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Characterization of Marburg virus glycoprotein in viral entry

Balaji Manicassamy1, Jizhen Wang, Emily Rumschlag

  • 1Department of Microbiology and Immunology, College of Medicine Research Building, University of Illinois at Chicago, 8133 COMRB, 909 S. Wolcott Ave., Chicago, IL 60612, USA.

Virology
|September 23, 2006
PubMed

Insights

Marburg glycoprotein (MGP) plays a key role in filovirus entry. This study shows MGP is sensitive to residue changes, unlike Ebola GP, suggesting different folding mechanisms for these viral glycoproteins.

Area of Science:

  • Virology
  • Molecular Biology
  • Infectious Diseases

Background:

  • Filovirus host tropism is determined by viral glycoproteins (GP).
  • Marburg GP (MGP) function in viral entry is less understood than Ebola GP (EGP).

Purpose of the Study:

  • To characterize the role of MGP in viral entry using a human immunodeficiency virus (HIV)-based pseudotyped virus system.
  • To investigate potential differences in the entry mechanisms of EGP and MGP.

Main Methods:

  • Utilized an HIV-based pseudotyped virus system to study MGP and EGP.
  • Developed a viral entry interference assay for filoviruses.
  • Analyzed the impact of MGP and EGP substitutions on viral entry.

Main Results:

  • The mucin-like region of MGP is not essential for virus entry, similar to EGP.
  • Ectopic expression of EGP or MGP interfered with pseudotyped virus entry, suggesting shared entry receptors.
  • MGP is more sensitive to substitutions in conserved residues than EGP, impacting its expression, incorporation, and entry mediation.

Conclusions:

  • Ebola and Marburg viruses likely utilize the same or similar host molecules for entry.
  • MGP's sensitivity to residue substitutions suggests distinct folding or structural properties compared to EGP.

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