Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Comparative Study
. 1990 Nov;179(1):463-8.
doi: 10.1016/0042-6822(90)90316-j.

Sequence comparison of the N genes of five strains of the coronavirus mouse hepatitis virus suggests a three domain structure for the nucleocapsid protein

M M Parker  1 , P S Masters
Affiliations
Comparative Study

Sequence comparison of the N genes of five strains of the coronavirus mouse hepatitis virus suggests a three domain structure for the nucleocapsid protein

M M Parker et al. Virology. 1990 Nov.

Abstract

To obtain information about the structure and evolution of the nucleocapsid (N) protein of the coronavirus mouse hepatitis virus (MHV), we determined the entire nucleotide sequences of the N genes of MHV-A59, MHV-3, MHV-S, and MHV-1 from cDNA clones. At the nucleotide level, the N gene sequences of these viral strains, and that of MHV-JHM, were more than 92% conserved overall. Even higher nucleotide sequence identity was found in the 3' untranslated regions (3' UTRs) of the five strains, which may reflect the role of the 3' UTR in negative-strand RNA synthesis. All five N genes were found to encode markedly basic proteins of 454 or 455 residues having at least 94% sequence identity in pairwise comparisons. However, amino acid sequence divergences were found to be clustered in two short segments of N, putative spacer regions that, together, constituted only 11% of the molecule. Thus, the data suggest that the MHV N protein is composed of three highly conserved structural domains connected to each other by regions that have much less constraint on their amino acid sequences. The first two conserved domains contain most of the excess of basic amino acid residues; by contrast, the carboxy-terminal domain is acidic. Finally, we noted that four of the five N genes contain an internal open reading frame that potentially encodes a protein of 207 amino acids having a large proportion of basic and hydrophobic residues.

PubMed Disclaimer

Similar articles

See all similar articles

Cited by

See all "Cited by" articles

References

    1. Sturman L.S., Holmes K.V. Adv. Virus Res. 1983;28:35–111. - PMC - PubMed
    1. Lai M.M.-C. BioEssays. 1986;5:257–260. - PMC - PubMed
    1. Spaan W., Cavanagh D., Horzinek M.C. J. Gen. Virol. 1988;69:2939–2952. - PubMed
    1. Gledhill A.W., Andrewes C.H. Brit. J. Exp. Pathol. 1951;32:559–568. - PMC - PubMed
    1. Dick G.W.A., Niven I.S.F., Gledhill A.W. Brit. J. Exp. Pathol. 1956;37:90–98. - PMC - PubMed

Publication types

Substances

LinkOut - more resources