Incorporation of influenza virus M-protein into liposomes

Bucher, Doris; Kharitonenkov, I G; Zakomirdin, Juri A.; Grigoriev, V.; Klimenko, S. M.; Davis, James F.

doi:10.1128/jvi.36.2.586-590.1980

Cited by 85 publications

(38 citation statements)

References 15 publications

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“…wt = 27 861 (Winter and Fields, 1980)] is the only protein component of the thick protein-lipid lining coupled to the outer single phospholipid layer. Interaction of M protein with lipid bilayer membranes and the resulting modification of the membrane structure have been reported (Bucher et al, 1980;Gregoriades, 1980). We sometimes detected apparently intermediate structures of membranes in which 3.8 or 5.3 nm thick proteinaceous material was intimately attached to the inner leaflet of a lipid bilayer (Figure 3a).…”

Section: Density Profiles Of the Viral Envelopesmentioning

confidence: 57%

Fine structure of influenza A virus observed by electron cryo-microscopy.

et al. 1994

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A rapidly frozen vitrified aqueous suspension of influenza A virus was observed by high resolution electron cryomicroscopy. The influenza particles were grouped into small (diameter < 150 nm) spherical particles with well organized interiors, large spherical ones with less internal organization, and framentous ones. Envelopes of most of the large virus particles were phospholipid bilayers, and the chromatography fraction containing these large particles was largely devoid of viral activity. The envelopes of most of the fiamentous and small spherical virus particles, on the other hand, gave a strange contrast which could be ascribed to a combination of a thin outer lipid monolayer and a 7.2 nm thick protein-containing inner layer. These latter particles represented most of the viral activity in the preparation. Densitometric traces of the near in-focus images confimed these structural differences. Some viral envelope structures apparently intermediate between these two distinct types of membrane were also detected. A structural model of intact biologically active influenza virus particles was formulated from these results, together with computer simulations.

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Section: Density Profiles Of the Viral Envelopesmentioning

confidence: 57%

Fine structure of influenza A virus observed by electron cryo-microscopy.

et al. 1994

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“…However, experiments to demonstrate direct interaction of HA and NA with M1 yielded contradictory results. Since a significant fraction of M1 alone was shown to bind membrane (Bucher et al, 1980;Gregoriades and Frangione, 1981;Hay, 1974;Ruigrok et al, 2000), coexpression of M1 with HA and NA did not significantly increase the membrane association of M1 (Kretzschmar et al, 1996;Zhang and Lamb, 1996). However, in one report, the HA and NA CTs have been shown to stimulate the membrane association of the M1 protein (Enami and Enami, 1996), and short synthetic peptides of the HA cytoplasmic sequence inhibited virus production (Collier et al, 1991).…”

Section: Interaction Of M1 With Envelope Proteinsmentioning

confidence: 95%

Assembly and budding of influenza virus

Nayak¹,

Hui²,

Barman³

2004

Virus Research

295

262

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Influenza viruses are causative agents of an acute febrile respiratory disease called influenza (commonly known as "flu") and belong to the Orthomyxoviridae family. These viruses possess segmented, negative stranded RNA genomes (vRNA) and are enveloped, usually spherical and bud from the plasma membrane (more specifically, the apical plasma membrane of polarized epithelial cells). Complete virus particles, therefore, are not found inside infected cells. Virus particles consist of three major subviral components, namely the viral envelope, matrix protein (M1), and core (viral ribonucleocapsid [vRNP]). The viral envelope surrounding the vRNP consists of a lipid bilayer containing spikes composed of viral glycoproteins (HA, NA, and M2) on the outer side and M1 on the inner side. Viral lipids, derived from the host plasma membrane, are selectively enriched in cholesterol and glycosphingolipids. M1 forms the bridge between the viral envelope and the core. The viral core consists of helical vRNP containing vRNA (minus strand) and NP along with minor amounts of NEP and polymerase complex (PA, PB1, and PB2). For viral morphogenesis to occur, all three viral components, namely the viral envelope (containing lipids and transmembrane proteins), M1, and the vRNP must be brought to the assembly site, i.e. the apical plasma membrane in polarized epithelial cells. Finally, buds must be formed at the assembly site and virus particles released with the closure of buds. Transmembrane viral proteins are transported to the assembly site on the plasma membrane via the exocytic pathway. Both HA and NA possess apical sorting signals and use lipid rafts for cell surface transport and apical sorting. These lipid rafts are enriched in cholesterol, glycosphingolipids and are relatively resistant to neutral detergent extraction at low temperature. M1 is synthesized on free cytosolic polyribosomes. vRNPs are made inside the host nucleus and are exported into the cytoplasm through the nuclear pore with the help of M1 and NEP. How M1 and vRNPs are directed to the assembly site on the plasma membrane remains unclear. The likely possibilities are that they use a piggy-back mechanism on viral glycoproteins or cytoskeletal elements. Alternatively, they may possess apical determinants or diffuse to the assembly site, or a combination of these pathways. Interactions of M1 with M1, M1 with vRNP, and M1 with HA and NA facilitate concentration of viral components and exclusion of host proteins from the budding site. M1 interacts with the cytoplasmic tail (CT) and transmembrane domain (TMD) of glycoproteins, and thereby functions as a bridge between the viral envelope and vRNP. Lipid rafts function as microdomains for concentrating viral glycoproteins and may serve as a platform for virus budding. Virus bud formation requires membrane bending at the budding site. A combination of factors including concentration of and interaction among viral components, increased viscosity and asymmetry of the lipid bilayer of the lipid raft as well as pulling and pushi...

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“…The hydropathy pattern of mumps virus and VSV matrix proteins did not have any obvious similarities with that of hRSV M protein, but all three showed a common region of low hydrophobicity at the N-terminus, followed by a gradual increase in hydrophobic value towards the C-terminus. The length of the hydrophobic regions was less than the minimum length required to form a transmembrane domain, but may mediate peripheral attachment to the host cell membrane [11].…”

Section: Introductionmentioning

confidence: 98%

Sequence and structure relatedness of matrix protein of human respiratory syncytial virus with matrix proteins of other negative-sense RNA viruses

Latiff

Meanger

Mills

et al. 2004

Clinical Microbiology and Infection

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Matrix proteins of viruses within the order Mononegavirales have similar functions and play important roles in virus assembly. Protein sequence alignment, phylogenetic tree derivation, hydropathy profiles and secondary structure prediction were performed on selected matrix protein sequences, using human respiratory syncytial virus matrix protein as the reference. No general conservation of primary, secondary or tertiary structure was found, except for a broad similarity in the hydropathy pattern correlating with the fact that all the proteins studied are membrane-associated. Interestingly, the matrix proteins of Ebola virus and human respiratory syncytial virus shared secondary structure homology.

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Incorporation of influenza virus M-protein into liposomes

Cited by 85 publications

References 15 publications

Fine structure of influenza A virus observed by electron cryo-microscopy.

Fine structure of influenza A virus observed by electron cryo-microscopy.

Assembly and budding of influenza virus

Sequence and structure relatedness of matrix protein of human respiratory syncytial virus with matrix proteins of other negative-sense RNA viruses

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