About: A Functional Henipavirus Envelope Glycoprotein Pseudotyped Lentivirus Assay System

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About: A Functional Henipavirus Envelope Glycoprotein Pseudotyped Lentivirus Assay System Goto Sponge NotDistinct Permalink

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

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	A Functional Henipavirus Envelope Glycoprotein Pseudotyped Lentivirus Assay System
Creator	Khetawat, Dimple Broder, Christopher
Source	Medline; PMC
abstract	BACKGROUND: Hendra virus (HeV) and Nipah virus (NiV) are newly emerged zoonotic paramyxoviruses discovered during outbreaks in Queensland, Australia in 1994 and peninsular Malaysia in 1998/9 respectively and classified within the new Henipavirus genus. Both viruses can infect a broad range of mammalian species causing severe and often-lethal disease in humans and animals, and repeated outbreaks continue to occur. Extensive laboratory studies on the host cell infection stage of HeV and NiV and the roles of their envelope glycoproteins have been hampered by their highly pathogenic nature and restriction to biosafety level-4 (BSL-4) containment. To circumvent this problem, we have developed a henipavirus envelope glycoprotein pseudotyped lentivirus assay system using either a luciferase gene or green fluorescent protein (GFP) gene encoding human immunodeficiency virus type-1 (HIV-1) genome in conjunction with the HeV and NiV fusion (F) and attachment (G) glycoproteins. RESULTS: Functional retrovirus particles pseudotyped with henipavirus F and G glycoproteins displayed proper target cell tropism and entry and infection was dependent on the presence of the HeV and NiV receptors ephrinB2 or B3 on target cells. The functional specificity of the assay was confirmed by the lack of reporter-gene signals when particles bearing either only the F or only G glycoprotein were prepared and assayed. Virus entry could be specifically blocked when infection was carried out in the presence of a fusion inhibiting C-terminal heptad (HR-2) peptide, a well-characterized, cross-reactive, neutralizing human mAb specific for the henipavirus G glycoprotein, and soluble ephrinB2 and B3 receptors. In addition, the utility of the assay was also demonstrated by an examination of the influence of the cytoplasmic tail of F in its fusion activity and incorporation into pseudotyped virus particles by generating and testing a panel of truncation mutants of NiV and HeV F. CONCLUSIONS: Together, these results demonstrate that a specific henipavirus entry assay has been developed using NiV or HeV F and G glycoprotein pseudotyped reporter-gene encoding retrovirus particles. This assay can be conducted safely under BSL-2 conditions and will be a useful tool for measuring henipavirus entry and studying F and G glycoprotein function in the context of virus entry, as well as in assaying and characterizing neutralizing antibodies and virus entry inhibitors.
has issue date	2010-11-12(xsd:dateTime)
bibo:doi	10.1186/1743-422x-7-312
bibo:pmid	21073718
has license	cc-by
sha1sum (hex)	e806597d3525be5b55b7bd8812217c2e53bced9f
schema:url	https://doi.org/10.1186/1743-422x-7-312
resource representing a document's title	A Functional Henipavirus Envelope Glycoprotein Pseudotyped Lentivirus Assay System
has PubMed Central identifier	PMC2994542
has PubMed identifier	21073718
schema:publication	Virol J
resource representing a document's body	covid:e806597d3525be5b55b7bd8812217c2e53bced9f#body_text
is schema:about of	named entity 'human' named entity 'infection' named entity 'functional' named entity 'retrovirus' named entity 'proper' named entity 'highly' named entity 'virus' named entity 'Assay' named entity 'HENIPAVIRUS' named entity 'MAMMALIAN' named entity 'PROBLEM' named entity 'CARRIED' named entity 'THESE' named entity 'LETHAL' named entity 'SEVERE' named entity 'DISEASE' named entity 'PANEL' named entity 'THEIR' named entity 'CYTOPLASMIC TAIL' named entity 'ITS' named entity 'GENERATING' named entity 'BIOSAFETY LEVEL' named entity 'ANIMALS' named entity 'ENCODING' named entity 'BROAD' named entity 'PREPARED' named entity 'NATURE' named entity 'HENDRA VIRUS' named entity 'RETROVIRUS' named entity 'HUMAN IMMUNODEFICIENCY VIRUS' named entity 'DEMONSTRATED' named entity 'C-TERMINAL' named entity 'EXAMINATION' named entity 'MAB' named entity 'NIV' named entity 'ASSAY' named entity 'ATTACHMENT' named entity 'INFECT' named entity 'CONTAINMENT' named entity 'RECEPTORS' named entity 'FUSION' named entity 'ACTIVITY' named entity 'HAVE' named entity 'VIRUS ENTRY' named entity 'RESTRICTION' named entity 'OCCUR' named entity 'ZOONOTIC' named entity 'OUTBREAKS' named entity 'HIGHLY' named entity 'CROSS-REACTIVE' named entity 'CONTINUE' named entity 'GREEN FLUORESCENT PROTEIN' named entity 'TROPISM' named entity 'MEASURING' named entity 'PRESENCE OF' named entity 'VIRUSES' named entity 'LACK' named entity 'EITHER' named entity 'AUSTRALIA' named entity 'HUMANS' named entity 'PARTICLES' named entity 'STAGE' named entity 'NIPAH VIRUS' named entity 'ROLES' named entity 'NEUTRALIZING ANTIBODIES' named entity 'USING' named entity 'EXTENSIVE' named entity 'ENTRY INHIBITORS' named entity 'SPECIFICITY' named entity 'LENTIVIRUS' named entity 'SIGNALS' named entity 'COULD BE' named entity 'INFLUENCE' named entity 'CONTEXT' named entity 'TARGET CELLS' named entity 'BACKGROUND' named entity 'ENVELOPE GLYCOPROTEIN' named entity 'G GLYCOPROTEIN' named entity 'HEV' named entity 'PROTEIN '

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