The intracellular cargo receptor ERGIC-53 is required for the production of infectious arenavirus, coronavirus, and filovirus particles

Joseph P. Klaus, Philip Eisenhauer, Joanne Russo, Anne B. Mason, Danh Do, Benjamin King, Douglas Taatjes, Cromwell Cornillez-Ty, Jonathan E. Boyson, Markus Thali, Chunlei Zheng, Lujian Liao, John R. Yates, Bin Zhang, Bryan A. Ballif, Jason W. Botten

Research output: Contribution to journalArticlepeer-review

Abstract

Arenaviruses and hantaviruses cause severe human disease. Little is known regarding host proteins required for their propagation. We identified human proteins that interact with the glycoproteins (GPs) of a prototypic arenavirus and hantavirus and show that the lectin endoplasmic reticulum (ER)-Golgi intermediate compartment 53 kDa protein (ERGIC-53), a cargo receptor required for glycoprotein trafficking within the early exocytic pathway, associates with arenavirus, hantavirus, coronavirus, orthomyxovirus, and filovirus GPs. ERGIC-53 binds to arenavirus GPs through a lectin-independent mechanism, traffics to arenavirus budding sites, and is incorporated into virions. ERGIC-53 is required for arenavirus, coronavirus, and filovirus propagation; in its absence, GP-containing virus particles form but are noninfectious, due in part to their inability to attach to host cells. Thus, we have identified a class of pathogen-derived ERGIC-53 ligands, a lectin-independent basis for their association with ERGIC-53, and a role for ERGIC-53 in the propagation of several highly pathogenic RNA virus families.

Original languageEnglish (US)
Pages (from-to)522-534
Number of pages13
JournalCell Host and Microbe
Volume14
Issue number5
DOIs
StatePublished - Nov 13 2013
Externally publishedYes

ASJC Scopus subject areas

  • Parasitology
  • Microbiology
  • Virology

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