Influence of membrane (M) protein on influenza A virus virion transcriptase activity in vitro and its susceptibility to rimantadine

Zvonarjev, A Y; Ghendon, Y. Z.

doi:10.1128/jvi.33.2.583-586.1980

Cited by 88 publications

(32 citation statements)

References 12 publications

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“…Virion structure implies that M1 acts as a bridge between the envelope and the vRNP and therefore must interact with both the viral envelope on the outer side and the vRNP on the inner side. As stated earlier, M1 was shown to interact with viral NEP (Akarsu et al, 2003;Ward et al, 1995;Yasuda et al, 1993), and vRNPs (Watanabe et al, 1996;Ye et al, 1999;Zvonarjev and Ghendon, 1980). The M1-vRNP complex can be isolated from either infected cells or purified virions by non-ionic detergent treatment under conditions where membrane glycoproteins are dissociated.…”

Section: Interaction Of M1 With Vrnp and M1 With M1mentioning

confidence: 76%

Assembly and budding of influenza virus

Nayak¹,

Hui²,

Barman³

2004

Virus Research

310

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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Section: Interaction Of M1 With Vrnp and M1 With M1mentioning

confidence: 76%

Assembly and budding of influenza virus

Nayak¹,

Hui²,

Barman³

2004

Virus Research

310

262

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“…It is conceivable that synthesis of the Ml protein is delayed because this protein may be involved in the transition between the early and late phases of viral infection, i.e., in stopping the transcription of vRNA into viral mRNA. The matrix (M) protein of another negative-strand RNA virus, vesicular stomatitis virus, has been implicated in the shut-down of viral RNA transcription (6,9,11,33), and the influenza virus Ml protein has been shown to inhibit viral RNA transcription in vitro (42).…”

Section: Short Pulses (3 Min) With [3h]uridine and Nonaqueousmentioning

confidence: 99%

Influenza virus gene expression: control mechanisms at early and late times of infection and nuclear-cytoplasmic transport of virus-specific RNAs

Shapiro¹,

Gurney²,

Krug³

1987

J Virol

170

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Single-stranded M13 DNAs specific for various influenza virus genomic segments were used to analyze the synthesis of virus-specific RNAs in infected cells. The results show that influenza virus infection is divided into two distinct phases. During the early phase, the syntheses of specific virion RNAs, viral mRNAs, and viral proteins were coupled. Thus, the NS (nonstructural) virion RNA was preferentially synthesized early, leading to the preferential synthesis of NS1 viral mRNA and NS1 protein; in contrast, M (matrix) RNA synthesis was delayed, leading to the delayed synthesis of Ml viral mRNA and Ml protein. This phase lasted for 2.5 h in BHK-21 cells, the time at which the rate of synthesis of all the viral mRNAs was maximal. During the second phase, the synthesis of all the virion RNAs remained at or near maximum until at least 5.5 h postinfection, whereas the rate of synthesis of all the viral mRNAs declined dramatically. By 4.5 h, the rate of synthesis of all the viral mRNAs was 5% of the maximum rate. Viral mRNA and protein syntheses were also not coupled, as the synthesis of all the viral proteins continued at maximum levels, indicating that protein synthesis during this phase was directed prinicipally by previously synthesized viral mRNAs. Short pulses (3 min) with [3H]uridine and nonaqueous fractionation of cells were used to show that influenza virion RNA synthesis occurred in the nucleus, demonstrating that all virus-specific RNA synthesis was nuclear. Virion RNAs, like viral mRNAs, were efficiently transported to the cytoplasm at both early and late times of infection. In contrast, the full-length transcripts of the virion RNAs, which are the templates for virion RNA synthesis, were sequestered in the nucleus. Thus, the template RNAs, which were synthesized only at early times, remained in the nucleus to direct virion RNA synthesis throughout infection. These results enabled us to present an overall scheme for the control of influenza virus gene expression.

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“…The M1 protein harbours an N-terminal (N) domain (aa 2-67), a middle (M) domain (aa 91-158) and a C-terminal (C) domain (aa 165-252) (Sha and Luo, 1997). The M domain (aa 91-158) of M1 provides multiple functional domains including a nuclear localization signal, nuclear export protein binding motif, a RNA-RNP binding site, transcription inhibition motifs and self-association domain (Zvonarjev andGhendon, 1980, Ye et al, 1989;Ye et al, 1995, Perez and Donis, 1998, Zhao et al, 1998Harris et al, 2001;Akarsu et al, 2003). M1 self-association is critical in many aspects of virus assembly and budding (reviewed in Nayak et al, 2004).…”

Section: Introductionmentioning

confidence: 99%