Structural insights into coronavirus entry

M. Alejandra Tortorici; David Veesler

doi:10.1016/bs.aivir.2019.08.002

Cited by 769SARS-CoV-2 and COVID-19 ResearchAnimal Virus Infections StudiesViral Infections and Outbreaks Research

Structural insights into coronavirus entry

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M. Alejandra Tortorici, David Veesler·2019·Advances in Virus Research

DOI 10.1016/bs.aivir.2019.08.002PMC PMC7112261

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Abstract

Coronaviruses (CoVs) have caused outbreaks of deadly pneumonia in humans since the beginning of the 21st century. The severe acute respiratory syndrome coronavirus (SARS-CoV) emerged in 2002 and was responsible for an epidemic that spread to five continents with a fatality rate of 10% before being contained in 2003 (with additional cases reported in 2004). The Middle-East respiratory syndrome coronavirus (MERS-CoV) emerged in the Arabian Peninsula in 2012 and has caused recurrent outbreaks in humans with a fatality rate of 35%. SARS-CoV and MERS-CoV are zoonotic viruses that crossed the species barrier using bats/palm civets and dromedary camels, respectively. No specific treatments or vaccines have been approved against any of the six human coronaviruses, highlighting the need to investigate the principles governing viral entry and cross-species transmission as well as to prepare for zoonotic outbreaks which are likely to occur due to the large reservoir of CoVs found in mammals and birds. Here, we review our understanding of the infection mechanism used by coronaviruses derived from recent structural and biochemical studies.

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The spike protein enables viral entry into host cells through the ACE-2 receptor.
“The S gene encodes for the prominent homotrimeric, type I fusion and transmembrane glycoprotein which enables viral entry into the host target cell through the angiotensin-converting enzyme-2 (ACE-2) receptor [5, 6].”
From Waves and variants of SARS-CoV-2: understanding the causes and effect of the COVID-19 catastrophe (2022) · cites this paper as [5]
The Introduction says spike promotes host attachment and membrane fusion during entry, and “Diversity of CoV receptors and entry mechanisms” identifies ACE2 as an entry receptor for SARS-CoV and HCoV-NL63. The same section describes other coronaviruses using different receptors, so the source does not support ACE2 as the entry receptor for coronaviruses generally. (LLM, conf=0.85)
Experimental — accuracy not yet measured
The spike protein mediates entry into host cells by binding the ACE-2 receptor.
“The S gene encodes for the prominent homotrimeric, type I fusion and transmembrane glycoprotein which enables viral entry into the host target cell through the angiotensin-converting enzyme-2 (ACE-2) receptor [5, 6].”
From Waves and variants of SARS-CoV-2: understanding the causes and effect of the COVID-19 catastrophe (2022) · cites this paper as [5]
The Introduction says the spike protein promotes host attachment and membrane fusion during entry. The section “Diversity of CoV receptors and entry mechanisms” identifies ACE2 as an entry receptor for SARS-CoV and HCoV-NL63, but also says other coronaviruses use different receptors. The unqualified claim that spike-mediated entry occurs through ACE2 is therefore broader than the source supports. (LLM, conf=0.88)
Experimental — accuracy not yet measured
The S gene encodes a homotrimeric type I fusion transmembrane glycoprotein that enables viral entry through the ACE-2 receptor.
“The S gene encodes for the prominent homotrimeric, type I fusion and transmembrane glycoprotein which enables viral entry into the host target cell through the angiotensin-converting enzyme-2 (ACE-2) receptor [5, 6].”
From Waves and variants of SARS-CoV-2: understanding the causes and effect of the COVID-19 catastrophe (2022) · cites this paper as [5]
The Introduction describes spike (S) as a trimeric class I fusion protein involved in viral entry, and Prefusion S architecture identifies its transmembrane region. However, Diversity of CoV receptors and entry mechanisms identifies ACE2 as an entry receptor for SARS-CoV and HCoV-NL63, while other coronaviruses use different receptors. The claim does not limit its ACE2 assertion to those viruses. (LLM, conf=0.87)
Experimental — accuracy not yet measured

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Structure, function and antigenicity of the SARS-CoV-2 spike glycoprotein
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SARS-CoV-2 vaccines in development
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Cross-neutralization of SARS-CoV-2 by a human monoclonal SARS-CoV antibody
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Distinct conformational states of SARS-CoV-2 spike protein
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Structural and Functional Analysis of the D614G SARS-CoV-2 Spike Protein Variant
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N-terminal domain antigenic mapping reveals a site of vulnerability for SARS-CoV-2
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“The S1 subunit comprises an N-terminal domain (NTD) and a receptor-binding domain (RBD), also known as domain A and B, respectively (Tortorici and Veesler, 2019).”
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Structures of Human Antibodies Bound to SARS-CoV-2 Spike Reveal Common Epitopes and Recurrent Features of Antibodies
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Ultrapotent human antibodies protect against SARS-CoV-2 challenge via multiple mechanisms
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Elicitation of Potent Neutralizing Antibody Responses by Designed Protein Nanoparticle Vaccines for SARS-CoV-2
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“2) ( 16 , 17 ).”
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Rapid Generation of Neutralizing Antibody Responses in COVID-19 Patients
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Impaired immune cell cytotoxicity in severe COVID-19 is IL-6 dependent
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Characterisation of the transcriptome and proteome of SARS-CoV-2 reveals a cell passage induced in-frame deletion of the furin-like cleavage site from the spike glycoprotein
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SARS-CoV-2 infects cells after viral entry via clathrin-mediated endocytosis
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Neutralizing Antibody and Soluble ACE2 Inhibition of a Replication-Competent VSV-SARS-CoV-2 and a Clinical Isolate of SARS-CoV-2
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Authors: Tortorici, M. A., & Veesler, D.
Affiliations: Centre National de la Recherche Scientifique (FR)
University of Washington (US)
Corresponding author: David Veesler
ORCID: M. Alejandra Tortorici
David Veesler
Venue: Advances in Virus Research
Publisher: Elsevier
Published: 2019
Volume: 105
Pages: 93-116
ISSN: 0065-3527 (ISSN-L)
DOI: 10.1016/bs.aivir.2019.08.002
PMC: PMC7112261
OpenAlex: W2969525890
Cited by: 769
References: 133
Citations by year: 2026: 10 · 2025: 28 · 2024: 50 · 2023: 66 · 2022: 134 · 2021: 220 · 2020: 257 · 2019: 1
FWCI: 399.89
Type: book chapter
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
Locations: Advances in virus research (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
HAL (submittedVersion)
Funders: National Institute of General Medical Sciences (R01GM120553)
National Institute of Allergy and Infectious Diseases (HHSN272201700059C)
Topics: Health Sciences › Medicine › Infectious Diseases › SARS-CoV-2 and COVID-19 Research
Life Sciences › Agricultural and Biological Sciences › Animal Science and Zoology › Animal Virus Infections Studies
Health Sciences › Medicine › Infectious Diseases › Viral Infections and Outbreaks Research
Keywords: coronavirus entry, SARS-CoV, MERS-CoV, viral infection mechanisms, interspecies transmission, zoonotic viruses, viral structural proteins, receptor binding, zoonotic disease outbreaks, bats, Camelus dromedarius
MeSH terms: Animals, Humans, Virion, Coronavirus, Virus Internalization, Host-Pathogen Interactions

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