Sequence and Structure of the Coronavirus Peplomer Protein
- 357 Downloads
Coronaviruses display a characteristic fringe of large (17–20 nm), clubshaped peplomers, each consisting of a di- or trimer of the peplomer protein (Cavanagh et al. 1983). The peplomer protein, E2, plays an important role during the infection proces. It mediates the binding of virions to the host-cell receptors and is involved in membrane fusion. In addition, the E2 protein appears to be a major inducer of protective immunity to coronaviral infection (reviewed by Sturman and Holmes, 1983).
KeywordsInfectious Bronchitis Virus Coiled Coil Heptad Repeat Mouse Hepatitis Virus Infectious Bronchitis Virus Strain
- Cavanagh, D., Davis, P.J., Pappin, D.J., Binns, M.M., Boursnell, M.E.G. and Brown, T.D.K., 1986, Coronavirus IBV: partial amino terminal sequencing of spike polypeptide S2 identifies the sequence Arg-Arg-Phe-Arg-Arg at the cleavage site of the spike precursor propolypeptide of IBV strains Beaudette and M41, Virus Res., 4: 133–143.PubMedCrossRefGoogle Scholar
- Niesters, H.G.M., Lenstra, J.A., Spaan, W.J.M., Zijderveld, A.J., Bleumink-Pluym, N.M.C., Hong, F., van Scharrenburg, G.J.M., Horzinek, M.C. and van der Zeijst, B.A.M., 1986, The peplomer protein sequence of the M41 strain of coronavirus IBV and its comparison with other Beaudette strains, Virus Res., 5: 253–263.PubMedCrossRefGoogle Scholar
- Siddell, St., Wege, W., and Ter Meulen, V., 1983, The biology of coronaviruses, J. gen.Virol., 64: 761: 776.Google Scholar