Influenza virus hemagglutinin and neuraminidase glycoproteins stimulate the membrane association of the matrix protein

Enami, Masayoshi; Enami, Kazue

doi:10.1128/jvi.70.10.6653-6657.1996

Cited by 129 publications

(60 citation statements)

References 53 publications

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“…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). Subsequently, Triton X-100 (TX-100) detergent treatment at low temperature was used to demonstrate the specific interaction of M1 with both HA and NA (Ali et al, 2000).…”

Section: Interaction Of M1 With Envelope Proteinsmentioning

confidence: 90%

Assembly and budding of influenza virus

Nayak¹,

Hui²,

Barman³

2004

Virus Research

309

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 Envelope Proteinsmentioning

confidence: 90%

Assembly and budding of influenza virus

Nayak¹,

Hui²,

Barman³

2004

Virus Research

309

262

View full text Add to dashboard Cite

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“…Overexpression of M1 in eukaryotic cells leads to the formation of intracellular tubular structures and the release of virus-like particles (VLPs), indicating that M1 contains all the information for assembly and budding [49]. VLP formation, however, is also enhanced by coexpression of HA which might augment M1 membrane association [49,50]. Although M1 has a high tendency to polymerise in vitro, its conformation upon cytoplasmic expression must be postulated to be monomeric as cytoplasmic and nuclear M1 pools have been reported in addition to membrane associated M1 [51,52].…”

Section: Influenza Virus M1mentioning

confidence: 99%

Structural studies on the Ebola virus matrix protein VP40 indicate that matrix proteins of enveloped RNA viruses are analogues but not homologues

Timmins

Ruigrok

Weissenhorn

2004

FEMS Microbiology Letters

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Matrix proteins are the driving force of assembly of enveloped viruses. Their main function is to interact with and polymerize at cellular membranes and link other viral components to the matrix-membrane complex resulting in individual particle shapes and ensuring the integrity of the viral particle. Although matrix proteins of different virus families show functional analogy, they share no sequence or structural homology, Their diversity is also evident in that they use a variety of late domain motifs to commit the cellular vacuolar protein sorting machinery to virus budding. Here, we discuss the structural and functional aspects of teh filovirus matrix protein VP40 and compare them to other known matrix protein structures from vesicular stomatitis virus adn retroviral matrix protein.

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“…In contrast, the mechanism responsible for the transport of the viral proteins which form the inside of the virion to the apical budding surfaces of the infected cells is poorly understood. For example, the role of the HA, NA, and M2 proteins in the localization of the viral matrix protein, M1, which lies underneath the viral envelope, is unclear (10,25,67). Interestingly, it appears that M1 interactions with HA and NA mediate the association of M1 with detergent-resistant membranes (2,4,69).…”

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confidence: 99%