Cell Host Microbe. 2013 Nov 13;14(5):522-34. doi: 10.1016/j.chom.2013.10.010.
Klaus JP1, Eisenhauer P, Russo J, Mason AB, Do D, King B, Taatjes D, Cornillez-Ty C, Boyson JE, Thali M, Zheng C, Liao L, Yates JR 3rd, Zhang B, Ballif BA, Botten JW. 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.
Copyright © 2013 Elsevier Inc. All rights reserved.
Comment in
- The lectin ERGIC-53 goes viral. [Cell Host Microbe. 2013]
- PMID:
- 24237698
- PMCID:
- PMC3999090
- DOI:
- 10.1016/j.chom.2013.10.010
- [Indexed for MEDLINE]
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