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. 1993 Mar;67(3):1185–1194. doi: 10.1128/jvi.67.3.1185-1194.1993

Identification of an immunodominant linear neutralization domain on the S2 portion of the murine coronavirus spike glycoprotein and evidence that it forms part of complex tridimensional structure.

C Daniel 1, R Anderson 1, M J Buchmeier 1, J O Fleming 1, W J Spaan 1, H Wege 1, P J Talbot 1
PMCID: PMC237483  PMID: 7679743

Abstract

Numerous studies have demonstrated that the spike glycoprotein of coronaviruses bears major determinants of pathogenesis. To elucidate the antigenic structure of the protein, a panel of monoclonal antibodies was studied by competitive ELISA, and their reactivities were assayed against fragments of the murine coronavirus murine hepatitis virus strain A59 S gene expressed in prokaryotic vectors. An immunodominant linear domain was localized within the predicted stalk, S2, of the peplomer. It is recognized by several neutralizing antibodies. Other domains were also identified near the proteolytic cleavage site, in the predicted globular head, S1, and in another part of the stalk. Furthermore, competition results suggest that the immunodominant functional domain forms part of a complex three-dimensional structure. Surprisingly, some antibodies which have no antiviral biological activities were shown to bind the immunodominant neutralization domain.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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