Nucleotide sequence of the glycoprotein S gene of bovine enteric coronavirus and comparison with the S proteins of two mouse hepatitis virus strains

Boireau, Pascal; Crucière, Catherine; Laporte, J.

doi:10.1099/0022-1317-71-2-487

Cited by 38 publications

(39 citation statements)

References 31 publications

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“…Both proteins display typical features of glycoproteins forming the peplomers of enveloped viruses. S and HE are implanted in the viral membrane at their C terminus (Boireau et al, 1990;Kienzle et al, 1990), trigger the immune system eliciting the production of neutralizing antibodies (Vautherot et al, 1984(Vautherot et al, , 1992Deregt et al, 1987) and interact with receptors on the cell surface (Vlasak et al, 1988;Schultze et al, 1991a, b;Stortz et al, 1991).…”

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confidence: 99%

“…The S1 subunit presumably forms the bulbous upper part of the projections (Cavanagh, 1983) and bears type-specific neutralization determinants (Cavanagh et al, 1988;Yoo 0001-1149SGM et al, 1991Vautherot et al, 1992). The $2 subunit has been predicted to contain two long a helices which are involved in the formation of the stalk of the peplomer (De Groot et al, 1987;Boireau et al, 1990), and elicits the production of group-specific monoclonal antibodies (MAbs) (Talbot et al, 1988;Lenstra et al, 1989).…”

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confidence: 99%

“…Expression of the fusion protein is under the control of the 2r promoter, itself repressed by a thermolabile ci857 repressor inactivated by a temperature shift from 25 °C to 42 °C. cDNA clones G7, PG7-8, PG7-8-12 and P33-23 (Boireau et al, 1990) were used to generate 10 partially overlapping restriction fragments covering the entire S gene (Fig. 1, Table 1).…”

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confidence: 99%

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Bovine coronavirus spike glycoprotein: localization of an immunodominant region at the amino-terminal end of S2

Vautherot¹,

Laporte²,

Boireau³

1992

Journal of General Virology

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We have identified the binding site of monoclonal antibodies (MAbs) against the $2 subunit of the bovine coronavirus spike (S) glycoprotein. The location of this site was first investigated by using prokaryotic expression of DNA restriction fragments covering the entire S gene. The amino acid sequence containing the antibody binding site was shortened from 70 to 20 amino acids by digestion of plasmid DNA with exonuclease III, followed by sequencing of the smallest digestion product encoding an immunoreactive fusion protein. Finally we synthesized a set of nonapeptides covering the 20 amino acid sequence extending from the N-terminal residue of the $2 subunit (Ala 769 to Tyr 798). MAbs reacted mainly with six consecutive overlapping peptides with the sequence TTGYRFTN-FEPFTV. Polyclonal antibodies from hyperimmunized or convalescent animals reacted only with the recombinant proteins identified by MAbs, and the hyperimmune serum bound to the same set ofpeptides. This suggests that this highly conserved linear antigenic determinant corresponds to an immunodominant region. This region resembles both in location and immunodominance the linear determinant defined on the infectious bronchitis virus $2 subunit. The presence of similar regions in the N-terminal region of the $2 subunit of other coronaviruses is discussed.

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Bovine coronavirus spike glycoprotein: localization of an immunodominant region at the amino-terminal end of S2

Vautherot¹,

Laporte²,

Boireau³

1992

Journal of General Virology

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“…Except for HCoV-OC43, BCoV and TCoV, these viruses do not seem to cross-react by seroneutralization or haemagglutination inhibition, but they all share common antigenic determinants on their structural proteins, as demonstrated by indirect immunofluorescence, Western blotting and immunoprecipitation assays (Dea & Tijssen, 1989). The S glycoprotein possesses an N-terminal signal sequence, which is cleaved during intracellular processing, and thus is absent from the mature S protein (Abraham et al, 1991 ;Boireau et al, 1990 ;Parker et al, 1990a, b). The S protein is synthesized as a high-molecular-mass precursor, which, after glycosylation, undergoes proteolytic cleavage, a host-celldependent event, to yield two subunits of molecular mass 85-100 kDa corresponding to the N-terminal S1 and the C-terminal S2 glycopolypeptides (Boireau et al, 1990 ;Parker et al, 1990a, b).…”

