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JBC Communications
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- Accelerated Communication Editors' PickOpen Access
The chaperone GRP78 is a host auxiliary factor for SARS-CoV-2 and GRP78 depleting antibody blocks viral entry and infection
Journal of Biological ChemistryVol. 296100759Published online: May 6, 2021- Anthony J. Carlos
- Dat P. Ha
- Da-Wei Yeh
- Richard Van Krieken
- Chun-Chih Tseng
- Pu Zhang
- and others
Cited in Scopus: 0The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), the causative agent of the COVID-19 global pandemic, utilizes the host receptor angiotensin-converting enzyme 2 (ACE2) for viral entry. However, other host factors might also play important roles in SARS-CoV-2 infection, providing new directions for antiviral treatments. GRP78 is a stress-inducible chaperone important for entry and infectivity for many viruses. Recent molecular docking analyses revealed putative interaction between GRP78 and the receptor-binding domain (RBD) of the SARS-CoV-2 Spike protein (SARS-2-S).