Structural analysis of tobacco etch potyvirus HC-pro oligomers involved in aphid transmission.

ABSTRACT: Oligomeric forms of the HC-Pro protein of the tobacco etch potyvirus (TEV) have been analyzed by analytical ultracentrifugation and single-particle electron microscopy combined with three-dimensional (3D) reconstruction. Highly purified HC-Pro protein was obtained from plants infected with TEV by using a modified version of the virus that incorporates a histidine tag at the HC-Pro N terminus (hisHC-Pro). The purified protein retained a high biological activity in solution when tested for aphid transmission. Sedimentation equilibrium showed that the hisHC-Pro preparations were heterogeneous in size. Sedimentation velocity confirmed the previous observation and revealed that the active protein solution contained several sedimenting species compatible with dimers, tetramers, hexamers, and oct

SUBMITTER: Ruiz-Ferrer V 

PROVIDER: S-EPMC1075709 | biostudies-literature | 2005 Mar

REPOSITORIES: biostudies-literature