Budding of alphaviruses

Henrik Garoff, Mathilda Sjöberg, R. Holland Cheng

Research output: Contribution to journalArticle

59 Citations (Scopus)

Abstract

Alphaviruses are small highly ordered enveloped RNA viruses, which replicate very efficiently in the infected cell. They consist of a nucleocapsid (NC) and a surrounding membrane with glycoproteins. In the NC the positive single stranded RNA genome of the virus is enclosed by a T = 4 icosahedral shell of capsid (C) proteins. The glycoproteins form a second shell with corresponding symmetry on the outside of the lipid membrane. These viruses mature by budding at the plasma membrane (PM) of the infected cell and enter into new cells by acid-triggered membrane fusion in endosomes. The viral glycoprotein consists of two subunits, E1, which carries the membrane fusion function, and E2, which suppresses this function until acid activation occurs. In the infected cell the RNA replication and transcription are confined to the cytoplasmic surface of endosome-derived vesicles called cytopathic vacuoles type I (CPV I). These structures are closely associated with membranes of the endoplasmic reticulum (ER), thereby creating a microenvironment for synthesis of viral proteins, assembly of the glycoproteins and formation of genome-C complexes. The budding process of the virus is initiated by C-glycoprotein interactions, possibly already before the glycoproteins arrive at the PM. This might involve a premade, ordered NC or a less ordered form of the genome-C complex. In the latter case, the interactions in the glycoprotein shell provide the major driving force for budding. The nature of the C-glycoprotein interaction has been resolved at atomic resolution by modelling. It involves hydrophobic interactions between a Tyr-X-Leu tripeptide in the internal tail of the E2 subunit and a pocket on the surface of the C protein. When the virus enters the endosome of a new cell the acid conditions trigger rearrangements in the glycoprotein shell, which result in the dissociation of the interactions that drive budding and a concomitant activation of the membrane fusion function in the E1 subunit.

Original languageEnglish (US)
Pages (from-to)103-116
Number of pages14
JournalVirus Research
Volume106
Issue number2 SPEC.ISS.
DOIs
StatePublished - Dec 2004
Externally publishedYes

Fingerprint

Alphavirus
Glycoproteins
Nucleocapsid
Membrane Fusion
Endosomes
Virus Release
RNA Viruses
Genome
Acids
Cell Membrane
Virus Assembly
Membrane Glycoproteins
Capsid Proteins
Viral Proteins
Membrane Lipids
Vacuoles
Hydrophobic and Hydrophilic Interactions
Endoplasmic Reticulum
Membrane Proteins
RNA

Keywords

  • Alphaviruses
  • Glycoprotein
  • T = 4 icosahedral symmetry

ASJC Scopus subject areas

  • Cancer Research
  • Molecular Biology
  • Virology

Cite this

Garoff, H., Sjöberg, M., & Cheng, R. H. (2004). Budding of alphaviruses. Virus Research, 106(2 SPEC.ISS.), 103-116. https://doi.org/10.1016/j.virusres.2004.08.008

Budding of alphaviruses. / Garoff, Henrik; Sjöberg, Mathilda; Cheng, R. Holland.

In: Virus Research, Vol. 106, No. 2 SPEC.ISS., 12.2004, p. 103-116.

Research output: Contribution to journalArticle

Garoff, H, Sjöberg, M & Cheng, RH 2004, 'Budding of alphaviruses', Virus Research, vol. 106, no. 2 SPEC.ISS., pp. 103-116. https://doi.org/10.1016/j.virusres.2004.08.008
Garoff H, Sjöberg M, Cheng RH. Budding of alphaviruses. Virus Research. 2004 Dec;106(2 SPEC.ISS.):103-116. https://doi.org/10.1016/j.virusres.2004.08.008
Garoff, Henrik ; Sjöberg, Mathilda ; Cheng, R. Holland. / Budding of alphaviruses. In: Virus Research. 2004 ; Vol. 106, No. 2 SPEC.ISS. pp. 103-116.
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