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Sequence and analysis of BECV F15 matrix protein
E Savoysky1, P Boireau, C Finance
1Laboratoire de Microbiologie Appliquée, Faculté des Sciences Pharmaceutiques et Biologiques, Nancy, France.
Abstract:
Clones from the bovine enteric coronavirus (F15) cDNA library were cloned in pBR322 and sequenced by the method of Sanger and Coulson. This led to the identification of a sequence of 1,300 bases which contained a single open reading frame of 690 bases yielding a protein having properties of the matrix protein (M). It was comprised of 230 amino acids with a molecular weight of 26,376 Da. It was hydrophobic and had a net charge of +8 at neutral pH. Analysis of its secondary structure could not establish a simple transmembrane arrangement of the amino acids. Comparison of its nucleotide sequence with that of BECV Mebus strain showed only a two-base change resulting in a 100% homology between the two amino acid sequences. Furthermore, a very conserved structure of M appeared on comparison with the Dayoff optimal alignment of MHV-A59, MHV-JHM, TGEV, IBV Beaudette and IBV 6/82M amino acid sequences. As the two strains of BECV, F15 and Mebus present some antigenic differences, this led us to reconsider the role of M in viral antigen specificity. A hypothesis is that, as it seems to possess the necessary information on its transmembrane region, it is an ideal candidate for the viral budding process.
Insights
Researchers identified the matrix protein (M) of bovine enteric coronavirus (BECV). This conserved protein, crucial for viral budding, shows high homology between BECV strains despite antigenic differences.
Area of Science:
- Virology
- Molecular Biology
Background:
- Bovine enteric coronavirus (BECV) causes significant enteric disease in cattle.
- Understanding the molecular components of BECV is essential for developing effective control strategies.
Purpose of the Study:
- To characterize the matrix protein (M) of a BECV F15 strain.
- To investigate the conservation and potential role of the BECV M protein in viral antigenicity and replication.
Main Methods:
- Cloning and sequencing of BECV F15 cDNA library using Sanger and Coulson methods.
- Bioinformatic analysis of the identified M protein sequence, including secondary structure prediction and homology comparisons.
Main Results:
- A 1,300-base sequence containing a 690-base open reading frame encoding a 230-amino acid matrix (M) protein (26,376 Da) was identified.
- The BECV M protein is hydrophobic with a net charge of +8 at neutral pH. Its secondary structure analysis did not reveal a simple transmembrane arrangement.
- High homology (100% amino acid identity) was observed between the M proteins of BECV F15 and Mebus strains, with significant conservation across other coronaviruses.
Conclusions:
- The BECV M protein is highly conserved, suggesting a critical role in viral structure or function.
- Despite high M protein homology, antigenic differences between BECV strains warrant further investigation into M's role in viral antigen specificity.
- The M protein's characteristics suggest it is a strong candidate for mediating the viral budding process.
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