Paramyxovirus Sendai virus-like particle formation by expression of multiple viral proteins and acceleration of its release by C protein

Sugahara, Fumihiro; Uchiyama, Tsuneo; Watanabe, Hitoshi; Shimazu, Yukie; Kuwayama, Masaru; Fujii, Yutaka; Kiyotani, Katsuhiro; Adachi, Akio; Kohno, Nobuoki; Yoshida, Takemi; Sakaguchi, Takemasa

doi:10.1016/j.virol.2004.04.019

Cited by 76 publications

(108 citation statements)

References 40 publications

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“…We previously reported generation of VLPs with authentic density and size by simultaneous expression of SeV proteins F, HN, M, N and C in 293T cells (18). In the VLP generation system, 25% of the viral protein was released into the medium in mock treatment, whereas treatment with 10 µM lactacystin and 10 µM MG132 decreased VLP production to 8% and 4%, respectively (Fig.…”

Section: Inhibition Of Sev-like Particle Formation By Proteasome Inhimentioning

confidence: 93%

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Cell‐Specific Inhibition of Paramyxovirus Maturation by Proteasome Inhibitors

Watanabe

Tanaka²,

Shimazu

et al. 2005

Microbiology and Immunology

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Effects of proteasome inhibitors on the replication of a paramyxovirus in comparison with the effects on replication of an orthomyxovirus and rhabdovirus were investigated. Treatment of Sendai virus (SeV)‐infected LLC‐MK2 cells with 50 μM MG132 reduced virus growth to ca. 1/10,000, and treatment with different concentrations of MG132 reduced virus growth in a dose‐dependent manner. Released amounts of viral proteins were reduced in correspondence with decrease in infectivity. The inhibition of virus maturation was confirmed by an SeV‐like particle formation system. Lactacystin also impaired SeV growth and zLL impaired the growth to a lesser extent, suggesting involvement of proteasomes in the restriction of virus growth. In the presence of MG132, localizations of the M protein and viral F and HN glycoproteins on the cell membrane appeared to be partly dissociated, although the viral glycoproteins were normally transported to the cell surface. These results suggest that an early step of SeV assembly was disturbed by proteasome inhibitors. The relationship of the results with ubiquitin is also discussed. SeV maturation was less susceptible and resistant to MG132 in CV1 cells and A549 cells, respectively, indicating cell specificity of the drug effect. Release of vesicular stomatitis virus also showed high susceptibility to MG132 and release of influenza virus A/WSN/33 was only mildly susceptible to the drug in LLC‐MK2 cells. Effects of proteasome inhibitors on virus maturation are thus highly cell‐specific and partly virus‐specific.

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Section: Inhibition Of Sev-like Particle Formation By Proteasome Inhimentioning

confidence: 93%

“…Virus-like particles (VLPs) were generated as described previously (18). Briefly, subconfluent 293T cells were transfected with plasmids for expression of SeV M, F, HN, N, and C proteins.…”

Section: Methodsmentioning

confidence: 99%

Cell‐Specific Inhibition of Paramyxovirus Maturation by Proteasome Inhibitors

Watanabe

Tanaka²,

Shimazu

et al. 2005

Microbiology and Immunology

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“…The specific residues in C protein that mediate its association with Alix have not been determined, and the way in which SeV exploits Alix may be different from that used by EIAV because C protein is not essential for viral budding. Instead, it accelerates virion production (Sugahara et al, 2004), and this is enhanced by overexpression of Alix (Sakaguchi et al, 2005).…”

Section: Enveloped Virus Buddingmentioning

confidence: 99%

The multiple personalities of Alix

Odorizzi

2006

Journal of Cell Science

166

150

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Alix is a cytosolic protein in mammalian cells that was originally identified on the basis of its association with proapoptotic signaling. More recent evidence has established that Alix has a hand in regulating other cellular mechanisms, including endocytic membrane trafficking and cell adhesion. Although Alix appears to participate directly in these various activities, the role it plays in each process has largely been inferred from the functions of proteins with which it interacts. For example, recruitment of Alix to endosomes is mediated by its N-terminal Bro1 domain, the structure of which was recently solved for its yeast orthologue, Bro1. The diversity of Alix functions is due to its proline-rich C-terminus, which provides multiple protein-binding sites. With this blueprint in hand, we can now ask whether Alix acts simply as an adaptor that links different proteins into networks or, instead, contributes a specific function to distinct molecular machineries.

