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Fig. 2. Glucose-regulated protein 78 (GRP78) plays a multifaceted role as a host factor that affects various stages of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) life cycle. It functions as a co-receptor, chaperone, protein stabilizer, and intermediary in cellular signaling and transcription processes. On the cell surface, GRP78 binds to the spike protein of SARS-CoV-2, triggering endocytosis and facilitating viral entry. Within the endoplasmic reticulum (ER), GRP78 assists in replicating and assembling viral proteins. It may also play a role in the exocytosis/egress of the virus and contribute to its overall stability, supporting a successful viral life cycle. Moreover, the interaction between SARS-CoV-2 and cell surface GRP78 could potentially activate cellular signaling pathways associated with inflammation and fibrosis. These pathways, in turn, may lead to the tissue and organ damage observed in coronavirus disease 2019 (COVID-19). ACE2, angiotensin-converting enzyme 2; ERGIC, ER–Golgi intermediate compartment.
J Obes Metab Syndr 2023;32:183~196 https://doi.org/10.7570/jomes23053
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