TY - JOUR
T1 - The intracellular cargo receptor ERGIC-53 is required for the production of infectious arenavirus, coronavirus, and filovirus particles
AU - Klaus, Joseph P.
AU - Eisenhauer, Philip
AU - Russo, Joanne
AU - Mason, Anne B.
AU - Do, Danh
AU - King, Benjamin
AU - Taatjes, Douglas
AU - Cornillez-Ty, Cromwell
AU - Boyson, Jonathan E.
AU - Thali, Markus
AU - Zheng, Chunlei
AU - Liao, Lujian
AU - Yates, John R.
AU - Zhang, Bin
AU - Ballif, Bryan A.
AU - Botten, Jason W.
PY - 2013/11/13
Y1 - 2013/11/13
N2 - 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.
AB - 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.
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U2 - 10.1016/j.chom.2013.10.010
DO - 10.1016/j.chom.2013.10.010
M3 - Article
C2 - 24237698
AN - SCOPUS:84887868167
SN - 1931-3128
VL - 14
SP - 522
EP - 534
JO - Cell Host and Microbe
JF - Cell Host and Microbe
IS - 5
ER -