Author
CHENG, SHU-LING - UNIV OF ILLINOIS | |
CHEN, YA - UNIV OF WISCONSIN | |
YEAGER, MARK - SCRIPPS RES. INST. | |
CRANG, RICHARD - UNIV OF ILLINOIS | |
Domier, Leslie | |
D'ARCY, CLEORA - UNIV OF ILLINOIS |
Submitted to: Phytopathology
Publication Type: Abstract Only Publication Acceptance Date: 8/7/1995 Publication Date: N/A Citation: N/A Interpretive Summary: Technical Abstract: The 50kDa protein of BYDV is a structural protein, which has been proposed to be on the external surface of virus particles. To observe fine surface structure, BYDV-PAV-IL particles were examined by cryo-transmission electron microscopy (cryo-TEM) and high resolution cryo-scanning electron microscopy (cryo-SEM). Both cryo-TEM and cryo-SEM confirmed an average particle diameter of 28 nm. Cryo-SEM revealed hexagonal particles with knob-shaped structures on the surface. In cryo-TEM preparations, spike- like protrusions with an average length of 7 nm were observed on the surface of the hexagonal virus particles. Many virus particles had one or more of these structures, but some particles had none. After treatment with 400 ng trypsin/ug virus for 1.5 hr, the number of particles with knob-shaped structures in cryo-SEM was reduced from 46% to 5%. We propose that these structures are the 50kDa protein. |