Welcome to the new version of CaltechAUTHORS. Login is currently restricted to library staff. If you notice any issues, please email coda@library.caltech.edu
Published July 15, 1985 | public
Journal Article

Primary structure of the cleavage site associated with trypsin enhancement of rotavirus SA11 infectivity

Abstract

The primary structure of the trypsin cleavage site in the outer layer protein VP3 of rotavirus SAU was determined. This cleavage enhances the infectivity of rotavirus SAU. Both VP8, one of the polypeptides generated by the cleavage, and VP3 had their a-NH2 blocked. Only VP5, the other polypeptide produced by the cleavage, was susceptible to sequential Edman degradation, indicating that it contained the new α-NH2 terminus generated by trypsin hydrolysis. The results indicated that purified VP5 is composed of two polypeptides with the following amino acid sequence at their N terminus: (a) ??VYTRAQPNQDA VVSKTS ... ; (b) AQPNQDAVVSKTS .... Sequencing of the DNA complementary to ds RNA segment 4 revealed a nucleotide sequence encoding the amino acid sequences indicated above, with only one different amino acid. From these results, the amino acid sequence of the site cleaved by trypsin was extended to cover the C termini (present in VP8). The following sequence, which contains two sites (indicated with asterisks) and can be cleaved by trypsin was deduced: ...VPVSIVSR*NIVYTR*AQPNQDIVVSKTS....

Additional Information

© 1985 Academic Press, Inc. Received October 17, 1984; accepted February 13, 1985. It is a pleasure to acknowledge the excellent technical assistance of T. Ballado, and the assistance of E. Merino with the computer. We also thank A. Navarro for help in some experiments, and F. Puerto and M. A. Loroño for performing the comparison of the different strains of SAU. This work was partially suppcrted by grants from the Consejo Nacional de Ciencia y Tecnología, and the World Health Organization.

Additional details

Created:
August 19, 2023
Modified:
October 18, 2023