About: Evidence for the interaction of the human metapneumovirus G and F proteins during virus-like particle formation

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About: Evidence for the interaction of the human metapneumovirus G and F proteins during virus-like particle formation Goto Sponge NotDistinct Permalink

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
title	Evidence for the interaction of the human metapneumovirus G and F proteins during virus-like particle formation
Creator	Fu, Yi Sugrue, Richard Ayi, Teck Jumat, Muhammad Loo, Liat Tan, Boon Tee, Nancy Wong, Pui
source	Medline; PMC
abstract	BACKGROUND: Human metapneumovirus (HMPV) is now a major cause of lower respiratory infection in children. Although primary isolation of HMPV has been achieved in several different cell lines, the low level of virus replication and the subsequent recovery of low levels of infectious HMPV have hampered biochemical studies on the virus. These experimental methodologies usually require higher levels of biological material that can be achieved following HMPV infection. In this study we demonstrate that expression of the HMPV F, G and M proteins in mammalian cells leads to HMPV virus-like particles (VLP) formation. This experimental strategy will serve as a model system to allow the process of HMPV virus assembly to be examined. METHODS: The HMPV F, G and M proteins were expressed in mammalian cell lines. Protein cross-linking studies, sucrose gradient centrifugation and in situ imaging was used to examine interactions between the virus proteins. VLP formation was examined using sucrose density gradient centrifugation and electron microscopy analysis. RESULTS: Analysis of cells co-expressing the F, G and M proteins demonstrated that these proteins interacted. Furthermore, in cells co-expression the three HMPV proteins the formation VLPs was observed. Image analysis revealed the VLPs had a similar morphology to the filamentous virus morphology that we observed on HMPV-infected cells. The capacity of each protein to initiate VLP formation was examined using a VLP formation assay. Individual expression of each virus protein showed that the G protein was able to form VLPs in the absence of the other virus proteins. Furthermore, co-expression of the G protein with either the M or F proteins facilitated their incorporation into the VLP fraction. CONCLUSION: Co-expression of the F, G and M proteins leads to the formation of VLPs, and that incorporation of the F and M proteins into VLPs is facilitated by their interaction with the G protein. Our data suggests that the G protein plays a central role in VLP formation, and further suggests that the G protein may also play a role in the recruitment of the F and M proteins to sites of virus particle formation during HMPV infection.
has issue date	2013-09-25(xsd:dateTime)
bibo:doi	10.1186/1743-422x-10-294
bibo:pmid	24067107
has license	cc-by
sha1sum (hex)	adbb0a486cf43c474df8b8b86fa6eacd422b171c
schema:url	https://doi.org/10.1186/1743-422x-10-294
resource representing a document's title	Evidence for the interaction of the human metapneumovirus G and F proteins during virus-like particle formation
has PubMed Central identifier	PMC3849350
has PubMed identifier	24067107
schema:publication	Virol J
resource representing a document's body	covid:adbb0a486cf43c474df8b8b86fa6eacd422b171c#body_text
is schema:about of	named entity 'TO BE EXAMINED' named entity 'MAMMALIAN' named entity 'FOLLOWING' named entity 'CELLS' named entity 'BIOCHEMICAL' named entity 'LOW' named entity 'THESE' named entity 'DIFFERENT' named entity 'VIRUS-LIKE PARTICLES' named entity 'PROCESS' named entity 'INFECTION' named entity 'M PROTEINS' named entity 'BIOLOGICAL MATERIAL' named entity 'LEVELS' named entity 'PRIMARY' named entity 'virus' named entity 'leads' named entity 'METHODOLOGIES' named entity 'INFECTIOUS' named entity 'SERVE' named entity 'LOW LEVEL' named entity 'MODEL SYSTEM' named entity 'EXPERIMENTAL' named entity 'SUBSEQUENT' named entity 'USUALLY' named entity 'HIGHER' named entity 'RECOVERY' named entity 'STUDY' named entity 'VIRUS REPLICATION' covid:arg/adbb0a486cf43c474df8b8b86fa6eacd422b171c named entity 'VIRUS-LIKE PARTICLE' named entity 'PARTICLE FORMATION' named entity 'PROTEINS' named entity 'METAPNEUMOVIRUS' named entity 'STRATEGY' named entity 'EXPRESSION' named entity 'ISOLATION' named entity 'VIRUS' named entity 'LEADS' named entity 'HAVE' named entity 'HMPV' named entity 'ALLOW' named entity 'STUDIES' named entity 'VIRUS ASSEMBLY' named entity 'FORMATION' named entity 'CELL LINES' named entity 'infection' named entity 'higher' named entity 'VLP' named entity 'virus' named entity 'virus-like particles' named entity 'expression' named entity 'w/v' named entity 'transfected' named entity 'biotinylated' named entity 'glycosaminoglycans' named entity 'w/v' named entity 'protein' named entity 'lower respiratory infection' named entity 'Alexa Fluor' named entity 'w/v' named entity 'immunoprecipitates' named entity 'PBS' named entity 'O-linked glycans' named entity 'protein' named entity 'FESEM' named entity 'antibodies' named entity 'SDS-PAGE' named entity 'Immunoblotting' named entity 'morphology' named entity 'virus' named entity 'protein' named entity 'RSV' named entity 'virus envelope'

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