This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Brüssow, H Articles by Marc-Martin, S Search for Related Content PubMed PubMed Citation Articles by Brüssow, H Articles by Marc-Martin, S

Polypeptide composition of rotavirus empty capsids and their possible use as a subunit vaccine.

Nestlé Research Centre, NESTEC Ltd., Vers-chez-les-Blanc, Lausanne, Switzerland.

ABSTRACT

Two types of empty capsid particles that differed with respect to the presence of the two outer shell proteins were isolated from MA-104 cells infected with bovine rotavirus V1005. Three previously uncharacterized polypeptides, I, II, and III, migrating between VP2 and VP6, were detected in empty capsids but not in single- and double-shelled rotavirus particles. Peptide mapping revealed that all three proteins were related to VP2. Polypeptides I, II, and III could be generated by in vitro trypsin digestion of empty capsids not exposed to trypsin in the infection medium. Labeled polypeptides appeared in empty capsids before they were detected in intracellular single- or double-shelled rotavirus particles. Empty capsids were also observed in MA-104 cells infected with bovine rotaviruses UK and NCDV, simian rotavirus SA11, and human rotavirus KU. VP7-containing empty capsid is the minimal subunit vaccine for cows; we failed to induce a substantial neutralizing antibody increase with VP7 purified under denaturating or nondenaturating conditions or with synthetic peptides corresponding to two regions of VP7.

This article has been cited by other articles:

• Potgieter, A. C., Steele, A. D., van Dijk, A. A. (2002). Cloning of complete genome sets of six dsRNA viruses using an improved cloning method for large dsRNA genes. J. Gen. Virol. 83: 2215-2223 [Abstract] [Full Text]  
• Delorme, C., Brüssow, H., Sidoti, J., Roche, N., Karlsson, K.-A., Neeser, J.-R., Teneberg, S. (2001). Glycosphingolipid Binding Specificities of Rotavirus: Identification of a Sialic Acid-Binding Epitope. J. Virol. 75: 2276-2287 [Abstract] [Full Text]