Sequence and structure of the coronavirus peplomer protein.

R. J. de Groot*, J. A. Lenstra, W. Luytjes, H. G. Niesters, M. C. Horzinek, B. A. van der Zeijst, W. J. Spaan

*Corresponding author for this work

    Research output: Chapter in Book/Report/Conference proceedingChapterAcademicpeer-review

    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)
    Original languageEnglish
    Title of host publicationCoronaviruses
    PublisherSpringer
    Pages31-38
    Number of pages8
    DOIs
    Publication statusPublished - 1 Dec 1987

    Publication series

    NameAdvances in Experimental Medicine and Biology
    PublisherSpringer
    Volume218
    ISSN (Print)0065-2598

    Keywords

    • Infectious Bronchitis Virus
    • Coiled Coil
    • Heptad Repeat
    • Mouse Hepatitis Virus
    • Infectious Bronchitis Virus Strain

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