Evidence for a coiled-coil structure in the spike proteins of coronaviruses. Journalof Molecular Biology 196

Evidence for a coiled-coil structure in the spike proteins of coronaviruses. Journalof Molecular Biology 196 (1987)

by R J DE GROOT, W LUYTJES, M C HORZINEK, B A M VAN DER ZEIJST, W J M SPAAN, J A LENSTRA

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The genome organization of the Nidovirales: similarities and differences between arteri-, toro-, and coronaviruses

by Antoine A. F. De Vries, Marian C. Horzinek, Peter J. M. Rottier, Raoul J. De Groot - Semin Virol , 1997

"... Viruses in the families Arteriviridae and Coronaviridae have enveloped virions which contain nonseg-mented, positive-stranded RNA, but the constituent genera differ markedly in genetic complexity and virion structure. Nevertheless, there are striking resemblances among the viruses in the organizatio ..."

Abstract - Cited by 49 (11 self) - Add to MetaCart

Viruses in the families Arteriviridae and Coronaviridae have enveloped virions which contain nonseg-mented, positive-stranded RNA, but the constituent genera differ markedly in genetic complexity and virion structure. Nevertheless, there are striking resemblances among the viruses in the organization and expression of their genomes, and sequence conservation among the polymerase polyproteins strongly suggests that they have a common ancestry. On this basis, the International Committee on Taxonomy of Viruses recently established a new order, Nidovirales, to contain the two families. Here, the common traits and distinguishing features of the Nidovirales are reviewed. r 1997 Academic Press KEY WORDS: arterivirus; coronavirus; torovirus; polyprotein processing; RNA recombination.

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Antigenic domains on the peplomer protein of avian infectious bronchitis virus: correlation with biological functions

by G. Koch, L. Hartog, A. Kant, D. J. Van Roozelaar - J. Gen. Virol , 1990

"... Monoclonal antibodies (MAbs) directed against struc-tural proteins of infectious bronchitis virus (IBV) were produced to analyse the antigenic structure of this virus. Competitive binding of enzyme-labelled and unlabelled MAbs to IBV peplomer protein was ana-lysed in an antibody binding assay to tes ..."

Abstract - Cited by 19 (0 self) - Add to MetaCart

Monoclonal antibodies (MAbs) directed against struc-tural proteins of infectious bronchitis virus (IBV) were produced to analyse the antigenic structure of this virus. Competitive binding of enzyme-labelled and unlabelled MAbs to IBV peplomer protein was ana-lysed in an antibody binding assay to test the relatedness ofthe epitopes defined by the MAbs. Based on the competition groups, eight epitope clusters were defined (S-A to S-H); six of these clusters (S1-A to S I-F) were located on the S1 subunit and two (S2-G and S2-H) on the $2 subunit of the peplomer protein. Epitope clusters S1-A and S1-B overlapped extensive-ly. The biological activities of the MAbs were deter-mined and correlated to the epitope clusters. Mono-clonal antibodies directed against epitope clusters S1-A to S1-E and one MAb directed against cluster S2-G moderately tostrongly neutralized IBV at titres higher than 2 log~o, whereas the remaining MAbs, directed against S1 and $2, neutralized at titres lower than 2 log~o. One MAb, directed against cluster S1-D, inhibited the agglutination of chicken erythrocytes.

Localization f antigenic sites of the E2 glycoprotein oftransmissible gastroenteritis coronavirus

by I CORREA, F GEBAUER, M J BULLIDO, C SuIl, M F D BAAY, K A ZWAAGSTRA, W P A POSTHUMUS, J A LENSTRA, L EN IUANES - Journal of General Virology , 1990

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Abstract - Cited by 18 (5 self) - Add to MetaCart

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Nucleotide sequence of the gene encoding the spike glycoprotein of human coronavirus HCV 229E

by Thomas Raabe, Barbara Schelle-prinz, Stuart G. Siddell - J. Gen. Virol , 1990

"... The gene encoding the spike glycoprotein of the human coronavirus HCV 229E has been cloned and sequenced. This analysis predicts an S polypeptide of 1173 amino acids with an M, of 128600. The polypeptide has 30 potential N-glycosylation sites. A number of structural features typical of coronavirus S ..."

