About: Molecular biology of transmissible gastroenteritis virus

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An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Molecular biology of transmissible gastroenteritis virus
Creator	Gelfi, Jacqueline Laude, Hubert Rasschaert, Denis Charley, Bernard Delmas, Bernard Godet, Murielle
Source	PMC
abstract	The causative agent (TGEV) of porcine transmissible gastroenteritis belongs to the Coronaviridae, a family of enveloped viruses with a positive, single-stranded RNA genome. Important progress has recently been made concerning the molecular biology of TGEV. The research work of our group has been focused on two main aspects: genome structure and functional domains of the envelope proteins. TGEV genomic RNA is organised into seven regions. The sequence of six of them, i.e. the 3′ most 8300 nucleotides, has been established from cDNA clones. Three genes encoding the structural proteins, the peplomer protein E2, the transmembrane protein E1 and the nucleoprotein, have been identified. Additional open reading frames allowed for the prediction of four non-structural polypeptides, the role of which remains to be discovered. The remaining part of the genome (estimated length 20 kb) is thought to encode the polymerase. Expression of TGEV genes involves the production of six subgenomic mRNAs, which together with the virion RNA, form a 3′ terminal nested set. The peplomer glycoprotein E2 (220 kDa) is 1431 residues long and highly glycosylated. Several domains were identified, including a C-terminal anchoring region and at least four major antigenic sites, which cluster in the amino half part of the molecule. Two sites containing most of the critical neutralisation determinants are highly conserved among TGEV strains. The glycoprotein E1 (29kDa) is mostly embedded in the membrane and plays a crucial role in the virion architecture. However, a short N-terminal domain protruding out of the particle mediates complement-dependent neutralisation, and induces alpha interferon synthesis, likely through a direct interaction with the lymphocyte membrane.
has issue date	2002-11-13(xsd:dateTime)
bibo:doi	10.1016/0378-1135(90)90144-k
bibo:pmid	2169670
has license	no-cc
sha1sum (hex)	c0d6f7ba23b828091f0126beb2481111aed644d7
schema:url	https://doi.org/10.1016/0378-1135%2890%2990144-k
resource representing a document's title	Molecular biology of transmissible gastroenteritis virus
has PubMed Central identifier	PMC7117338
has PubMed identifier	2169670
schema:publication	Vet Microbiol
resource representing a document's body	covid:c0d6f7ba23b828091f0126beb2481111aed644d7#body_text
is schema:about of	named entity 'MOLECULAR BIOLOGY' named entity 'transmissible' named entity 'TRANSMISSIBLE GASTROENTERITIS VIRUS' named entity 'TRANSMISSIBLE GASTROENTERITIS VIRUS' named entity 'DELMAS' named entity 'VET' named entity 'MOLECULAR BIOLOGY' named entity '154' named entity 'H.%' named entity 'glycoprotein' named entity 'coronavirus' named entity 'TGEV' named entity 'hepatitis virus' named entity 'antigenic determinants' named entity '22 N-terminal' named entity 'glycosylation' named entity 'genome' named entity 'protein' named entity 'highly conserved' named entity 'polypeptide' named entity 'virus' named entity 'Transmissible gastroenteritis' named entity 'intracellular' named entity 'MAbs' named entity 'lymphocyte' named entity 'surface antigens' named entity 'coding regions' named entity 'TGEV' named entity 'glycoprotein' named entity 'kDa' named entity 'cysteine' named entity 'causative agent' named entity 'enteric disease' named entity 'C-terminus' named entity 'heterodimer' named entity 'nucleotides' named entity 'nucleoprotein' named entity 'coronaviruses' named entity 'protein' named entity 'cDNA' named entity 'nucleotides' named entity 'ectodomain' named entity 'genome' named entity 'polypeptide chain' named entity 'genomic information' named entity 'RNAs' named entity 'protein' named entity 'acylation' named entity 'hydrophilic' named entity 'polypeptide' named entity 'amino acid sequence' named entity 'nested set' named entity 'consensus sequence' named entity 'hydrophobic' named entity 'genome' named entity 'kilobases' named entity 'molecule' named entity 'genome' named entity 'nucleotide' named entity 'subgenomic RNAs' named entity 'lipid membrane' named entity 'tropism' named entity 'virion' named entity 'porcine' named entity 'antiserum' named entity 'IBV' named entity 'RNA' named entity 'protein' named entity 'mRNA' named entity 'TGEV' named entity 'cleavage' named entity 'MHV' named entity 'kDa' named entity 'TGEV' named entity 'IFN' named entity 'swine'

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