Structure of the S1 subunit C-terminal domain from bat-derived coronavirus HKU5 spike protein

Han, Xue; Qi, Jianxun; Song, Hao; Wang, Qihui; Zhang, Yanfang; Wu, Ying; Lu, Guangwen; Yuen, Kwok‐Yung; Shi, Yi; Gao, George F.

doi:10.1016/j.virol.2017.04.016

Cited by 14 publications

(12 citation statements)

References 47 publications

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“…Similar to other studied beta coronaviruses CTD structure shows two conserved subdomains [21]. One is the core subdomain that is composed of 5 inverse parallel beta strands (ß1, ß2, ß3, ß4, and ß7) structure with a disulfide bond between ß2 and ß4 strands.…”

Section: Sars-supporting

confidence: 57%

SARS-CoV-2 S Protein Binding hACE2: Viral Entry, Pathogenesis, Prognosis, and Potential Therapeutic Targets

Al-Zaidan¹,

Mestiri²,

Raza³

et al. 2020

Preprint

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Pneumonia cases of unknown etiology in Wuhan, China, were reported to the WHO on 31st of December 2019. Later the pathogen was reported to be a novel coronavirus designated Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) that causes Coronavirus Disease 2019 (COVID-19). SARS-CoV-2 is a novel pathogenic beta coronavirus that infects humans causing severe respiratory illness. However, multifarious factors can contribute to the susceptibility to COVID-19 related morbidity and mortality such as age, gender and underlying comorbidities. Importantly, SARS-CoV and SARS-CoV-2 entry into the host cells is mediated via ACE2 receptor. However, ACE2 receptor binding affinity to SARS-CoV-2 is 4 folds higher than that to SARS-CoV. Identification of different aspects such as binding affinity, differential antigenic profiles of spike glycoproteins, and ACE2 polymorphisms might influence the investigation of potential therapeutic strategies targeting SARS-CoV-2/ACE2 binding interface. Here we aim to elaborate on SARS-CoV-2 S1/ACE2 ligand that facilitates viral internalization as well as to highlight the differences between SARS-CoVs binding affinity to ACE2. We also discuss the possible immunogenic sequences of spike glycoprotein and the effect of ACE2 polymorphism on viral binding/infectivity and host susceptibility to disease. Furthermore, targeting of ACE2 will be discussed to understand its role in therapeutics.

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Section: Sars-supporting

confidence: 57%

SARS-CoV-2 S Protein Binding hACE2: Viral Entry, Pathogenesis, Prognosis, and Potential Therapeutic Targets

Al-Zaidan¹,

Mestiri²,

Raza³

et al. 2020

Preprint

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“…Each S protomer consists of S1 and S2 domains with the receptor binding domain (RBD) located on the S1 domain ( Narkhede et al, 2020 ). S1 domain amino acid extended from 1 – 745 where (RBD) located in it extended from 375 – 604 ( Han et al, 2017 ). Amino acid residues of the SARS-CoV-2 RBD LYS417, GLY446, TYR449, TYR453, LEU455, PHE456, ALA475, PHE486, ASN487, LYS489, GLN493, GLY496, GLN498, THR500, ASN501, GLY502 and LYS505 Are the residues in contact to ACE2 ( Lan et al, 2020 ).…”

Section: Resultsmentioning

confidence: 99%

Optimization and evaluation of propolis liposomes as a promising therapeutic approach for COVID-19

Refaat

Mady

Sarhan

et al. 2021

International Journal of Pharmaceutics

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“…3b). SARS-CoV, MERS-CoV, HKU4 and HKU5 have receptor-binding motif (RBM) in this insertion region responsible for binding their respective protein receptors 45 . In the CTD of HKU2, there is only one short loop between the β5 and β6 strands of the core twisted β-sheet (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…Cryo-EM structures of spike trimer from all four coronavirus genera have been reported: the α-coronavirus spike structures are determined for HCoV-NL63 31 , HCoV-229E 27 and PEDV 32 ; the β-coronavirus spike structures are determined for MHV 33,34 , HCoV-HKU1 35 , HCoV-OC43 29 , SARS-CoV 21,36–38 and MERS-CoV 36,39,40 ; the γ-coronavirus spike structure is determined for IBV 41 and the δ-coronavirus spike structure is determined for PdCoV 42,43 . The cryo-EM structures of bat coronavirus spike trimers have not been reported, and only crystal structures of the CTD from HKU4 44 , HKU5 45 and HKU9 46 were determined.…”

