About: Influenza virus morphogenesis and budding

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An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Influenza virus morphogenesis and budding
Creator	Zhou, Hong Barman, Subrata Yamada, Hiroshi Nayak, Debi Balogun, Rilwan
Source	Elsevier; Medline; PMC
abstract	Influenza viruses are enveloped, negative stranded, segmented RNA viruses belonging to Orthomyxoviridae family. Each virion consists of three major subviral components, namely (i) a viral envelope decorated with three transmembrane proteins hemagglutinin (HA), neuraminidase (NA) and M2, (ii) an intermediate layer of matrix protein (M1), and (iii) an innermost helical viral ribonucleocapsid [vRNP] core formed by nucleoprotein (NP) and negative strand viral RNA (vRNA). Since complete virus particles are not found inside the cell, the processes of assembly, morphogenesis, budding and release of progeny virus particles at the plasma membrane of the infected cells are critically important for the production of infectious virions and pathogenesis of influenza viruses as well. Morphogenesis and budding require that all virus components must be brought to the budding site which is the apical plasma membrane in polarized epithelial cells whether in vitro cultured cells or in vivo infected animals. HA and NA forming the outer spikes on the viral envelope possess apical sorting signals and use exocytic pathways and lipid rafts for cell surface transport and apical sorting. NP also has apical determinant(s) and is probably transported to the apical budding site similarly via lipid rafts and/or through cortical actin microfilaments. M1 binds the NP and the exposed RNAs of vRNPs, as well as to the cytoplasmic tails (CT) and transmembrane (TM) domains of HA, NA and M2, and is likely brought to the budding site on the piggy-back of vRNP and transmembrane proteins. Budding processes involve bud initiation, bud growth and bud release. Presence of lipid rafts and assembly of viral components at the budding site can cause asymmetry of lipid bilayers and outward membrane bending leading to bud initiation and bud growth. Bud release requires fusion of the apposing viral and cellular membranes and scission of the virus buds from the infected cellular membrane. The processes involved in bud initiation, bud growth and bud scission/release require involvement both viral and host components and can affect bud closing and virus release in both positive and negative ways. Among the viral components, M1, M2 and NA play important roles in bud release and M1, M2 and NA mutations all affect the morphology of buds and released viruses. Disassembly of host cortical actin microfilaments at the pinching-off site appears to facilitate bud fission and release. Bud scission is energy dependent and only a small fraction of virus buds present on the cell surface is released. Discontinuity of M1 layer underneath the lipid bilayer, absence of outer membrane spikes, absence of lipid rafts in the lipid bilayer, as well as possible presence of M2 and disassembly of cortical actin microfilaments at the pinching off site appear to facilitate bud fission and bud release. We provide our current understanding of these important processes leading to the production of infectious influenza virus particles.
has issue date	2009-08-01(xsd:dateTime)
bibo:doi	10.1016/j.virusres.2009.05.010
bibo:pmid	19481124
has license	green-oa
sha1sum (hex)	c90acbf3fb15e35889f2e2cba93f0c963287be0c
schema:url	https://doi.org/10.1016/j.virusres.2009.05.010
resource representing a document's title	Influenza virus morphogenesis and budding
has PubMed Central identifier	PMC2730999
has PubMed identifier	19481124
schema:publication	Virus Research
resource representing a document's body	covid:c90acbf3fb15e35889f2e2cba93f0c963287be0c#body_text
is schema:about of	named entity 'strand' named entity 'cells' named entity 'site' named entity 'spikes' named entity 'budding' named entity 'viral' named entity 'processes' named entity 'VIRUS' named entity 'NOT FOUND' named entity 'APICAL' named entity 'MORPHOGENESIS' named entity 'CULTURED CELLS' named entity 'SPIKES' named entity 'SORTING' named entity 'NEGATIVE STRAND' named entity 'MICROFILAMENTS' named entity 'VIRAL COMPONENTS' named entity 'INFECTIOUS' named entity 'INTERMEDIATE' named entity 'THE CELL' named entity 'INFECTED' named entity 'CORTICAL' named entity 'IN VITRO' named entity 'OUTER' named entity 'NEURAMINIDASE' named entity 'CELL SURFACE' named entity '28I' named entity 'INFLUENZA VIRUSES' named entity 'SEGMENTED ' named entity 'TRANSPORT' named entity 'RNAS' named entity 'BINDS' named entity 'PLASMA MEMBRANE' named entity 'MATRIX PROTEIN' named entity 'TAILS' named entity 'VIRION' named entity 'FORMING' named entity 'BELONGING' named entity 'MAJOR' named entity 'SITE' named entity 'INSIDE' named entity 'FAMILY' named entity 'PATHOGENESIS' named entity 'DECORATED' named entity 'SIGNALS' named entity 'USE' named entity 'INFLUENZA VIRUS' named entity 'HEMAGGLUTININ' named entity 'VIRIONS' named entity 'LIPID RAFTS' named entity 'RELEASE' named entity 'PROCESSES' named entity 'PROBABLY' named entity 'LAYER' named entity 'FORMED' named entity 'COMPONENTS' named entity 'EXPOSED' named entity 'COMPLETE' named entity 'ORTHOMYXOVIRIDAE' named entity 'BACK OF' named entity 'CORE' named entity 'BROUGHT' named entity 'MORPHOGENESIS' named entity 'BUDDING' named entity 'TRANSMEMBRANE PROTEINS' named entity 'CYTOPLASMIC' named entity 'NUCLEOPROTEIN' named entity 'BUDDING' named entity 'TRANSMEMBRANE' named entity 'APICAL PLASMA MEMBRANE' named entity 'RNA VIRUSES' named entity 'ASSEMBLY' named entity 'VIRAL RNA' named entity 'EPITHELIAL CELLS' named entity 'NEGATIVE' named entity 'VIRAL' named entity 'POSSESS'

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