Do lipid rafts mediate virus assembly and pseudotyping?

Briggs, John; Wilk, Thomas; Fuller, Stephen D.

doi:10.1099/vir.0.18779-0

Cited by 113 publications

(76 citation statements)

References 126 publications

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“…However, the generated virions were not infectious (Shioda & Shibuta, 1990). Budding of retroviruses seems to occur at ordered lipid microdomains, called lipid rafts (Briggs et al, 2003). It is possible that, when expressed in mammalian cells, GP64 may end up in these lipid rafts and thereby in the envelope of lentiviruses.…”

Section: Discussionmentioning

confidence: 99%

GP64 of group I nucleopolyhedroviruses cannot readily rescue infectivity of group II f-null nucleopolyhedroviruses

Westenberg

Vlak

2008

Journal of General Virology

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The genus Nucleopolyhedrovirus (NPV) of the family Baculoviridae can be subdivided phylogenetically into two groups. The same division can be made on the basis of their budded virus (BV) envelope fusion protein. Group I NPVs are characterized by the presence of a GP64-like major envelope fusion protein, which is involved in viral attachment and the fusion of virus and cell membrane, and is required for budding of progeny nucleocapsids. Group II NPVs have an envelope fusion protein unrelated to GP64, named F. In contrast to GP64, F proteins are found in all baculoviruses, but they are not functional as envelope fusion proteins in group I NPVs. Autographa californica multiple NPV (AcMNPV) lacking GP64 can be pseudotyped by the F protein of Spodoptera exigua multiple NPV (SeMNPV), suggesting that F proteins are functionally analogous to GP64. GP64 homologues are thought to have been acquired by group I NPVs during evolution, thereby giving these viruses a selective advantage and obviating the need for a functional F protein. To address this supposition experimentally, attempts were made to pseudotype a group II NPV, SeMNPV, with GP64. Transfection of an f-null SeMNPV bacmid into Se301 cells did not result in the production of infectious BVs. This defect was rescued by insertion of SeMNPV f, but not by insertion of AcMNPV gp64. This suggests that the functional analogy between GP64 and F is not readily reciprocal and that F proteins from group II NPVs may provide additional functions in BV formation that are lacking in the GP64 type of fusion protein.

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Section: Discussionmentioning

confidence: 99%

GP64 of group I nucleopolyhedroviruses cannot readily rescue infectivity of group II f-null nucleopolyhedroviruses

Westenberg

Vlak

2008

Journal of General Virology

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“…As mentioned previously, they have been suggested as the site of viral assembly for certain enveloped viruses e.g. HIV-1 (Briggs et al 2003;D. H. Nguyen and Hildreth 2000).…”

Section: Glycosylphosphatidylinositol (Gpi) Modificationmentioning

confidence: 99%

“…The mechanisms behind pseudotyping are believed to be related to the presence of membrane subdomains in cellular membranes which function as sites for viral assembly and/or budding of a range of different viral species (Briggs et al 2003;Metzner et al 2008a;Pickl et al 2001). Since viruses from quite different taxonomical origins are assembled at such sites, incorporation of proteins from different virus backgrounds can occur.…”

Section: Viral Surfacementioning

confidence: 99%

“…Thus, this may constitute a type 2 incorporation. The co-localisation of molecules at membrane microdomains may also form the framework for pseudotyping events (Briggs et al 2003;Metzner et al 2008a;Pickl et al 2001) (see section 2.2.). Discriminating between type 2 and type 3 incorporation events may be difficult, since directed co-localisation is not easy to demonstrate and the concept of membrane microdomains is controversial (Shaw 2006).…”

Section: Introduction -Proteins Of Retroviral Surfacesmentioning

confidence: 99%

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Surface Modification of Retroviral Vectors for Gene Therapy

Metzner¹,

Dangerfield²

2011

Viral Gene Therapy

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“…Membrane lipids are active players in the complex process of retroviral assembling, and pseudotyping that takes place at the host cell membrane, in which interactions of membrane lipid rafts select both envelope and core proteins, recruiting later the other viral components by cooperative interaction. The production of infectious particles is known to rely on the efficiency of this process, which is dependent upon a delicate equilibrium of lipid type and amounts, easily disturbed by lipid deprivation (Briggs et al 2003). Therefore, changes in serum concentration that disturb cell membrane lipid composition will ultimately affect viral particle membrane properties (Rawat et al 2003) possibly resulting in a higher production of non-infectious particles.…”

Section: Serum Supplemented Vs Serum-free Mediamentioning

confidence: 99%