About: Nipah virus fusion protein: Importance of the cytoplasmic tail for endosomal trafficking and bioactivity

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About: Nipah virus fusion protein: Importance of the cytoplasmic tail for endosomal trafficking and bioactivity 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	Nipah virus fusion protein: Importance of the cytoplasmic tail for endosomal trafficking and bioactivity
Creator	Maisner, Andrea Weis, Michael
source	Elsevier; Medline; PMC
abstract	Abstract Nipah virus (NiV) is a highly pathogenic paramyxovirus which encodes two surface glycoproteins: the receptor-binding protein G and the fusion protein F. As for all paramyxoviruses, proteolytic activation of the NiV-F protein is an indispensable prerequisite for viral infectivity. Interestingly, proteolytic activation of NiV-F differs principally from other paramyxoviruses with respect to protease usage (cathepsins instead of trypsin- or furin-like proteases), and the subcellular localization where cleavage takes place (endosomes instead of Golgi or plasma membrane). To allow efficient F protein activation needed for productive virus replication and cell-to-cell fusion, the NiV-F cytoplasmic tail contains a classical tyrosine-based endocytosis signal (Y525RSL) that we have shown earlier to be needed for F uptake and proteolytic activation. In this report, we furthermore revealed that an intact endocytosis signal alone is not sufficient for full bioactivity. The very C-terminus of the cytoplasmic tail is needed in addition. Deletions of more than four residues did not affect F uptake or endosomal cleavage but downregulated the surface expression, likely by delaying the intracellular trafficking through endosomal-recycling compartments. Given that the NiV-F cytoplasmic tail is needed for timely and correct intracellular trafficking, endosomal cleavage and fusion activity, the influence of tail truncations on NiV-mediated cell-to-cell fusion and on pseudotyping lentiviral vectors is discussed.
has issue date	2015-09-30(xsd:dateTime)
bibo:doi	10.1016/j.ejcb.2015.05.005
bibo:pmid	26059400
has license	els-covid
sha1sum (hex)	49c37548b2dc49396b686e242dd20a426dd907da
schema:url	https://doi.org/10.1016/j.ejcb.2015.05.005
resource representing a document's title	Nipah virus fusion protein: Importance of the cytoplasmic tail for endosomal trafficking and bioactivity
has PubMed Central identifier	PMC7114669
has PubMed identifier	26059400
schema:publication	European Journal of Cell Biology
resource representing a document's body	covid:49c37548b2dc49396b686e242dd20a426dd907da#body_text
is schema:about of	named entity 'plasma membrane' named entity 'endosomal' named entity 'proteolytic' named entity 'paramyxoviruses' named entity 'downregulated' named entity 'NIPAH VIRUS' named entity 'FUSION PROTEIN' named entity 'BIOACTIVITY' named entity 'INFLUENCE' named entity 'PROTEIN ' named entity 'PROTEIN G' named entity 'PATHOGENIC' named entity 'LIKELY' named entity 'AFFECT' named entity 'BINDING PROTEIN' named entity 'INDISPENSABLE' named entity 'PRODUCTIVE' named entity 'EARLIER' named entity 'TIMELY' named entity 'USAGE' named entity 'PROTEOLYTIC ACTIVATION' named entity 'FUSION' named entity 'RESPECT' named entity 'PROTEIN ACTIVATION' named entity 'DID' named entity 'PROTEASES' named entity 'TRYPSIN' named entity 'CLASSICAL' named entity 'ADDITION' named entity 'TAIL' named entity 'ALLOW' named entity 'HIGHLY' named entity 'SURFACE' named entity 'VIRAL' named entity 'PREREQUISITE' named entity 'CYTOPLASMIC TAIL' named entity 'ENDOCYTOSIS' named entity '525' named entity 'IS A' named entity 'INTRACELLULAR' named entity 'PLASMA MEMBRANE' named entity 'VIRUS REPLICATION' named entity 'PARAMYXOVIRUSES' named entity 'BIOACTIVITY' named entity 'CONTAINS' named entity 'CELL FUSION' named entity 'C-TERMINUS' named entity 'COMPARTMENTS' named entity 'RECEPTOR' named entity 'REVEALED' named entity 'RSL' named entity 'SUFFICIENT' named entity 'MEDIATED' named entity 'NEEDED' named entity 'REPORT' named entity 'CORRECT' named entity 'NIPAH VIRUS' named entity 'THE NIV' named entity 'BUT' named entity 'PLACE' named entity 'ACTIVITY' named entity 'CYTOPLASMIC TAIL' named entity 'TRAFFICKING' named entity 'FUSION PROTEIN' named entity 'EXPRESSION' named entity 'NIV' named entity 'GIVEN' named entity 'FURIN' named entity 'PARAMYXOVIRUS' named entity 'PROTEIN F' named entity 'LIKE' named entity 'PROTEASE' named entity 'HAVE' named entity 'WHERE' named entity 'SIGNAL' named entity 'RECYCLING' named entity 'CLEAVAGE' named entity 'F PROTEIN' named entity 'UPTAKE' named entity 'VECTORS'

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