About: Hepatitis C Virus Resistance to Carbohydrate-Binding Agents

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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	Hepatitis C Virus Resistance to Carbohydrate-Binding Agents
Creator	Brochot, Etienne Castelain, Sandrine Duverlie, Gilles Dubuisson, Jean Fournier, Carole Descamps, Véronique Francois, Catherine Helle, Francois Izquierdo, Laure Morel, Virginie Oliveira, Catarina
Source	Medline; PMC
abstract	Carbohydrate binding agents (CBAs), including natural lectins, are more and more considered as broad-spectrum antivirals. These molecules are able to directly inhibit many viruses such as Human Immunodeficiency Virus (HIV), Hepatitis C Virus (HCV), Dengue Virus, Ebola Virus or Severe Acute Respiratory Syndrome Coronavirus through binding to envelope protein N-glycans. In the case of HIV, it has been shown that CBAs select for mutant viruses with N-glycosylation site deletions which are more sensitive to neutralizing antibodies. In this study we aimed at evaluating the HCV resistance to CBAs in vitro. HCV was cultivated in the presence of increasing Galanthus nivalis agglutinin (GNA), Cyanovirin-N, Concanavalin-A or Griffithsin concentrations, during more than eight weeks. At the end of lectin exposure, the genome of the isolated strains was sequenced and several potential resistance mutations in the E1E2 envelope glycoproteins were identified. The effect of these mutations on viral fitness as well as on sensitivity to inhibition by lectins, soluble CD81 or the 3/11 neutralizing antibody was assessed. Surprisingly, none of these mutations, alone or in combination, conferred resistance to CBAs. In contrast, we observed that some mutants were more sensitive to 3/11 or CD81-LEL inhibition. Additionally, several mutations were identified in the Core and the non-structural proteins. Thus, our results suggest that in contrast to HIV, HCV resistance to CBAs is not directly conferred by mutations in the envelope protein genes but could occur through an indirect mechanism involving mutations in other viral proteins. Further investigations are needed to completely elucidate the underlying mechanisms.
has issue date	2016-02-12(xsd:dateTime)
bibo:doi	10.1371/journal.pone.0149064
bibo:pmid	26871442
has license	cc-by
sha1sum (hex)	ad60294d191a68f9db374d7ec49f42c2303b3b00
schema:url	https://doi.org/10.1371/journal.pone.0149064
resource representing a document's title	Hepatitis C Virus Resistance to Carbohydrate-Binding Agents
has PubMed Central identifier	PMC4752358
has PubMed identifier	26871442
schema:publication	PLoS One
resource representing a document's body	covid:ad60294d191a68f9db374d7ec49f42c2303b3b00#body_text
is schema:about of	named entity 'Hepatitis C Virus' named entity 'N-glycosylation' named entity 'genome' named entity 'mutations' named entity 'CBAs' named entity 'observed' named entity 'assessed' named entity 'fitness' named entity 'neutralizing antibody' named entity 'CBAs' named entity 'inhibition' named entity 'protein' named entity 'evaluating' named entity 'RESISTANCE TO' named entity 'MECHANISMS' named entity 'CONSIDERED' named entity 'CYANOVIRIN-N' named entity 'SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS' named entity 'PRESENCE OF' named entity 'EBOLA VIRUS' named entity 'COMPLETELY' named entity 'EVALUATING' named entity 'INCREASING' named entity 'VIRUSES' named entity 'MORE THAN' named entity 'AT THE END' named entity 'CONCANAVALIN' named entity 'HUMAN IMMUNODEFICIENCY VIRUS' named entity 'EFFECT' named entity 'CD81' named entity 'VIRAL FITNESS' named entity 'UNDERLYING' named entity 'NEUTRALIZING ANTIBODIES' named entity 'DIRECTLY' named entity 'NATURAL' named entity 'INDIRECT' named entity 'BINDING' named entity 'VIRUS RESISTANCE' named entity 'STRAINS' named entity 'AGGLUTININ' named entity 'NON-STRUCTURAL PROTEINS' named entity 'PROTEIN N' named entity 'MOLECULES' named entity 'ANTIVIRALS' named entity 'CARBOHYDRATE' named entity 'N-GLYCOSYLATION SITE' named entity 'PROTEIN ' named entity 'CORE' named entity 'HCV' named entity 'BINDING' named entity 'COMBINATION' named entity 'DENGUE VIRUS' named entity 'HEPATITIS C VIRUS' named entity 'SENSITIVE TO' named entity 'ISOLATED' named entity 'NEEDED' named entity 'LECTIN' named entity 'ENVELOPE' named entity 'OBSERVED' named entity 'HIV' named entity 'CONCENTRATIONS' named entity 'GLYCOPROTEINS' named entity 'INCLUDING' named entity 'ASSESSED' named entity 'GENOME' named entity 'CARBOHYDRATE BINDING' named entity 'STUDY' named entity 'INVOLVING' named entity 'GENES' named entity 'MUTATIONS' named entity 'MECHANISM'

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