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Molecular analysis of the S1 subunit of the spike glycoprotein of respiratory and enteric bovine coronavirus isolates.

ABSTRACT: It is unclear whether respiratory and enteric bovine coronavirus (BoCV) strains are distinctive in biological, antigenic and genetic characteristics. In the present study, we analyzed the nucleotide and amino acid sequence of the S1 subunit of the S glycoprotein, including the cleavage site, of both respiratory (n=5) and enteric (n=3) BoCV isolates including two paired isolates from the same feedlot animals and compared them with the prototype Mebus and two enteric and one respiratory BoCV strains from Quebec. A total of 75 polymorphic nucleotides were identified in the S1 subunit of the spike glycoprotein of BoCV isolates compared with the Mebus strain. These polymorphisms led to 42 amino acid changes at 38 distinct sites. The amino acid changes were distributed throughout the S1 subunit with clustering around residues 40-118, 146-179, and 458-531. Among these variations, only 19 amino acid substitutions altered the charge, hydrophobicity and surface probability of the protein. Based on phylogenetic analysis, our respiratory and enteric isolates clustered into two major groups with two subgroups. Although, there were only a few amino acid changes between the respiratory and enteric paired isolates, the other two respiratory isolates, one isolated from the same farm as a paired strain and the other from a different farm, showed more sequence diversity. Amino acid alterations in residues 113, 115, 118, 146, 148, 501, 510 and 531 of respiratory isolates conferred significant changes in the predicted secondary structure compared with the prototype winter dysentery (WD) and the calf diarrhea (CD) strains of BoCV. In conclusion, the data suggests that respiratory strains of BoCV may differ genetically from the classical calf enteric and adult WD strains.

SUBMITTER: Hasoksuz M

PROVIDER: S-EPMC7127276 | biostudies-literature | 2002 Mar

REPOSITORIES: biostudies-literature

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Molecular analysis of the S1 subunit of the spike glycoprotein of respiratory and enteric bovine coronavirus isolates.

Hasoksuz Mustafa M Sreevatsan Srinand S Cho Kyoung Oh KO Hoet Armando E AE Saif Linda J LJ

Virus research 20020301 1-2

It is unclear whether respiratory and enteric bovine coronavirus (BoCV) strains are distinctive in biological, antigenic and genetic characteristics. In the present study, we analyzed the nucleotide and amino acid sequence of the S1 subunit of the S glycoprotein, including the cleavage site, of both respiratory (n=5) and enteric (n=3) BoCV isolates including two paired isolates from the same feedlot animals and compared them with the prototype Mebus and two enteric and one respiratory BoCV strai ...[more]

PMID: 11900843

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Project description:The novel coronavirus originated in December 2019 in Hubei, China. This contagious disease named as COVID-19 resulted in a massive expansion within 6 months by spreading to more than 213 countries. Despite the availability of antiviral drugs for the treatment of various viral infections, it was concluded by the WHO that there is no medicine to treat novel CoV, SARS-CoV-2. It has been confirmed that SARS-COV-2 is the most highly virulent human coronavirus and occupies the third position following SARS and MERS with the highest mortality rate. The genetic assembly of SARS-CoV-2 is segmented into structural and non-structural proteins, of which two-thirds of the viral genome encodes non-structural proteins and the remaining genome encodes structural proteins. The most predominant structural proteins that make up SARS-CoV-2 include spike surface glycoproteins (S), membrane proteins (M), envelope proteins (E), and nucleocapsid proteins (N). This review will focus on one of the four major structural proteins in the CoV assembly, the spike, which is involved in host cell recognition and the fusion process. The monomer disintegrates into S1 and S2 subunits with the S1 domain necessitating binding of the virus to its host cell receptor and the S2 domain mediating the viral fusion. On viral infection by the host, the S protein is further cleaved by the protease enzyme to two major subdomains S1/S2. Spike is proven to be an interesting target for developing vaccines and in particular, the RBD-single chain dimer has shown initial success. The availability of small molecules and peptidic inhibitors for host cell receptors is briefly discussed. The development of new molecules and therapeutic druggable targets for SARS-CoV-2 is of global importance. Attacking the virus employing multiple targets and strategies is the best way to inhibit the virus. This article will appeal to researchers in understanding the structural and biological aspects of the S protein in the field of drug design and discovery.

Dataset Information

Molecular analysis of the S1 subunit of the spike glycoprotein of respiratory and enteric bovine coronavirus isolates.

Publications

Molecular analysis of the S1 subunit of the spike glycoprotein of respiratory and enteric bovine coronavirus isolates.

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