Section: Introductionmentioning

confidence: 99%

Cryo-EM structures of HKU2 and SADS-CoV spike glycoproteins and insights into coronavirus evolution

Qiao

Guo

et al. 2020

Preprint

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19A new porcine coronavirus SADS-CoV was recently identified from suckling piglets 20 with severe diarrhea in southern China and its genome sequence is most identical (~95% 21 identity) to that of bat α-coronavirus HKU2. It again indicates bats are the natural 22 reservoir of many coronaviruses that have great potential for cross-species transmission 23 to animals and humans by recombination and/or mutation. Here we report the cryo-EM 24 structures of HKU2 and SADS-CoV spike glycoprotein trimers at 2.38 Å and 2.83 Å 25 resolution, respectively. HKU2 and SADS-CoV spikes exhibit very high structural 26 similarity, with subtle differences mainly distributed in the NTD and CTD of the S1 27 subunit responsible for cell attachment and receptor binding. We systematically 28 analyzed and compared the NTD, CTD, SD1 and SD2 domains of the S1 subunit and 29 the S2 subunit of HKU2 spike with those of α-, β-, γ-, and δ-coronavirus spikes. The 30 results show that the NTD and CTD of HKU2/SADS-CoV are probably the most 31 ancestral in the evolution of spike. Although the S2 subunit mediating membrane fusion 32 is highly conserved, the connecting region after fusion peptide in HKU2/SADS-CoV 33 S2 subunit also adopts a conformation distinct from other coronaviruses. These results 34 structurally demonstrate a close evolutionary relationship between HKU2 /SADS-CoV 35 and β-coronavirus spikes and provide new insights into the evolution and cross-species 36 transmission of coronaviruses. : bioRxiv preprint 39 Coronaviruses, categorized into the order Nidovirales family Coronaviridae and 40 subfamily Coronavirinae, are a large group of viral pathogens with a wide host range 1 . 41 Their infections in humans, other mammals and birds can cause respiratory, hepatic, 42 enteric and neurological diseases with varying severity 2 . The severe acute respiratory 43 syndrome coronavirus (SARS-CoV) and Middle East respiratory syndrome coronavirus 44 (MERS-CoV) have posed severe threats to human health in the 21 st century 1,3 . In the 45 meantime, coronaviruses infecting domestic animals also bring substantial economic 46 losses 4 . For example, the swine acute diarrhea syndrome coronavirus (SADS-CoV) 47 (also known as SeACoV and PEAV) isolated in 2017 caused outbreaks of severe watery 48 diarrhea of suckling piglets with a mortality up to 90% in several commercial pig farms 49 in Guangdong Province of China 5-10 . SADS-CoV is an α-coronavirus and other 50 representative members in the α-genus are porcine epidemic diarrhea virus 51 (PEDV), porcine transmissible gastroenteritis coronavirus (TGEV), porcine respiratory 52 coronavirus (PRCV), human NL63 and 229E coronaviruses (HCoV-NL63 and HCoV-53 229E) 1 . Representative members in other three genera include mouse hepatitis 54 coronavirus (MHV), bovine coronavirus (BCoV), SARS-CoV, MERS-CoV, HCoV-55 OC43 and HCoV-HKU1 in the β-genus, avian infectious bronchitis virus (IBV) in the 56 γ-genus and porcine deltacoronavirus (PdCoV) in the δ-genus 1 . 57 Cross-species transmission promoted by genetic r...

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Structure of the S1 subunit C-terminal domain from bat-derived coronavirus HKU5 spike protein

Cited by 14 publications

References 47 publications

SARS-CoV-2 S Protein Binding hACE2: Viral Entry, Pathogenesis, Prognosis, and Potential Therapeutic Targets

SARS-CoV-2 S Protein Binding hACE2: Viral Entry, Pathogenesis, Prognosis, and Potential Therapeutic Targets

Optimization and evaluation of propolis liposomes as a promising therapeutic approach for COVID-19

Cryo-EM structures of HKU2 and SADS-CoV spike glycoproteins and insights into coronavirus evolution

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