Interaction of severe acute respiratory syndrome-coronavirus and NL63 coronavirus spike proteins with angiotensin converting enzyme-2

Mathewson, Alison C.; Bishop, Alexandra; Yao, Yongxiu; Kemp, Fred; Ren, Junyuan; Chen, Hongying; Xu, Xiaodong; Berkhout, Ben; Hoek, Lia van der; Jones, Ian M.

doi:10.1099/vir.0.2008/003962-0

Cited by 75 publications

(69 citation statements)

References 25 publications

(42 reference statements)

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“…One may assume that such binding will result in the efficient inactivation of the virus. Unfortunately, it was not possible to determine whether HTCC polymer hampers NL63-S/ACE2 interaction, as the affinity of NL63-S to ACE2 is very low (Lin et al, 2008;Mathewson et al, 2008) and it was not possible to visualize this process with accessible methods. Careful analysis of polymers suggests that the combination of particular polymeric chain and its proper substituent is indispensable for its activity.…”

Section: Discussionmentioning

confidence: 99%

Novel polymeric inhibitors of HCoV-NL63

et al. 2013

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The human coronavirus NL63 is generally classified as a common cold pathogen, though the infection may also result in severe lower respiratory tract diseases, especially in children, patients with underlying disease, and elderly. It has been previously shown that HCoV-NL63 is also one of the most important causes of croup in children. In the current manuscript we developed a set of polymer-based compounds showing prominent anticoronaviral activity. Polymers have been recently considered as promising alternatives to small molecule inhibitors, due to their intrinsic antimicrobial properties and ability to serve as matrices for antimicrobial compounds. Most of the antimicrobial polymers show antibacterial properties, while those with antiviral activity are much less frequent. A cationically modified chitosan derivative, N-(2-hydroxypropyl)-3-trimethylammonium chitosan chloride (HTCC), and hydrophobically-modified HTCC were shown to be potent inhibitors of HCoV-NL63 replication. Furthermore, both compounds showed prominent activity against murine hepatitis virus, suggesting broader anticoronaviral activity.

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Section: Discussionmentioning

confidence: 99%

Novel polymeric inhibitors of HCoV-NL63

et al. 2013

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“…The receptor-binding domain (RBD) has been mapped to amino acid residues 318-510 for SARS-CoV , and 476-616 for NL63 (Li et al, 2007;Lin et al, 2008). The RBDs of these two viruses bind to a largely overlapping region of hACE2 (Li et al, 2007), although the receptor-binding affinity of NL63 S is much less compared with SARS-CoV S (Lin et al, 2008;Mathewson et al, 2008). In addition, SARS-CoV S and NL63 S may cause differential downregulation of hACE2 level by induced shedding of its ectodomain from the cell surface (Haga et al, 2008;Glowacka et al, 2010).…”

Section: Introductionmentioning

confidence: 99%

Characterization of the spike protein of human coronavirus NL63 in receptor binding and pseudotype virus entry

Lin

Yan

et al. 2011

Virus Research

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The spike (S) protein of human coronavirus NL63 (HCoV-NL63) mediates both cell attachment by binding to its receptor hACE2 and membrane fusion during virus entry. We have previously identified the receptor-binding domain (RBD) and residues important for RBD-hACE2 association. Here, we further characterized the S protein by investigating the roles of the cytoplasmic tail and 19 residues located in the RBD in protein accumulation, receptor binding, and pseudotype virus entry. For these purposes, we first identified an entry-efficient S gene template from a pool of gene variants and used it as a backbone to generate a series of cytoplasmic tail deletion and single residue substitution mutants. Our results showed that: (i) deletion of 18aa from the C-terminus enhanced the S protein accumulation and virus entry, which might be due to the deletion of intracellular retention signals; (ii) further deletion to residue 29 also enhanced the amount of S protein on the cell surface and in virion, but reduced virus entry by 25%, suggesting that residues 19-29 contributes to membrane fusion; (iii) a 29aa-deletion mutant had a defect in anchoring on the plasma membrane, which led to a dramatic decrease of S protein in virion and virus entry; (iv) a total of 15 residues (Y498, V499, V531, G534, G537, D538, S540, G575, S576, E582, W585, Y590, T591, V593 and G594) within RBD were important for receptor binding and virus entry. They probably form three receptor binding motifs, and the third motif is conserved between NL63 and SARS-CoV.

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“…DQ865956.1), were generated as described previously (1,5,18). Expression levels were similar and all HAs were competent for SA binding by hemadsorption with either turkey or guinea pig red blood cells (Fig.…”

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confidence: 99%

Receptor Binding Profiles of Avian Influenza Virus Hemagglutinin Subtypes on Human Cells as a Predictor of Pandemic Potential

Shelton

Ayora-Talavera

Ren

et al. 2011

J Virol

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The host adaptation of influenza virus is partly dependent on the sialic acid (SA) isoform bound by the viral hemagglutinin (HA). Avian influenza viruses preferentially bind the α-2,3 SA and human influenza viruses the α-2,6 isoform. Each isoform is predominantly associated with different surface epithelial cell types of the human upper airway. Using recombinant HAs and human tracheal airway epithelial cells in vitro and ex vivo , we show that many avian HA subtypes do not adhere to this canonical view of SA specificity. The propensity of avian viruses to adapt to human receptors may thus be more widespread than previously supposed.

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Interaction of severe acute respiratory syndrome-coronavirus and NL63 coronavirus spike proteins with angiotensin converting enzyme-2

Cited by 75 publications

References 25 publications

Novel polymeric inhibitors of HCoV-NL63

Novel polymeric inhibitors of HCoV-NL63

Characterization of the spike protein of human coronavirus NL63 in receptor binding and pseudotype virus entry

Receptor Binding Profiles of Avian Influenza Virus Hemagglutinin Subtypes on Human Cells as a Predictor of Pandemic Potential

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