» Articles » PMID: 12761383

Hepatitis C Virus Glycoproteins Mediate PH-dependent Cell Entry of Pseudotyped Retroviral Particles

Overview
Specialty Science
Date 2003 May 23
PMID 12761383
Citations 380
Authors
Affiliations
Soon will be listed here.
Abstract

HIV pseudotypes bearing native hepatitis C virus (HCV) glycoproteins (strain H and Con1) are infectious for the human hepatoma cell lines Huh-7 and PLC/PR5. Infectivity depends on coexpression of both E1 and E2 glycoproteins, is pH-dependent, and can be neutralized by mAbs mapping to amino acids 412-447 within E2. Cell-surface expression of one or all of the candidate receptor molecules (CD81, low-density lipoprotein receptor, scavenger receptor class B type 1, and dendritic cell-specific intercellular adhesion molecule 3 grabbing nonintegrin) failed to confer permissivity to HIV-HCV pseudotype infection. However, HIV-HCV pseudotype infectivity was inhibited by a recombinant soluble form of CD81 and a mAb specific for CD81, suggesting that CD81 may be a component of a receptor complex.

Citing Articles

Tetraspanin CD81 serves as a functional entry factor for porcine circovirus type 2 infection.

Li J, Lv L, Gao Y, Sun Y, Bai J, Wang X J Virol. 2025; 99(2):e0140824.

PMID: 39745447 PMC: 11853000. DOI: 10.1128/jvi.01408-24.


Poly(rC)-Binding Protein 2 Does Not Directly Participate in HCV Translation or Replication, but Rather Modulates Genome Packaging.

Cousineau S, Camargo C, Sagan S Viruses. 2024; 16(8).

PMID: 39205194 PMC: 11359930. DOI: 10.3390/v16081220.


Pseudovirus-Based Systems for Screening Natural Antiviral Agents: A Comprehensive Review.

Trischitta P, Tamburello M, Venuti A, Pennisi R Int J Mol Sci. 2024; 25(10).

PMID: 38791226 PMC: 11121416. DOI: 10.3390/ijms25105188.


Neutralizing antibodies evolve to exploit vulnerable sites in the HCV envelope glycoprotein E2 and mediate spontaneous clearance of infection.

Frumento N, Sinnis-Bourozikas A, Paul H, Stavrakis G, Zahid M, Wang S Immunity. 2024; 57(1):40-51.e5.

PMID: 38171362 PMC: 10874496. DOI: 10.1016/j.immuni.2023.12.004.


ASPP2 binds to hepatitis C virus NS5A protein via an SH3 domain/PxxP motif-mediated interaction and potentiates infection.

Smirnov A, Magri A, Lotz R, Han X, Yin C, Harris M J Gen Virol. 2023; 104(9).

PMID: 37750869 PMC: 7615710. DOI: 10.1099/jgv.0.001895.


References
1.
Higginbottom A, Quinn E, Kuo C, Flint M, WILSON L, Bianchi E . Identification of amino acid residues in CD81 critical for interaction with hepatitis C virus envelope glycoprotein E2. J Virol. 2000; 74(8):3642-9. PMC: 111874. DOI: 10.1128/jvi.74.8.3642-3649.2000. View

2.
Tan R, Harouse J, Gettie A, Cheng-Mayer C . In vivo adaptation of SHIV(SF162): chimeric virus expressing a NSI, CCR5-specific envelope protein. J Med Primatol. 1999; 28(4-5):164-8. DOI: 10.1111/j.1600-0684.1999.tb00265.x. View

3.
Agnello V, Abel G, Elfahal M, Knight G, Zhang Q . Hepatitis C virus and other flaviviridae viruses enter cells via low density lipoprotein receptor. Proc Natl Acad Sci U S A. 1999; 96(22):12766-71. PMC: 23090. DOI: 10.1073/pnas.96.22.12766. View

4.
Wellnitz S, Klumpp B, Barth H, Ito S, Depla E, Dubuisson J . Binding of hepatitis C virus-like particles derived from infectious clone H77C to defined human cell lines. J Virol. 2002; 76(3):1181-93. PMC: 135804. DOI: 10.1128/jvi.76.3.1181-1193.2002. View

5.
Lozach P, Lortat-Jacob H, de Lacroix de Lavalette A, Staropoli I, Foung S, Amara A . DC-SIGN and L-SIGN are high affinity binding receptors for hepatitis C virus glycoprotein E2. J Biol Chem. 2003; 278(22):20358-66. DOI: 10.1074/jbc.M301284200. View