Coronaviruses pp 123-129 | Cite as

Deduced Amino Acid Sequence and Potential O-Glycosylation Sites for the Bovine Coronavirus Matrix Protein

  • William Lapps
  • Brenda G. Hogue
  • David A. Brian
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 218)


The nucleotide sequence of the matrix (M) protein gene of the bovine coronavirus (BCV) was determined by sequencing cDNA clones derived from genomic RNA. The gene was found to map at the 5′ side of the nucleocapsid protein gene and its sequence predicts a protein of 230 amino acids having a molecular weight of 26,376. The BCV M protein shares extensive sequence homology with the matrix protein of the mouse hepatitis coronavirus (MHV) but differs notably in the amino terminal region external to the virion envelope where BCV apparently uses at least two of its six potential O-glycosylation sites.


Deduce Amino Acid Sequence Envelope Glycoprotein Viral Glycoprotein Amino Terminal Region Sequencing cDNA Clone 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


  1. Armstrong, J., H. Niemann, S. Smeekens, P. Rottier, and G. Warren. 1984. Sequence and topology of a model intracellular membrane protein, E1 glycoprotein, from a coronavirus. Nature 308: 751–752.PubMedCrossRefGoogle Scholar
  2. Collins, A. R., R. L. Knobler, H. Powell, and M. J. Buchmeier. 1982. Monoclonal antibodies to murine hepatitis virus-4 (strain JHM) define the viral glycoprotein responsible for attachment and cell-cell fusion. Virology 119: 358–371.PubMedCrossRefGoogle Scholar
  3. Gubler, U. and B. J. Hoffman. 1983. A simple and very efficient method for generating cDNA libraries. Gene 25: 263–269.PubMedCrossRefGoogle Scholar
  4. Hogue, B. G., B. King, and D. A. Brian. 1984. Antigenic relationships among proteins of bovine coronavirus, human respiratory coronavirus OC43, and mouse hepatitis coronavirus A59. J. Virol. 51: 384–388.PubMedGoogle Scholar
  5. Holmes, K. V., E. W. Doller, and L. S. Sturman. 1981. Tunicamycin resistant glycosylation of a coronavirus glycoprotein: demonstration of a novel type of viral glycoprotein. Virology 115: 334–344.PubMedCrossRefGoogle Scholar
  6. King, B., and D. A. Brian. 1982. Bovine coronavirus structural protein. J. Virol. 42: 700–707.PubMedGoogle Scholar
  7. Klenk, H. D. and R. Rott. 1981. Cotranslational and posttranslational processing of viral glycoproteins. Curr. Top. Microbiol. Immunol. 90: 19–48.CrossRefGoogle Scholar
  8. Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680–685.PubMedCrossRefGoogle Scholar
  9. Lapps, W., and D. A. Brian. 1985. Oligonucleotide fingerprints of antigenically related bovine coronavirus and human coronavirus OC43. Arch. Virol. 816: 101–108.CrossRefGoogle Scholar
  10. Maxam, A. M., and W. Gilbert. 1980. Sequencing end-labeled DNA with base-specific chemical cleavages. Meth. Enzymol. 65: 499–560.PubMedCrossRefGoogle Scholar
  11. Niemann, H., B. Boschek, D. Evans, M. Rosing, T. Taraura, and H.-D. Klenk. 1982. Post-translational glycosylation of coronavirus glycoprotein El: Inhibition by monensin. The EMBO Journal 1: 1499–1504.PubMedGoogle Scholar
  12. Niemann, H., G. Heisterberg-Moutsis, R. Geyer, H.-D. Klenk, and M. Wirth. 1984. Glycoprotein E1 of MHV-A59: Structure of the O-linked carbohydrates and construction of full length recombinant cDNA clones. Adv. Exp. Biol. Med. 173: 201–213.Google Scholar
  13. Niemann, H., and H.-D. Klenk. 1981. Coronavirus glycoprotein El, a new type of viral glycoprotein. J. Mol. Biol. 153: 993–1010.PubMedCrossRefGoogle Scholar
  14. Queen, C. and L. J. Korn. 1984. A comprehensive sequence analysis program for the IBM personal computer. Nucl. Acids Res. 12: 581–599.PubMedCrossRefGoogle Scholar
  15. Rottier, P., D. Brandenburg, J. Armstrong, B. Van Der Zeijst, and G. Warren. 1984. Assembly in vitro of a spanning membrane protein of the endoplasmic reticulum: The E1 glycoprotein of coronavirus mouse hepatitis virus A59. Proc. Natl. Acad. Sci. USA 81: 1421–1425.PubMedCrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1987

Authors and Affiliations

  • William Lapps
    • 1
  • Brenda G. Hogue
    • 1
  • David A. Brian
    • 1
  1. 1.Department of MicrobiologyThe University of TennesseeKnoxvilleUSA

Personalised recommendations