Idiosyncratic Mòjiāng virus attachment glycoprotein directs a host-cell entry pathway distinct from genetically related henipaviruses

The attachment glycoprotein (HNV-G) of henipaviruses interacts with host receptors at the cell surface and is a major determinant of species tropism. Here the authors provide structural and functional evidence that the emergent henipavirus, Mòjiang virus, uses an entry mechanism that is independent...

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Autores principales:	Ilona Rissanen, Asim A. Ahmed, Kristopher Azarm, Shannon Beaty, Patrick Hong, Sham Nambulli, W. Paul Duprex, Benhur Lee, Thomas A. Bowden
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/4404ab8f23964705abc8973e53d1de3d
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spelling	oai:doaj.org-article:4404ab8f23964705abc8973e53d1de3d2021-12-02T17:06:11ZIdiosyncratic Mòjiāng virus attachment glycoprotein directs a host-cell entry pathway distinct from genetically related henipaviruses10.1038/ncomms160602041-1723https://doaj.org/article/4404ab8f23964705abc8973e53d1de3d2017-07-01T00:00:00Zhttps://doi.org/10.1038/ncomms16060https://doaj.org/toc/2041-1723The attachment glycoprotein (HNV-G) of henipaviruses interacts with host receptors at the cell surface and is a major determinant of species tropism. Here the authors provide structural and functional evidence that the emergent henipavirus, Mòjiang virus, uses an entry mechanism that is independent of known paramyoxviral cellular receptors.Ilona RissanenAsim A. AhmedKristopher AzarmShannon BeatyPatrick HongSham NambulliW. Paul DuprexBenhur LeeThomas A. BowdenNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-11 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Ilona Rissanen Asim A. Ahmed Kristopher Azarm Shannon Beaty Patrick Hong Sham Nambulli W. Paul Duprex Benhur Lee Thomas A. Bowden Idiosyncratic Mòjiāng virus attachment glycoprotein directs a host-cell entry pathway distinct from genetically related henipaviruses
description	The attachment glycoprotein (HNV-G) of henipaviruses interacts with host receptors at the cell surface and is a major determinant of species tropism. Here the authors provide structural and functional evidence that the emergent henipavirus, Mòjiang virus, uses an entry mechanism that is independent of known paramyoxviral cellular receptors.
format	article
author	Ilona Rissanen Asim A. Ahmed Kristopher Azarm Shannon Beaty Patrick Hong Sham Nambulli W. Paul Duprex Benhur Lee Thomas A. Bowden
author_facet	Ilona Rissanen Asim A. Ahmed Kristopher Azarm Shannon Beaty Patrick Hong Sham Nambulli W. Paul Duprex Benhur Lee Thomas A. Bowden
author_sort	Ilona Rissanen
title	Idiosyncratic Mòjiāng virus attachment glycoprotein directs a host-cell entry pathway distinct from genetically related henipaviruses
title_short	Idiosyncratic Mòjiāng virus attachment glycoprotein directs a host-cell entry pathway distinct from genetically related henipaviruses
title_full	Idiosyncratic Mòjiāng virus attachment glycoprotein directs a host-cell entry pathway distinct from genetically related henipaviruses
title_fullStr	Idiosyncratic Mòjiāng virus attachment glycoprotein directs a host-cell entry pathway distinct from genetically related henipaviruses
title_full_unstemmed	Idiosyncratic Mòjiāng virus attachment glycoprotein directs a host-cell entry pathway distinct from genetically related henipaviruses
title_sort	idiosyncratic mòjiāng virus attachment glycoprotein directs a host-cell entry pathway distinct from genetically related henipaviruses
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/4404ab8f23964705abc8973e53d1de3d
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Idiosyncratic Mòjiāng virus attachment glycoprotein directs a host-cell entry pathway distinct from genetically related henipaviruses

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