Sequence and structure of the coronavirus peplomer protein.
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Publication date
1987-12-01
Authors
de Groot, R.J.
Lenstra, Johannes A.
Luytjes, W.
Niesters, H. G.
Horzinek, M. C.
van der Zeijst, B. A.
Spaan, W. J.
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Abstract
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)
Keywords
Infectious Bronchitis Virus, Coiled Coil, Heptad Repeat, Mouse Hepatitis Virus, Infectious Bronchitis Virus Strain, General Biochemistry,Genetics and Molecular Biology, SDG 3 - Good Health and Well-being
Citation
de Groot, R J, Lenstra, J A, Luytjes, W, Niesters, H G, Horzinek, M C, van der Zeijst, B A & Spaan, W J 1987, Sequence and structure of the coronavirus peplomer protein. in Coronaviruses. Advances in Experimental Medicine and Biology, vol. 218, Springer, pp. 31-38. https://doi.org/10.1007/978-1-4684-1280-2_4