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confidence: 99%

“…The S glycoprotein possesses an N-terminal signal sequence, which is cleaved during intracellular processing, and thus is absent from the mature S protein (Abraham et al, 1991 ;Boireau et al, 1990 ;Parker et al, 1990a, b). The S protein is synthesized as a high-molecular-mass precursor, which, after glycosylation, undergoes proteolytic cleavage, a host-celldependent event, to yield two subunits of molecular mass 85-100 kDa corresponding to the N-terminal S1 and the C-terminal S2 glycopolypeptides (Boireau et al, 1990 ;Parker et al, 1990a, b). Deduced amino acid sequences of BCoV and HCoV-OC43 revealed as much as 95, 91, 94 and 96 % identities between their HE, S, M and N proteins, respectively (Mounir & Talbot, 1992, 1993a.…”

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Sequence of the 3′-terminal end (8·1 kb) of the genome of porcine haemagglutinating encephalomyelitis virus: comparison with other haemagglutinating coronaviruses

Sasseville

Boutin

Gélinas

et al. 2002

Journal of General Virology

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Coronaviruses are enveloped, positive-stranded RNA viruses responsible for enteric, hepatitis, neurological and respiratory infections in humans and animals. Porcine haemagglutinating encephalomyelitis virus (HEV) is a member of the antigenic subgroup of haemagglutinating coronaviruses, including human respiratory coronavirus (HCoV-OC43), bovine coronavirus (BCoV) and some North American isolates of

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Roles in Cell-to-Cell Fusion of Two Conserved Hydrophobic Regions in the Murine Coronavirus Spike Protein

1998

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The spike (S) protein of coronavirus mouse hepatitis virus (MHV), mediates attachment and fusion during viral entry and cell-to-cell fusion later in infection. By analogy with other viral proteins that induce cell fusion the MHV S protein would be expected to have a hydrophobic stretch of amino acids that serves as a fusion peptide. Sequence analysis suggests that the S protein falls within the group of fusion proteins having internal rather than N-terminal fusion peptides. Based on the features of known viral fusion peptides, we identified two regions (PEP1 and PEP2) of MHV-A59 S2 as possible fusion peptides. Site-directed mutagenesis and an in viro cell-to-cell fusion assay were used to evaluate the roles of PEP1 and PEP2, as well as a third previously identified putative fusion domain (PEP3) in membrane fusion. Substitution of bulky hydrophobic residues with charged residues within PEP1 affects the fusion activity of the S protein without affecting processing and surface expression. Similar substitutions within PEP2 result in a fusion-negative phenotype; however, these mutant S proteins also exhibit defects in protein processing and surface expression which likely explain the loss of the ability to induce fusion. Thus PEP1 remains a candidate fusion peptide, while PEP2 may play a significant role in the overall structure or oligomerization of the S protein. PEP3 is an unlikely putative fusion peptide since it is not conserved among coronaviruses and nonconservative amino acid substitutions in PEP3 have minimal effects on cell-to-cell fusion.

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Nucleotide sequence of the glycoprotein S gene of bovine enteric coronavirus and comparison with the S proteins of two mouse hepatitis virus strains

Cited by 38 publications

References 31 publications

Bovine coronavirus spike glycoprotein: localization of an immunodominant region at the amino-terminal end of S2

Bovine coronavirus spike glycoprotein: localization of an immunodominant region at the amino-terminal end of S2

Sequence of the 3′-terminal end (8·1 kb) of the genome of porcine haemagglutinating encephalomyelitis virus: comparison with other haemagglutinating coronaviruses

Roles in Cell-to-Cell Fusion of Two Conserved Hydrophobic Regions in the Murine Coronavirus Spike Protein

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