Human coronavirus NL63 employs the severe acute respiratory syndrome coronavirus receptor for cellular entry

By Heike Hofmann, K. Pyrć, L. van der Hoek, Martina Geier, B. Berkhout, S. Pöhlmann. Proceedings of the National Academy of Sciences of the United States of America, 2005

803 citations recorded by the source corpus.

Subfields: Epidemiology, Infectious Diseases

View Paper: https://www.semanticscholar.org/paper/c9580f125be054436a052599483d12205d65beb0

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Citations in the corpus

Coronavirus Pathogenesis and the Emerging Pathogen Severe Acute Respiratory Syndrome Coronavirus (2005, background): “Surprisingly, it was recently shown that the newly identified group I human coronavirus NL63 also uses ACE2 as its receptor (136).”
Human Coronavirus HKU1 Spike Protein Uses O-Acetylated Sialic Acid as an Attachment Receptor Determinant and Employs Hemagglutinin-Esterase Protein as a Receptor-Destroying Enzyme (2015, background): “hCoV-NL63 and SARS-CoV both employ human angiotensin-converting enzyme 2 (ACE2) to mediate cellular entry (11, 12), while hCoV-NL63 utilizes heparan sulfate proteoglycans for attachment to target cells (13).”
Structure, Function, and Evolution of Coronavirus Spike Proteins (2016, neutral): “zinc peptidase angiotensin-converting enzyme 2 (ACE2) (20, 21).”
A Transmembrane Serine Protease Is Linked to the Severe Acute Respiratory Syndrome Coronavirus Receptor and Activates Virus Entry (2010, background): “Zoonotic CoVs may thus evolve affinities for those receptors that are associated with S-activating TTSPs, as might be inferred by the existence of the SARS-CoV and HCoV NL63, whose divergent S proteins both bind to ACE2 receptors (15, 16, 29).”
Coronavirus Diversity, Phylogeny and Interspecies Jumping (2009, background): “It is also noteworthy that at least one member of group 1b, HCoV-NL63, also uses ACE2 as the receptor for cell entry, as in the case of SARS-CoV, though the site of binding on ACE2 is different (52, 53).”
The Molecular Biology of Coronaviruses (2006, background): “The most outstanding exception to the generality of APN as a receptor for group 1 coronaviruses is the discovery that HCoV-NL63 cannot use hAPN to initiate infection; instead it is able to employ the same receptor as SARS-CoV, namely ACE2 (Hofmann et al., 2005).”
Are children less susceptible to COVID-19? (2020, methodology): “The SARS virus, SARS-CoV-2, and human coronavirus-NL63 (HCoV-NL63) all use the angiotensin-converting enzyme-2 (ACE2) as the cell receptor in humans.(13,14) Previous studies demonstrated that HCoV-NL63 infection is more common in adults than in children.”
Identification of residues in the receptor-binding domain (RBD) of the spike protein of human coronavirus NL63 that are critical for the RBD-ACE2 receptor interaction. (2008, background): “However, hACE2 is a functional receptor for NL63 (Hofmann et al., 2005).”
ACE2 Receptor Expression and Severe Acute Respiratory Syndrome Coronavirus Infection Depend on Differentiation of Human Airway Epithelia (2005, background): “Recently, angiotensin converting enzyme 2 (ACE2) was identified as a receptor for both SARS-CoV (21) and NL63 (12).”
Zoonotic origins of human coronaviruses (2020, background): “Intriguingly, HCoV-NL63 also binds to ACE2 but with a different part of S [77] .”
First infection by all four non-severe acute respiratory syndrome human coronaviruses takes place during childhood (2013, background): “The seroprevalence of HCoV antibodies varies widely among studies, which used different antigens and methodologies [6,13-18,26-33].”
A human coronavirus evolves antigenically to escape antibody immunity (2020, background): “Of the four human-endemic common-cold coronaviruses, the two alphacoronaviruses 229E and NL63 are similar to SARS-CoV-2 in binding a protein receptor via the spike’s receptor-binding domain (RBD, also known as S1-B) (Hofmann et al., 2005; Walls et al., 2020; Yeager et al., 1992).”
The human coronavirus HCoV-229E S-protein structure and receptor binding (2019, background): “HCoV-229E and 43 HCoV-NL63 are closely related alphacoronaviruses that use different host proteins as receptors 44 (8, 9), while HCoV-OC43 and HCoV-HKU1 are betacoronaviruses that both use 9-O-acetylsialic 45 acids as receptor(10, 11).”
Structural insights into coronavirus entry (2019, background): “Remarkably, viruses from different genera, such as HCoV-NL63 (α-CoV) and SARS-CoV (β-CoV), can recognize the same region of ACE2 (entry receptor) using structurally distinct B domains (Hofmann et al., 2005; Li et al., 2005a, 2003; Wu et al., 2009).”