Folding of viral envelope glycoproteins in the endoplasmic reticulum

Ineke Braakman, Eelco Van Anken

Research output: Contribution to journalArticle

Abstract

Viral glycoproteins fold and oligomerize in the endoplasmic reticulum of the host cell. They employ the cellular machinery and receive assistance from cellular folding factors. During the folding process, they are retained in the compartment and their structural quality is checked by the quality control system of the endoplasmic reticulum. A special characteristic that distinguishes viral fusion proteins from most cellular proteins is the extensive conformational change they undergo during fusion of the viral and cellular membrane. Many viral proteins fold in conjunction with and dependent on a viral partner protein, sometimes even synthesized from the same mRNA. Relevant for folding is that viral glycoproteins from the same or related virus families may consist of overlapping sets of domain modules. The consequences of these features for viral protein folding are at the heart of this review.

Original languageEnglish
Pages (from-to)533-539
Number of pages7
JournalTraffic
Volume1
Issue number7
Publication statusPublished - 2000

Keywords

  • Endoplasmic reticulum
  • Protein folding
  • Viral glycoprotein

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Genetics
  • Molecular Biology
  • Structural Biology

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  • Cite this

    Braakman, I., & Van Anken, E. (2000). Folding of viral envelope glycoproteins in the endoplasmic reticulum. Traffic, 1(7), 533-539.