Influenza type A virus neuraminidase does not play a role in viral entry, replication, assembly, or budding

Liu, Chongguang; Eichelberger, Maryna C.; Compans, Richard W.; Air, Gillian M.

doi:10.1128/jvi.69.2.1099-1106.1995

Cited by 340 publications

(170 citation statements)

References 20 publications

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“…Thus, the bat-derived H17 and H18 are unique among the characterized HAs and might use a different entry mechanism. NA-like molecules N10 and N11 are not sialidases NA is the second virus-surface envelope protein and is a sialidase, responsible for cleavage of SA from glycans on the host cell surface to release the emerging progeny virus, prevent virus aggregation, and help virus migration [45,46]. Therefore it has an opposite function from HA, SA-binding versus SA-releasing.…”

Section: Reviewmentioning

confidence: 99%

Bat-derived influenza-like viruses H17N10 and H18N11

Tefsen

et al. 2014

Trends in Microbiology

305

224

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Shorebirds and waterfowls are believed to be the reservoir hosts for influenza viruses, whereas swine putatively act as mixing vessels. The recent identification of two influenza-like virus genomes (designated H17N10 and H18N11) from bats has challenged this notion. A crucial question concerns the role bats might play in influenza virus ecology. Structural and functional studies of the two major surface envelope proteins, hemagglutinin (HA) and neuraminidase (NA), demonstrate that neither has canonical HA or NA functions found in influenza viruses. However, putative functional modules and domains in other encoded proteins are conserved, and the N-terminal domain of the H17N10 polymerase subunit PA has a classical structure and function. Therefore, potential genomic reassortments of such influenza-like viruses with canonical influenza viruses cannot be excluded at this point and should be assessed.

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Section: Reviewmentioning

confidence: 99%

Bat-derived influenza-like viruses H17N10 and H18N11

Tefsen

et al. 2014

Trends in Microbiology

305

224

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“…Neither HA nor NA is absolutely required for virus budding, since virus particles lacking either HA or NA can bud in HA or NA temperature sensitive (ts) mutants at the restrictive temperature (Palese et al, 1974;Pattnaik et al, 1986). Besides, virus budding has been shown to occur in the absence of NA (Liu et al, 1995). On the other hand, virus budding does not occur in the absence of M1, and M1 expressed alone can form virus-like particles in transfected cells (Gómez-Puertas et al, 2000;Latham and Galarza, 2001).…”

Section: Transport Of M1 and Vrnp To The Assembly Sitementioning

confidence: 99%

Assembly and budding of influenza virus

Nayak¹,

Hui²,

Barman³

2004

Virus Research

308

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 RDE activity prevents the viruses from self-aggregation and promotes release of viral progenies from the infected cell (Höfling et al, 1996;Liu et al, 1995). In addition, the RDE may also play a role early during infection (Brossmer et al, 1993;Huang et al, 1985;Matrosovich et al, 2004;Ohuchi et al, 1995;Strobl and Vlasak, 1993).…”

Section: Introductionmentioning

confidence: 99%

Structural and functional analysis of the hemagglutinin-esterase of infectious salmon anaemia virus

et al. 2010

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Infectious salmon anaemia virus (ISAV) is a piscine orthomyxovirus causing a serious disease in farmed Atlantic salmon (Salmo salar L.). The virus surface glycoprotein hemagglutinin-esterase (HE) is responsible for both viral attachment and release. Similarity to bovine and porcine torovirus hemagglutinin-esterase (BToV HE, PToV HE), bovine coronavirus HE (BCoV HE) and influenza C hemagglutinin-esterase-fusion (InfC HEF) proteins were exploited in a computational homology-based structure analysis of ISAV HE. The analysis resolved structural aspects of the protein and identified important features of relevance to ISAV HE activity. By recombinant expression and purification of secretory HE (recHE) proteins, receptor-binding and quantitative analyses of enzymatic activities displayed by ISAV HE molecules are presented for the first time. Three different recHE molecules were constructed: one representing a high virulent isolate, one a low virulent, while in the third a Ser(32) to Ala(32) amino acid substitution was introduced in the enzymatic catalytic site as inferred from the model. The three amino acid differences between the high and low virulent variants, of which two localized to the putative receptor-binding domain and one in the esterase domain, had no impact on receptor-binding or -release activities. In contrast, the Ser(32) amino acid substitution totally abolished enzymatic activity while receptor binding increased, as observed by agglutination of Atlantic salmon red blood cells. This demonstrates the essential role of a serine in the enzyme's catalytic site. In conclusion, structural analysis of ISAV HE in combination with selected recHE proteins gave insights into structure-function relationships and opens up for further studies aiming at dissecting molecular determinants of ISAV virulence.

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Influenza type A virus neuraminidase does not play a role in viral entry, replication, assembly, or budding

Cited by 340 publications

References 20 publications

Bat-derived influenza-like viruses H17N10 and H18N11

Bat-derived influenza-like viruses H17N10 and H18N11

Assembly and budding of influenza virus

Structural and functional analysis of the hemagglutinin-esterase of infectious salmon anaemia virus

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