Nature Communications· 2020Q1
Characterization of spike glycoprotein of SARS-CoV-2 on virus entry and its immune cross-reactivity with SARS-CoV
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- Q1SCImago
- 2020year
Short summary
SARS-CoV-2 uses human ACE2 as its receptor and enters cells primarily via endocytosis, with PIKfyve, TPC2, and cathepsin L being critical for this process. The SARS-CoV-2 spike protein is less stable than SARS-CoV's, and antibodies or sera from recovered SARS or COVID-19 patients show limited cross-neutralization.
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Key points
- Human ACE2 is confirmed as the receptor for SARS-CoV-2.
- SARS-CoV-2 entry into cells occurs mainly via endocytosis, requiring PIKfyve, TPC2, and cathepsin L.
- SARS-CoV-2 spike protein is less stable than SARS-CoV spike protein.
- Limited cross-neutralization exists between SARS-CoV and SARS-CoV-2 antibodies/sera.
AI-generated from the title and abstract; the full text is not read.
Abstract
Since 2002, beta coronaviruses (CoV) have caused three zoonotic outbreaks, SARS-CoV in 2002-2003, MERS-CoV in 2012, and the newly emerged SARS-CoV-2 in late 2019. However, little is currently known about the biology of SARS-CoV-2. Here, using SARS-CoV-2 S protein pseudovirus system, we confirm that human angiotensin converting enzyme 2 (hACE2) is the receptor for SARS-CoV-2, find that SARS-CoV-2 enters 293/hACE2 cells mainly through endocytosis, that PIKfyve, TPC2, and cathepsin L are critical for entry, and that SARS-CoV-2 S protein is less stable than SARS-CoV S. Polyclonal anti-SARS S1 antibodies T62 inhibit entry of SARS-CoV S but not SARS-CoV-2 S pseudovirions. Further studies using recovered SARS and COVID-19 patients' sera show limited cross-neutralization, suggesting that recovery from one infection might not protect against the other. Our results present potential targets for development of drugs and vaccines for SARS-CoV-2.
The authors' abstract, as published at the source. Nature Communications, 2020 · DOI ↗
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Field: Infectious Diseases
Infectious DiseasesMedicine