Linear neutralizing epitopes on the peplomer protein of coronaviruses

W. P A Posthumus, R. H. Meloen, L. Enjuanes, I. Correa, A. P. van Nieuwstadt, G. Koch, R. J. de Groot, J. G. Kusters, W. Luytjes, W. J. Spaan, B. A M van der Zeijst, J. A. Lenstra

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

    Abstract

    Three years ago, we reported a comparison of the primary structures of the S peplomer proteins of three coronaviruses - mouse hepatitis virus (MHV, strain A59), infectious bronchitis virus (IBV, strain M41), and feline infectious peritonitis virus (FIPV, strain 79-1146) - which represent the three antigenic clusters in the Coronavirus family (De Groot et al., 1987a, b). A periodicity in the C-terminal part of the S sequence indicated the presence of a coiled-coil structure, which forms the stalk of the peplomer. The nonconserved N-terminal sequence probably forms the bulbous part of the peplomer.
    Original languageEnglish
    Title of host publicationCoronaviruses and their Diseases
    PublisherSpringer
    Pages181-188
    Number of pages8
    DOIs
    Publication statusPublished - 1 Dec 1990

    Publication series

    NameAdvances in Experimental Medicine and Biology
    PublisherSpringer New York
    Volume276
    ISSN (Print)0065-275X

    Keywords

    • Infectious Bronchitis Virus
    • Antigenic Site
    • Hybrid Protein
    • Linear Epitope
    • Mouse Hepatitis Virus

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