About: Identifying SARS-CoV Membrane Protein Amino Acid Residues Linked to Virus-Like Particle Assembly

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About: Identifying SARS-CoV Membrane Protein Amino Acid Residues Linked to Virus-Like Particle Assembly 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	Identifying SARS-CoV Membrane Protein Amino Acid Residues Linked to Virus-Like Particle Assembly
Creator	Huang, Kuo-Jung Tseng, Ying-Tzu Wang, Chin-Tien Wang, Shiu-Mei Chang, Chia-Hui
Source	Medline; PMC
abstract	Severe acute respiratory syndrome coronavirus (SARS-CoV) membrane (M) proteins are capable of self-assembly and release in the form of membrane-enveloped vesicles, and of forming virus-like particles (VLPs) when coexpressed with SARS-CoV nucleocapsid (N) protein. According to previous deletion analyses, M self-assembly involves multiple M sequence regions. To identify important M amino acid residues for VLP assembly, we coexpressed N with multiple M mutants containing substitution mutations at the amino-terminal ectodomain, carboxyl-terminal endodomain, or transmembrane segments. Our results indicate that a dileucine motif in the endodomain tail (218LL219) is required for efficient N packaging into VLPs. Results from cross-linking VLP analyses suggest that the cysteine residues 63, 85 and 158 are not in close proximity to the M dimer interface. We noted a significant reduction in M secretion due to serine replacement for C158, but not for C63 or C85. Further analysis suggests that C158 is involved in M-N interaction. In addition to mutations of the highly conserved 107-SWWSFNPE-114 motif, substitutions at codons W19, W57, P58, W91, Y94 or F95 all resulted in significantly reduced VLP yields, largely due to defective M secretion. VLP production was not significantly affected by a tryptophan replacement of Y94 or F95 or a phenylalanine replacement of W19, W57 or W91. Combined, these results indicate the involvement of specific M amino acids during SARS-CoV virus assembly, and suggest that aromatic residue retention at specific positions is critical for M function in terms of directing virus assembly.
has issue date	2013-05-20(xsd:dateTime)
bibo:doi	10.1371/journal.pone.0064013
bibo:pmid	23700447
has license	cc-by
sha1sum (hex)	0ba1801a150e25b029cf3c2a38573435b21dea80
schema:url	https://doi.org/10.1371/journal.pone.0064013
resource representing a document's title	Identifying SARS-CoV Membrane Protein Amino Acid Residues Linked to Virus-Like Particle Assembly
has PubMed Central identifier	PMC3659117
has PubMed identifier	23700447
schema:publication	PLoS One
resource representing a document's body	covid:0ba1801a150e25b029cf3c2a38573435b21dea80#body_text
is schema:about of	named entity 'CONTAINING' named entity 'SARS-COV' named entity 'ECTODOMAIN' named entity 'TRANSMEMBRANE' named entity 'RELEASE' named entity 'VESICLES' named entity 'ASSEMBLY' named entity 'MEMBRANE' named entity 'AMINO' named entity 'CAPABLE' named entity 'MUTANTS' named entity 'TO IDENTIFY' named entity 'SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS' named entity 'multiple' named entity 'Identifying' named entity 'IDENTIFYING' named entity 'FORM' named entity 'FORMING' named entity 'AMINO ACID' named entity 'PROTEIN AMINO ACID' named entity 'SARS-COV' named entity 'MEMBRANE PROTEIN' named entity 'DELETION' named entity 'REGIONS' named entity 'VIRUS-LIKE PARTICLES' named entity 'NUCLEOCAPSID' named entity 'MULTIPLE' named entity 'PROTEIN' named entity 'ASSEMBLY' named entity 'VIRUS-LIKE PARTICLE' named entity 'SEQUENCE' named entity 'TERMINAL' named entity 'ACCORDING' named entity 'SELF-ASSEMBLY' named entity 'VLP' named entity 'SEGMENTS' named entity 'MUTATIONS' named entity 'PREVIOUS' named entity 'CARBOXYL' named entity 'IMPORTANT' named entity 'SUBSTITUTION' named entity 'PROTEINS' covid:arg/0ba1801a150e25b029cf3c2a38573435b21dea80 named entity 'deletion' named entity 'amino-terminal' named entity 'transmembrane segments' named entity 'residues' named entity 'nucleocapsid' named entity 'SARS-CoV' named entity 'ectodomain' named entity 'VLP' named entity 'SARS-CoV' named entity 'nucleocapsid' named entity 'membrane (M) proteins' named entity 'amino acid residues' named entity 'ectodomain' named entity 'VLP' named entity 'secretion' named entity 'nucleocapsid' named entity 'mutation' named entity 'culture medium' named entity '1 ml' named entity 'transfection' named entity 'W57' named entity 'transfected' named entity 'antiserum' named entity 'glycerol' named entity 'eluted' named entity 'SARS-CoV' named entity 'lysis buffer' named entity '293T cells' named entity 'electrophoresis' named entity 'ICN Pharmaceuticals' named entity 'similar function' named entity 'nucleocapsid' named entity 'aromatic' named entity 'cysteine'

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