A structural view of coronavirus–receptor interactions

Reguera, Juan; Mudgal, Gaurav; Santiago, César; Casasnovas, José M.

doi:10.1016/j.virusres.2014.10.005

Cited by 58 publications

(52 citation statements)

References 81 publications

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“…Substitution of these two amino acids with the human-specific N479 and T487, either individually or in combination, dramatically increases the affinity of S for the human receptor [64,68]. This increased binding affinity is believed to be related to the elimination of unfavorable free charges at the interface upon mutation [70] and the extra contacts established by the methyl group of T487 [71]. Residue changes at other positions in the RBM might also be related to the SARS-CoV adaption.…”

Section: Feature Reviewmentioning

confidence: 99%

Bat-to-human: spike features determining ‘host jump’ of coronaviruses SARS-CoV, MERS-CoV, and beyond

Wang

Gao

2015

Trends in Microbiology

580

590

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Both severe acute respiratory syndrome coronavirus (SARS-CoV) and Middle East respiratory syndrome coronavirus (MERS-CoV) are zoonotic pathogens that crossed the species barriers to infect humans. The mechanism of viral interspecies transmission is an important scientific question to be addressed. These coronaviruses contain a surface-located spike (S) protein that initiates infection by mediating receptor-recognition and membrane fusion and is therefore a key factor in host specificity. In addition, the S protein needs to be cleaved by host proteases before executing fusion, making these proteases a second determinant of coronavirus interspecies infection. Here, we summarize the progress made in the past decade in understanding the cross-species transmission of SARS-CoV and MERS-CoV by focusing on the features of the S protein, its receptor-binding characteristics, and the cleavage process involved in priming.

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Section: Feature Reviewmentioning

confidence: 99%

Bat-to-human: spike features determining ‘host jump’ of coronaviruses SARS-CoV, MERS-CoV, and beyond

Wang

Gao

2015

Trends in Microbiology

580

590

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“…We identified DEGs with DEseq2 by screening for differential genes with a fold change ≥2.00 and an adjusted P-value ≤ 0.05 was based on method described previously by Ref. [16].…”

Section: Rnaseq Data Analysesmentioning

confidence: 99%

Transcriptomic analysis of small intestinal mucosa from porcine epidemic diarrhea virus infected piglets

Sun

Fahd

et al. 2019

Microbial Pathogenesis

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A B S T R A C TCaused by porcine epidemic diarrhea virus (PEDV), porcine epidemic diarrhea (PED) is an acute infectious disease which causes damage to the intestine including intestinal villus atrophy and shedding, leading to serious economic losses to the pig industry worldwide. In order to obtain detailed information about the pathogenesis and host immune response in a PEDV-infected host for first In vivo study we used high-throughput sequencing to analyze the gene expression differences of the small intestinal mucosa after infection with PEDV. Transcripts obtained were over 65,525,000 clean reads after reassembly were 22,605 genes detected, of which 22,248 were known genes and 371 new genes were predicted. Moreover, 3168 genes expression was up-regulated and 3876 genes down-regulated. (Gene Ontology) GO annotation and functional enrichment analysis indicated that all of the DEGs (differentially expressed genes) were annotated into biological process, cellular component and molecular function. Most of these unigenes are annotated in cellular processes, the cell and binding. KEGG analysis of the DEGs showed that a total of 7044 DEGs unigenes were annotated into 323 pathways classified into 6 main categories. Most of these unigenes are annotated were related to immune system response to the infectious diseases pathways. In addition, 20 DEGs were verified by quantitative real-time PCR. As the first, in vivo, RNAseq analysis of piglets and PEDV infection, our study provides knowledge about the transcriptomics of intestinal mucosa in PEDV-infected piglets, from which a complex molecular pathways and pathogenesis-related biological processes are involved in PEDV interaction with piglet intestinal mucosa.

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“…The receptor binding domain (RBD) within the S1 subunit and the heptad repeat region within the S2 subunit were mapped (38). Some authors speculate that S1 also contains a domain responsible for binding to the attachment receptors on the cell surface, which triggers binding with ACE2 (27,41). Of note, it has been shown that purified full-length S protein of HCoV-NL63 exhibits surprisingly low-affinity binding to its putative receptor (43).…”

Section: Discussionmentioning

confidence: 99%

Membrane Protein of Human Coronavirus NL63 Is Responsible for Interaction with the Adhesion Receptor

Naskalska

Dąbrowska

Szczepański

et al. 2019

J Virol

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Human coronavirus NL63 (HCoV-NL63) is a common respiratory virus that causes moderately severe infections. We have previously shown that the virus uses heparan sulfate proteoglycans (HSPGs) as the initial attachment factors, facilitating viral entry into the cell. In the present study, we show that the membrane protein (M) of HCoV-NL63 mediates this attachment. Using viruslike particles lacking the spike (S) protein, we demonstrate that binding to the cell is not S protein dependent. Furthermore, we mapped the M protein site responsible for the interaction with HSPG and confirmed its relevance using a viable virus. Importantly, in silico analysis of the region responsible for HSPG binding in different clinical isolates and the Amsterdam I strain did not exhibit any signs of cell culture adaptation. IMPORTANCE It is generally accepted that the coronaviral S protein is responsible for viral interaction with a cellular receptor. Here we show that the M protein is also an important player during early stages of HCoV-NL63 infection and that the concerted action of the two proteins (M and S) is a prerequisite for effective infection. We believe that this study broadens the understanding of HCoV-NL63 biology and may also alter the way in which we perceive the first steps of cell infection with the virus. The data presented here may also be important for future research into vaccine or drug development.

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A structural view of coronavirus–receptor interactions

Cited by 58 publications

References 81 publications

Bat-to-human: spike features determining ‘host jump’ of coronaviruses SARS-CoV, MERS-CoV, and beyond

Bat-to-human: spike features determining ‘host jump’ of coronaviruses SARS-CoV, MERS-CoV, and beyond

Transcriptomic analysis of small intestinal mucosa from porcine epidemic diarrhea virus infected piglets

Membrane Protein of Human Coronavirus NL63 Is Responsible for Interaction with the Adhesion Receptor

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