The role of the hepatitis C virus glycoproteins in infection

Flint, Mike; McKeating, Jane A.

doi:10.1002/(sici)1099-1654(200003/04)10:2<101::aid-rmv268>3.0.co;2-w

Cited by 76 publications

(55 citation statements)

References 87 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…In addition to that, different viruses can be used as a scaffold for E1E2 glycoproteins, a concept called pseudotyping. The first HCV pseudotypes elaborated were based on modified influenza [48] or vesicular stomatitis virus viruses [49][50][51][52]. However, to our knowledge, except for one report [49], only chimeric glycoproteins, 5 consisting of the ectodomains from E1E2 and both the transmembrane domain and cytoplasmic tail from the heterologous virus, could be incorporated into the pseudovirus envelope.…”

Section: Overview On the Viral Entry Systemsmentioning

confidence: 99%

Entry and replication of recombinant hepatitis C viruses in cell culture

Vièyres

Pietschmann

2013

Methods

View full text Add to dashboard Cite

Section: Overview On the Viral Entry Systemsmentioning

confidence: 99%

Entry and replication of recombinant hepatitis C viruses in cell culture

Vièyres

Pietschmann

2013

Methods

View full text Add to dashboard Cite

“…E1 and E2, the putative viral envelope glycoproteins, are cleaved from the polyprotein precursor by host signal peptidases. Both are predicted to be transmembrane proteins with a large N-terminal ectodomain and a Cterminal hydrophobic region (18) and are heavily modified by N-linked glycosylation (22).…”

Section: Hepatitis C Virus (Hcv)mentioning

confidence: 99%

Identification of Conserved Residues in the E2 Envelope Glycoprotein of the Hepatitis C Virus That Are Critical for CD81 Binding

Owsianka

Timms

Tarr

et al. 2006

J Virol

227

268

View full text Add to dashboard Cite

Hepatitis C virus (HCV) cell entry involves interaction between the viral envelope glycoprotein E2 and the cell surface receptor CD81. Knowledge of conserved E2 determinants important for successful binding will facilitate development of entry inhibitors designed to block this interaction. Previous studies have assigned the CD81 binding function to a number of discontinuous regions of E2. To better define specific residues involved in receptor binding, a panel of mutants of HCV envelope proteins was generated, where conserved residues within putative CD81 binding regions were sequentially mutated to alanine. Mutant proteins were tested for binding to a panel of monoclonal antibodies and CD81 and for their ability to form noncovalent heterodimers and confer infectivity in the retroviral pseudoparticle (HCVpp) assay. Detection by conformation-sensitive monoclonal antibodies indicated that the mutant proteins were correctly folded. Mutant proteins fell into three groups: those that bound CD81 and conferred HCVpp infectivity, those that abrogated both CD81 binding and HCVpp infectivity, and a final group containing mutants that were able to bind CD81 but were noninfectious in the HCVpp assay. Specific amino acids conserved across all genotypes that were critical for CD81 binding were W420, Y527, W529, G530, and D535. These data significantly increase our understanding of the CD81 receptor-E2 binding process.Hepatitis C virus (HCV) is the sole member of the Hepacivirus genus within the family Flaviviridae. It is a major cause of community-acquired and posttransfusion hepatitis. More than 170 million people worldwide are seropositive for HCV, and only 20% of those infected are able to clear the virus. In the remaining 80% of individuals, the virus persists and can

show abstract

“…These N-glycosylation sites are well conserved, suggesting that they play essential roles in the function of these proteins. E2 is thought to initiate viral attachment, whereas E1 may be involved in virus-cell membrane fusion (7,8).…”

Section: Introductionmentioning

confidence: 99%

Specifically Binding of L-ficolin to N-glycans of HCV Envelope Glycoproteins E1 and E2 Leads to Complement Activation

Liu

Ali

et al. 2009

Cell Mol Immunol

View full text Add to dashboard Cite

L-ficolin, one of lectin families, is a recently identified complement factor that initiates lectin pathway of complement. Little is known about its role in viral hepatitis. In the present study, we found that L-ficolin in serum from 103 patients with hepatitis C virus (HCV), were significantly higher than that in 150 healthy controls. We further found that L-ficolin expressions were significantly increased in vitro study by HCV JFH-1 infected human hepatocyte cell line Huh7.5.

show abstract

The role of the hepatitis C virus glycoproteins in infection

Cited by 76 publications

References 87 publications

Entry and replication of recombinant hepatitis C viruses in cell culture

Entry and replication of recombinant hepatitis C viruses in cell culture

Identification of Conserved Residues in the E2 Envelope Glycoprotein of the Hepatitis C Virus That Are Critical for CD81 Binding

Specifically Binding of L-ficolin to N-glycans of HCV Envelope Glycoproteins E1 and E2 Leads to Complement Activation

Contact Info

Product

Resources

About