About: Characterization of the Ectodomain of the Envelope Protein of Dengue Virus Type 4: Expression, Membrane Association, Secretion and Particle Formation in the Absence of Precursor Membrane Protein

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About: Characterization of the Ectodomain of the Envelope Protein of Dengue Virus Type 4: Expression, Membrane Association, Secretion and Particle Formation in the Absence of Precursor Membrane Protein Goto Sponge NotDistinct Permalink

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Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	Characterization of the Ectodomain of the Envelope Protein of Dengue Virus Type 4: Expression, Membrane Association, Secretion and Particle Formation in the Absence of Precursor Membrane Protein
Creator	Wang, Wei-Kung Hsieh, Szu-Chia Tsai, Wen-Yang Nerurkar, Vivek
source	PMC
abstract	BACKGROUND: The envelope (E) of dengue virus (DENV) is the major target of neutralizing antibodies and vaccine development. After biosynthesis E protein forms a heterodimer with precursor membrane (prM) protein. Recent reports of infection enhancement by anti-prM monoclonal antibodies (mAbs) suggest anti-prM responses could be potentially harmful. Previously, we studied a series of C-terminal truncation constructs expressing DENV type 4 prM/E or E proteins and found the ectodomain of E protein alone could be recognized by all 12 mAbs tested, suggesting E protein ectodomain as a potential subunit immunogen without inducing anti-prM response. The characteristics of DENV E protein ectodomain in the absence of prM protein remains largely unknown. METHODOLOGY/PRINCIPAL FINDINGS: In this study, we investigated the expression, membrane association, glycosylation pattern, secretion and particle formation of E protein ectodomain of DENV4 in the presence or absence of prM protein. E protein ectodomain associated with membrane in or beyond trans-Golgi and contained primarily complex glycans, whereas full-length E protein associated with ER membrane and contained high mannose glycans. In the absence of prM protein, E protein ectodomain can secrete as well as form particles of approximately 49 nm in diameter, as revealed by sucrose gradient ultracentrifugation with or without detergent and electron microscopy. Mutational analysis revealed that the secretion of E protein ectodomain was affected by N-linked glycosylation and could be restored by treatment with ammonia chloride. CONCLUSIONS/SIGNIFICANCE: Considering the enhancement of DENV infectivity by anti-prM antibodies, our findings provide new insights into the expression and secretion of E protein ectodomain in the absence of prM protein and contribute to future subunit vaccine design.
has issue date	2014-06-20(xsd:dateTime)
bibo:doi	10.1371/journal.pone.0100641
bibo:pmid	24950216
has license	cc-by
sha1sum (hex)	e10af65e4c33f25a580260de1b277ca738dcc886
schema:url	https://doi.org/10.1371/journal.pone.0100641
resource representing a document's title	Characterization of the Ectodomain of the Envelope Protein of Dengue Virus Type 4: Expression, Membrane Association, Secretion and Particle Formation in the Absence of Precursor Membrane Protein
has PubMed Central identifier	PMC4065094
has PubMed identifier	24950216
schema:publication	PLoS One
resource representing a document's body	covid:e10af65e4c33f25a580260de1b277ca738dcc886#body_text
is schema:about of	named entity 'prM' named entity 'responses' named entity 'potential' named entity 'biosynthesis' named entity 'protein' named entity 'protein' named entity 'harmful' named entity 'After' named entity 'Association' named entity 'Characterization' covid:arg/e10af65e4c33f25a580260de1b277ca738dcc886 named entity 'envelope' named entity 'remains' named entity 'expressing' named entity 'inducing' named entity 'biosynthesis' named entity 'protein' named entity 'DENV' named entity 'mAbs' named entity 'vaccine' named entity 'DENV' named entity 'protein' named entity 'dengue virus' named entity 'ectodomain' named entity 'immunogen' named entity 'Ectodomain' named entity 'protein' named entity 'alanine' named entity 'Western blot' named entity 'transfected' named entity 'N-glycosylation' named entity 'Western blot' named entity 'C-terminal' named entity 'molecular mechanism' named entity 'VLPs' named entity 'Perkin Elmer' named entity 'sucrose' named entity 'DENV' named entity 'VLPs' named entity 'recombinant' named entity 'neutralizing antibodies' named entity 'plasmid DNA' named entity 'EH1' named entity 'subviral particles' named entity 'ectodomain' named entity 'membrane association' named entity 'dengue shock syndrome' named entity 'immune serum' named entity 'electron micrographs' named entity 'ectodomain' named entity 'cell lysates' named entity 'Tris-buffered saline' named entity 'PBS' named entity 'prophylactic' named entity 'protein' named entity 'Mutant' named entity 'protein' named entity 'a-helical' named entity 'centrifugation' named entity 'transfected' named entity 'VLPs' named entity 'valine' named entity 'Tris-HCl' named entity 'nuclei' named entity 'protein' named entity 'mAb' named entity 'antigenic' named entity '293T cells' named entity 'virus-like particles' named entity 'Tris-HCl' named entity 'incubation' named entity 'quality control' named entity 'immunogen' named entity 'non-denaturing' named entity 'N-linked glycosylation' named entity 'TBEV' named entity 'ectodomain' named entity '10.6'

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