Furin cleavage of the SARS coronavirus spike glycoprotein enhances cell–cell fusion but does not affect virion entry

Follis, Kathryn E.; York, Joanne; Nunberg, Jack H.

doi:10.1016/j.virol.2006.02.003

Cited by 220 publications

(226 citation statements)

References 67 publications

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“…In spite of lacking conserved cleavage sites, they all consist of two domains, S1 and S2, showing the conserved GxCx motif in S1 around the cleavage site and the conserved nonamer motif IPTNFSISI or similar motif in S2. These motifs have been observed in other known CoVs (Follis et al, 2006). The S1 is responsible for virus binding to the receptor on the target cells and may contain receptor binding domains (RBDs) that directly bind to host cellular receptors.…”

Section: Partial Genome Sequence and Organizationmentioning

confidence: 84%

“…As shown in Fig. 2, spike proteins of the seven bat CoVs lack furin protease recognition site, such as RRADR-S in Murine Hepatitis Virus (MHV), RRSRG-A in human CoV OC43 (HCoV OC43), RRSRR-A in bovine CoV (BCoV) (Follis et al, 2006), and cathepsin L cleavage site (VAYT-M) as in SARS-CoV (Bosch et al, 2008). In spite of lacking conserved cleavage sites, they all consist of two domains, S1 and S2, showing the conserved GxCx motif in S1 around the cleavage site and the conserved nonamer motif IPTNFSISI or similar motif in S2.…”

Section: Partial Genome Sequence and Organizationmentioning

confidence: 99%

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Genomic characterization of seven distinct bat coronaviruses in Kenya

et al. 2012

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To better understand the genetic diversity and genomic features of 41 coronaviruses (CoVs) identified from Kenya bats in 2006, seven CoVs as representatives of seven different phylogenetic groups identified from partial polymerase gene sequences, were subjected to extensive genomic sequencing. As a result, 15-16kb nucleotide sequences encoding complete RNA dependent RNA polymerase, spike, envelope, membrane, and nucleocapsid proteins plus other open reading frames (ORFs) were generated. Sequences analysis confirmed that the CoVs from Kenya bats are divergent members of Alphacoronavirus and Betacoronavirus genera. Furthermore, the CoVs BtKY22, BtKY41, and BtKY43 in Alphacoronavirus genus and BtKY24 in Betacoronavirus genus are likely representatives of 4 novel CoV species. BtKY27 and BtKY33 are members of the established bat CoV species in Alphacoronavirus genus and BtKY06 is a member of the established bat CoV species in Betacoronavirus genus. The genome organization of these seven CoVs is similar to other known CoVs from the same groups except for differences in the number of putative ORFs following the N gene. The present results confirm a significant diversity of CoVs circulating in Kenya bats. These Kenya bat CoVs are phylogenetically distant from any previously described human and animal CoVs. However, because of the examples of host switching among CoVs after relatively minor sequence changes in S1 domain of spike protein, a further surveillance in animal reservoirs and understanding the interface between host susceptibility is critical for predicting and preventing the potential threat of bat CoVs to public health.

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Section: Partial Genome Sequence and Organizationmentioning

confidence: 84%

Section: Partial Genome Sequence and Organizationmentioning

confidence: 99%

Genomic characterization of seven distinct bat coronaviruses in Kenya

et al. 2012

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“…In the case of PEDV, the S protein could not be cleaved into S1 and S2 subunits, due to a lack of proteolytic cleavage sites (Duarte and Laude, 1994;Park et al, 2006;Yeo et al, 2003). However, the S1 domain (residues 1-789) and the S2 domain (residues 790-1383) have been artificially defined by the conserved nonamer and the GxCx motifs at the position of S protein cleavage sites in coronavirus group II members (Follis et al, 2006). Based on bioinformatics analysis of the S protein structure of other coronaviruses, the S1 domain is thought to form the spherical head of the S protein, and is easily accessible to neutralizing antibodies.…”

Section: Discussionmentioning

confidence: 99%

Identification of two novel B cell epitopes on porcine epidemic diarrhea virus spike protein

Sun

Feng

Shi

et al. 2008

Veterinary Microbiology

179

175

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S1D (residues 636-789) is a neutralizing epitope region on the spike protein (S) of porcine epidemic diarrhea virus (PEDV). To accurately identify epitopes on S1D, the S1-phage library containing the gene encoding the S1D region of PEDV S protein was micropanned by six specific monoclonal antibodies (McAbs) against the S1D region. These micropanned epitope regions (MER) were focused on 696-779 amino acids of the S protein. To further map epitopes of the MER, seven overlapping mini-fragments covering MER nucleotides were separately synthesized and expressed in Escherichia coli BL21 with a GST tag. These mini-GST fusion proteins were scanned by ELISA and Western blotting with the six McAbs, and the result showed that S1D5 (residues 744-759) and S1D6 (residues 756-771) are two linear epitopes of the PEDV S protein. The antisera of the epitopes S1D5 and S1D6 could react with the native S protein of PEDV. Furthermore, Pepscan of the two linear epitopes demonstrated that SS2 ((748)YSNIGVCK(755)) and SS6 ((764)LQDGQVKI(771)) are two core epitopes on S1D5 and S1D6, respectively, located on the S protein of PEDV.

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“…As with several coronaviruses, the spike glycoprotein can be proteolytically cleaved into two non-covalently associated glycoproteins: the virion-associated S1 (666 amino acid residues) containing the receptor attachment site and the transmembrane-anchored S2 (583 residues) responsible for fusion activity (Bergeron et al, 2005; Follis et al, 2006; Li et al, 2005). …”

Section: Introductionmentioning

confidence: 99%

Identification of N-linked carbohydrates from severe acute respiratory syndrome (SARS) spike glycoprotein

Ritchie¹,

Harvey²,

et al. 2010

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N-glycans were released from the SARS coronavirus (SARS-CoV) spike glycoprotein produced in Vero E6 cells and their structures were determined by a combination of matrix-assisted laser desorption/ionization (MALDI) mass spectrometry, negative ion electrospray collision-induced dissociation time-of-flight mass spectrometry and normal-phase high-performance liquid chromatography with exoglycosidase digestion. Major glycans were high-mannose (Man5–9GlcNAc2), hybrid and bi-, tri- and tetra-antennary complex with and without bisecting GlcNAc and core fucose. Complex glycans with fewer than the full complement of galactose residues were present and sialylation was negligible. Treatment with the glucosidase inhibitor N-butyl-deoxynojirimycin (NB-DNJ) inhibited N-glycan processing as evidenced by the appearance of glycans of composition Glc3Man7–9GlcNAc2. However, some complex glycans remained suggesting the presence of an α-endomannosidase. Our data in tissue culture indicate that inhibition of N-glycan processing may be considered as a therapeutic strategy against SARS CoV infections.

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Furin cleavage of the SARS coronavirus spike glycoprotein enhances cell–cell fusion but does not affect virion entry

Cited by 220 publications

References 67 publications

Genomic characterization of seven distinct bat coronaviruses in Kenya

Genomic characterization of seven distinct bat coronaviruses in Kenya

Identification of two novel B cell epitopes on porcine epidemic diarrhea virus spike protein

Identification of N-linked carbohydrates from severe acute respiratory syndrome (SARS) spike glycoprotein

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