Characterization of Marburg virus glycoprotein in viral entry

Balaji Manicassamy; Jizhen Wang; Emily Rumschlag; Stéphanie Tymen; Valentina Volchkova; Viktor Volchkov; Lijun Rong

doi:10.1016/j.virol.2006.06.041

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Characterization of Marburg virus glycoprotein in viral entry

Journal article

Open access

Peer reviewed

Characterization of Marburg virus glycoprotein in viral entry

Balaji Manicassamy, Jizhen Wang, Emily Rumschlag, Stéphanie Tymen, Valentina Volchkova, Viktor Volchkov and Lijun Rong

Virology (New York, N.Y.), Vol.358(1), pp.79-88

2007

DOI: 10.1016/j.virol.2006.06.041

PMID: 16989883

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Abstract

One major determinant of host tropism for filoviruses is viral glycoprotein (GP), which is involved in receptor binding and viral entry. Compared to Ebola GP (EGP), Marburg GP (MGP) is less well characterized in viral entry. In this study, using a human immunodeficiency virus-based pseudotyped virus as a surrogate system, we have characterized the role of MGP in viral entry. We have shown that like EGP, the mucin-like region of MGP (289–501) is not essential for virus entry. We have developed a viral entry interference assay for filoviruses, and using this assay, we have demonstrated that transfection of EGP or MGP in target cells can interfere with EGP/HIV and MGP/HIV pseudotyped virus entry in a dose-dependent manner. These results are consistent with the notion that Ebola and Marburg viruses use the same or a related host molecule(s) for viral entry. Substitutions of the non-conserved residues in MGP1 did not impair MGP-mediated viral entry. Unlike that of EGP1, individual substitutions of many conserved residues of MGP1 exerted severe defects in MGP expression, incorporation to HIV virions, and thus its ability to mediate viral entry. These results indicate that MGP is more sensitive to substitutions of the conserved residues, suggesting that MGP may fold differently from EGP.

Viral entry

Receptor interference

Filovirus glycoprotein

Receptor binding domain

Marburg virus GP

Ebola virus GP

Details

Title: Subtitle: Characterization of Marburg virus glycoprotein in viral entry
Creators: Balaji Manicassamy - Department of Microbiology and Immunology, College of Medicine Research Building, University of Illinois at Chicago, 8133 COMRB, 909 S. Wolcott Ave., Chicago, IL 60612, USA
Jizhen Wang - Department of Microbiology and Immunology, College of Medicine Research Building, University of Illinois at Chicago, 8133 COMRB, 909 S. Wolcott Ave., Chicago, IL 60612, USA
Emily Rumschlag - Department of Microbiology and Immunology, College of Medicine Research Building, University of Illinois at Chicago, 8133 COMRB, 909 S. Wolcott Ave., Chicago, IL 60612, USA
Stéphanie Tymen - Department of Microbiology and Immunology, College of Medicine Research Building, University of Illinois at Chicago, 8133 COMRB, 909 S. Wolcott Ave., Chicago, IL 60612, USA
Valentina Volchkova - Filovirus Laboratory, INSERM U758, Claude Bernard University, Lyon-1, IFR128, Lyon, France
Viktor Volchkov - Filovirus Laboratory, INSERM U758, Claude Bernard University, Lyon-1, IFR128, Lyon, France
Lijun Rong - Department of Microbiology and Immunology, College of Medicine Research Building, University of Illinois at Chicago, 8133 COMRB, 909 S. Wolcott Ave., Chicago, IL 60612, USA
Resource Type: Journal article
Publication Details: Virology (New York, N.Y.), Vol.358(1), pp.79-88
DOI: 10.1016/j.virol.2006.06.041
PMID: 16989883
NLM abbreviation: Virology
ISSN: 0042-6822
eISSN: 1096-0341
Publisher: Elsevier Inc
Language: English
Date published: 2007
Academic Unit: Microbiology and Immunology
Record Identifier: 9984083870302771

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