VP7-containing empty capsids, but not purified VP7 or synthetic peptides, can induce neutralizing antibodies in cows, suggesting their potential as a subunit vaccine.
May inform minimal subunit vaccine design in cattle; leaves open translation beyond this animal model.
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.
No takes yet. Share an insight, caveat, or question.
Brüssow et al. (1990) studied this question.
Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:
More from Journal of Virology