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Localization of major neutralizing epitopes on the S1 polypeptide of the murine coronavirus peplomer glycoprotein

A recombinant baculovirus system has been used to express the amino terminal half of the murine coronavirus (JHMV) peplomer glycoprotein in insect cells. The expressed polypeptide is glycosylated and is recognized by a set of monoclonal antibodies (mAbs) specific for JHMV S protein. Three of these m...

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Detalles Bibliográficos
Autores principales: Sayaka, Takase-Yoden, Tateki, Kikuchi, Siddell, Stuart G., Fumihiro, Taguchi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Published by Elsevier B.V. 1991
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7133859/
https://www.ncbi.nlm.nih.gov/pubmed/1645909
http://dx.doi.org/10.1016/0168-1702(91)90011-J
Descripción
Sumario:A recombinant baculovirus system has been used to express the amino terminal half of the murine coronavirus (JHMV) peplomer glycoprotein in insect cells. The expressed polypeptide is glycosylated and is recognized by a set of monoclonal antibodies (mAbs) specific for JHMV S protein. Three of these mAbs have a very high neutralizing activity for JHMV but not for other MHV strains. These results indicate that JHMV-specific, major neutralizing epitopes reside in the amino terminal S1 subunit of the peplomer glycoprotein.