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. 1991 Aug;65(8):4334–4340. doi: 10.1128/jvi.65.8.4334-4340.1991

Rotavirus spike structure and polypeptide composition.

I D Anthony 1, S Bullivant 1, S Dayal 1, A R Bellamy 1, J A Berriman 1
PMCID: PMC248872  PMID: 1649333

Abstract

Negatively stained preparations of rotavirus imaged with a low dose of electrons provide sufficient contrast to reveal surface projections or spikes. The number of spikes found projecting from different particles indicates that not all 60 peripentonal sites are occupied. Treatment at pH 11.2 with 250 mM ammonium hydroxide specifically removes the spikes, yielding smooth double-shelled particles of the same diameter as that of the native virus. Protein analysis confirms that the released spikes are composed of polypeptide VP4 (or its two cleavage products VP5* and VP8*) and that the smooth particle retains the other major outer shell protein VP7. Spikeless particles can be decorated by a monoclonal antibody specific for the major immunodominant neutralizing domain of VP7, implying that removal of the spikes does not denature the VP7 that is retained on the surface of the smooth particle.

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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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