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 359510
Title Baculovirus envelope fusion proteins F and GP64 exploit distinct receptors to gain entry into cultured insect cells
Author(s) Westenberg, M.; Uijtdewilligen, P.; Vlak, J.M.
Source Journal of General Virology 88 (2007). - ISSN 0022-1317 - p. 3302 - 3306.
Department(s) Laboratory of Virology
Publication type Refereed Article in a scientific journal
Publication year 2007
Keyword(s) nuclear polyhedrosis-virus - californica multicapsid nucleopolyhedrovirus - membrane-fusion - recombinant baculovirus - lymantria-dispar - mammalian-cells - genome sequence - lines - glycoprotein - mechanism
Abstract Group II nucleopolyhedroviruses (NPVs), e.g. Helicoverpa armigera (Hear) NPV and Spodoptera exigua (Se) MNPV (multiple NPV), lack a GP64-like protein that is present in group I NPVs, e.g. Autographa californica (Ac)MNPV, but have an unrelated envelope fusion protein named F. Three AcMNPV viruses were constructed by introducing AcMNPV gp64, HearNPV f or SeMNPV f genes, respectively, into a gp64-negative AcMNPV bacmid. Sf21 cells were incubated with different amounts of inactivated budded virus to occupy receptors and were subsequently infected with a fixed amount of infectious virus to compete for attachment. The results suggest that GP64 and F act on their own and use different receptors, while the two different F proteins exploit the same receptor. Additionally, gp64-null AcMNPV pseudotyped with baculovirus F was, in contrast to GP64, unable to transduce mammalian cells, indicating that mammalian cells do not possess baculovirus F protein receptors despite the structural similarity of baculovirus F to vertebrate viral fusion proteins.
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