About: Mutations in the Leucine Zipper-Like Motif of the Human Parainfluenza Virus 3 Fusion Protein Impair Fusion Activity

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About: Mutations in the Leucine Zipper-Like Motif of the Human Parainfluenza Virus 3 Fusion Protein Impair Fusion Activity 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	Mutations in the Leucine Zipper-Like Motif of the Human Parainfluenza Virus 3 Fusion Protein Impair Fusion Activity
Creator	Zhao, Li Lin, Bin Wang, Zhiyu Chen, Yuzhen Chu, Fulu Li, Zhenmei Ren, Guijie Song, Yanyan Wen, Hongling Xie, Wenli Xie, Wenyan Yan, Shaofeng
Source	Medline; PMC
abstract	OBJECTIVE: To investigate the effect of the leucine zipper-like motif between HRA and HRB of the human parainfluenza virus 3 fusion protein on fusion activity. METHODS: Site-directed mutagenesis was utilized to substitute the heptadic residues at 257, 264, 271, 278, 285, 292, and 299 in this motif with alanine. Additionally, 3 middle heptadic leucine residues at 271, 278, and 285 were replaced with alanine singly or in combination. A vaccinia virus-T7 RNA polymerase transient expression system was employed to express the wild-type or mutated fusion (F) proteins. Three different types of membrane fusion assays were performed to analyze the fusogenic activity, fluorescence-activated cell sorting (FACS) analysis was executed to examine the cell surface expression level, and a coimmunoprecipitation assay was conducted to probe the hemagglutinin-neuraminidase (HN)-F interaction at the cell surface. RESULTS: All of the substitutions in this motif exhibited diminished or even lost fusion activity in all stages of fusion, although they all had no effect on cell surface expression. In the coimmunoprecipitation assay, all mutants resulted in decreased detection of the HN-F complexes compared with that of the wild-type F protein. CONCLUSIONS: This motif has an important influence on fusion activity, and its integrality is indispensable for membrane fusion.
has issue date	2015-12-23(xsd:dateTime)
bibo:doi	10.1159/000441978
bibo:pmid	26694747
has license	no-cc
sha1sum (hex)	15272bd755b2aa025cbb802c313f107bcf0513ac
schema:url	https://doi.org/10.1159/000441978
resource representing a document's title	Mutations in the Leucine Zipper-Like Motif of the Human Parainfluenza Virus 3 Fusion Protein Impair Fusion Activity
has PubMed Central identifier	PMC7179560
has PubMed identifier	26694747
schema:publication	Intervirology
resource representing a document's body	covid:15272bd755b2aa025cbb802c313f107bcf0513ac#body_text
is schema:about of	named entity 'surface' named entity 'integrality' named entity 'fusion' named entity 'FUSION' named entity 'activity' named entity 'lost' named entity 'motif' named entity 'membrane fusion' named entity 'Mutations' named entity 'coimmunoprecipitation' named entity 'protein' named entity 'cell surface' named entity 'Mutations' named entity 'membrane fusion' named entity 'Human Parainfluenza Virus' named entity 'MEMBRANE FUSION' named entity 'F PROTEIN' named entity 'ACTIVITY' named entity 'assay' named entity 'CONCLUSIONS' named entity 'EXPRESSION' named entity 'INDISPENSABLE' named entity 'DECREASED' named entity 'NO EFFECT' named entity 'DETECTION' named entity 'LOST' named entity 'Leucine Zipper-Like' named entity 'COMPARED' named entity 'ASSAY' named entity 'Fusion Protein' covid:arg/15272bd755b2aa025cbb802c313f107bcf0513ac named entity 'mutants' named entity 'ALL STAGES' named entity 'COIMMUNOPRECIPITATION' named entity 'LEUCINE ZIPPER' named entity 'wild-type' named entity 'motif' named entity 'mutants' named entity 'cell' named entity 'coimmunoprecipitation' named entity 'fusion' named entity 'expression' named entity 'activity' named entity 'Protein' named entity 'Human' named entity 'fusion' named entity 'protein' named entity 'assay' named entity 'Parainfluenza' named entity 'DIMINISHED' named entity 'complexes' named entity 'influence' named entity 'This' named entity 'indispensable' named entity 'wild-type' named entity 'Virus' named entity 'Leucine' named entity 'Motif' named entity 'MUTANTS' named entity 'ON CELL' named entity 'WILD-TYPE' named entity 'COMPLEXES' named entity 'Activity' named entity 'CELL SURFACE' named entity 'INFLUENCE' named entity 'IMPORTANT' named entity 'ITS' named entity 'MOTIF' named entity 'PROTEIN ' named entity 'MOTIF'

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