Abstract - Cited by 14 (4 self) - Add to MetaCart

The gene encoding the spike glycoprotein of the human coronavirus HCV 229E has been cloned and sequenced. This analysis predicts an S polypeptide of 1173 amino acids with an M, of 128600. The polypeptide has 30 potential N-glycosylation sites. A number of structural features typical of coronavirus S proteins can be recognized, including a signal sequence, a membrane anchor, heptad repeat structures and a carboxy-terminal cysteine cluster. A detailed, computer-aided comparison with the S proteins of infectious bronchitis virus, feline infectious peritonitis virus, transmissible gastroenteritis virus and murine hepatitis virus, strain JHM is presented. We have also done a Northern blot analysis of viral RNAs in HCV 229Einfected cells using synthetic oligonucleotides. On the basis of this analysis, and by analogy to the replication strategy of other coronaviruses, we are able to propose a model for the organization and expression of the HCV 229E genome.

2003. Variable sensitivity to substitutions in the N-terminal heptad repeat of Mason-Pfizer monkey virus transmembrane protein

by Chisu Song, Eric Hunter, Chisu Song, Eric Hunter - J

"... This article cites 47 articles, 26 of which can be accessed free ..."

Abstract - Cited by 11 (5 self) - Add to MetaCart

This article cites 47 articles, 26 of which can be accessed free

Molecular characterization of the S protein gene of human coronavirus OC43

by Samir Mounir, Pierre J - J. Gen , 1993

"... The gene encoding the spike protein of the OC43 strain of human coronavirus (HCV-OC43) was cloned and sequenced. The complete nucleotide sequence revealed an open reading frame of 4062 nucleotides encoding a protein of 1353 amino acids with a predicted M r of 150078. Structural features include 22 N ..."

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The gene encoding the spike protein of the OC43 strain of human coronavirus (HCV-OC43) was cloned and sequenced. The complete nucleotide sequence revealed an open reading frame of 4062 nucleotides encoding a protein of 1353 amino acids with a predicted M r of 150078. Structural features include 22 N-glycosylation sites, an N-terminal hydrophobic signal sequence of 17 amino acids, an hydrophilic cysteine-rich sequence of 35 amino acids near the C terminus, and a potential proteolytic cleavage site (RRSR) between amino acid residues 758 and 759, yielding S1 and $2 segments of 84730 and 65 366 M r, respectively. The predicted amino acid sequence of the spike protein of HCV-OC43 has 91 % identity with that of the Mebus strain of bovine coronavirus, revealing more sequence divergence in the putative bulbous part (S1) than in the predicted stem region ($2). Human coronaviruses (HCV) are enveloped positive-stranded RNA viruses that cause respiratory infections and have been associated with gastrointestinal nd

Bovine coronavirus peplomer glycoproteins: detailed antigenic analyses of S1, $2 and HE

by Jean-francois Vautherot, P Scal Boireau, Jacques Laporte - Journal of General Virology , 1992

"... Forty-four monoclonal antibodies (MAbs) to the G11o isolate of bovine enteric oronavirus were used for the characterization f the peplomer proteins S and HE. Fourteen of these MAbs reacted with HE and the remaining 30 with the products of the S gene, S1 (19 MAbs), $2 (six MAbs) and gp200 (five MAbs) ..."

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Forty-four monoclonal antibodies (MAbs) to the G11o isolate of bovine enteric oronavirus were used for the characterization f the peplomer proteins S and HE. Fourteen of these MAbs reacted with HE and the remaining 30 with the products of the S gene, S1 (19 MAbs), $2 (six MAbs) and gp200 (five MAbs). S1 and HE were found to carry major neutralization determi-nants, and S 1 appeared to elicit the production of the MAbs displaying the highest neutralizing activity. The topography of the epitopes was assessed by means of a competitive binding assay; the 44 MAbs defined four independent antigenic domains on S1, two on $2, one on gp200 and two on HE. All the neutralizing anti-S1 MAbs mapped in antigenic sites A and B and all the neutralizing anti-HE MAbs in HE-B. Antigenic site S1-B was further subdivided into four subsites. Func-tional mapping was performed by testing a library of neutralization-resistant mu ants against he neutraliz-ing MAbs. Analysis of their reactivity in a neutral-ization test confirmed the overall distribution of epitopes in S1-B and HE-B.