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“…Expression of certain Ms in eukaryotic cells in the absence of other viral proteins can induce formation of virus-like particles (VLPs). The efficiency of VLP generation can be increased if the M is coexpressed with a viral glycoprotein (15)(16)(17)(18). Ms share a tendency to oligomerize, a feature likely to be important in the self-assembly and budding processes (19).…”

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confidence: 99%

Surface features of a Mononegavirales matrix protein indicate sites of membrane interaction

Money

McPhee²,

Mosely³

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

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The matrix protein (M) of respiratory syncytial virus (RSV), the prototype viral member of the Pneumovirinae (family Paramyxoviridae, order Mononegavirales), has been crystallized and the structure determined to a resolution of 1.6 Å. The structure comprises 2 compact ␤-rich domains connected by a relatively unstructured linker region. Due to the high degree of side-chain order in the structure, an extensive contiguous area of positive surface charge covering Ϸ600 Å 2 can be resolved. This unusually large patch of positive surface potential spans both domains and the linker, and provides a mechanism for driving the interaction of the protein with a negatively-charged membrane surface or other virion components such as the nucleocapsid. This patch is complemented by regions of high hydrophobicity and a striking planar arrangement of tyrosine residues encircling the C-terminal domain. Comparison of the RSV M sequence with other members of the Pneumovirinae shows that regions of divergence correspond to surface exposed loops in the M structure, with the majority of viral species-specific differences occurring in the N-terminal domain.CD ͉ crystal structure ͉ respiratory syncytial virus ͉ sequence alignment R espiratory syncytial virus (RSV) is the prototype member of the Pneumovirinae, a subfamily of the Paramyxoviridae (order Mononegavirales). Morphologically, the extracellular virion consists of a lipid bilayer envelope, within which are embedded 3 glycoproteins, 2 of which (F and G) are important in cell attachment and viral entry into target cells. The third, the SH protein, contributes to pathology in the host (1). Internally, virions contain helical nucleocapsids that consist of N protein tightly bound to the negative-sense nonsegmented genomic RNA. The nucleocapsid in turn is associated with components of the viral RNA-dependent RNA polymerase (L, P, M2-1, and M2-2 proteins), forming the holo-nucleocapsid (2-4). Between the holo-nucleocapsid and the outer envelope there is a layer of matrix protein (M), which is associated peripherally with the membrane (5). The other family members of the Mononegavirales (Rhabdoviridae, Filoviridae, and Bornaviridae) all subscribe to this basic arrangement of the virion, although the overall morphology can vary between the families. For example, Paramyxoviridae virions are pleiomorphic, whereas the Rhabdoviridae have a regular bullet shape structure, and the Filoviridae have a more filamentous shape. Extracellular RSV virions form by a budding process that occurs at the plasma membrane within specialized lipid domains (5, 6) and M appears to drive the final assembly process, which is the incorporation of the holo-nucleocapsid and initiation of the budding process (7,8). Before budding, there is a coordinated assembly of viral components; and it is evident that the glycoproteins and M proteins are important determinants of the location on the plasma membrane at which the virus buds (9). It is also possible that the interaction between M and the glycoproteins, possibly mediat...

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Paramyxovirus Sendai virus-like particle formation by expression of multiple viral proteins and acceleration of its release by C protein

Cited by 76 publications

References 40 publications

Cell‐Specific Inhibition of Paramyxovirus Maturation by Proteasome Inhibitors

Cell‐Specific Inhibition of Paramyxovirus Maturation by Proteasome Inhibitors

The multiple personalities of Alix

Surface features of a Mononegavirales matrix protein indicate sites of membrane interaction

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