The Glossina pallidipes salivary gland hypertrophy virus (GpSGHV) is a dsDNA virus with rod-shaped, enveloped virions. Its 190-kb genome contains 160 putative protein-coding open reading frames (ORFs). Here, structural components, protein composition and associated aspects of GpSGHV morphogenesis and cytopathology were investigated. Four morphologically distinct structures: nucleocapsid, tegument, envelope, and helical surface projections, were observed in purified GpSGHV virions by electron microscopy. Nucleocapsids were present in virogenic stroma within the nuclei of infected salivary gland cells, whereas enveloped virions were located in the cytoplasm. The cytoplasm of infected cells appeared disordered and the plasma membranes disintegrated. Treatment of virions with 1% Nonidet P-40 efficiently partitioned the virions into envelope and nucleocapsid fractions. The fractions were separated by 12% SDS-PAGE followed by in-gel trypsin digestion and analysis of the tryptic peptides by LC-MS/MS. Using the MaxQuant program with Andromeda as a database search engine, a total of forty-five viral proteins were identified. Of these, ten and fifteen were associated with the envelope and the nucleocapsid fractions respectively, while twenty were detected in both fractions, most likely representing tegument proteins. In addition, fifty-one host-derived proteins were identified in the proteome of the virus particle, thirteen of which were verified to be incorporated into the mature virion using a proteinase K protection assay. This study provides important information about GpSGHV biology and suggests options for development of future anti-GpSGHV strategies by interfering with virus-host interactions.
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