Biochemical Characterization of Rift Valley Fever Virus
Abstract
Rift Valley fever virus (RVFV) polypeptides were shown to share similar biochemical properties with members of the family Bunyaviradae. Electrophoretic analysis of RVFV revealed one nonglycosylated and two glycosylated major proteins with molecular weights of 25,000, 56,000, and 65,000 respectively. In addiction, a 100,000 MW glycoprotein was found. The 25,000 MW protein was identified as the major nucleocapsid protein. The virion density in CsCl was 1.21 g/mi, while that of the nucleocapsid was 1.29 g/ml. The number and molecular weights of major structural polypeptides of several diverse RVFV isolates were identical. The presence of three RNA segments, large, medium, and small, with molecular weights of 2.7, 1.7, and 0.6 x 10 (expn 6) was demonstrated. The close relationships of RVFV proteins and RNA with reported molecular weights of some members of the Phlebotomus fever (PHL) group viruses were compatible with the serological cross-reactivity among these viruses. These findings support the classification of RVFV with the PHL group viruses in the family Bunyaviradae.
Document Details
- Document Type
- Technical Report
- Publication Date
- Jan 01, 1980
- Accession Number
- ADA090880
Entities
People
- Barry J. Erlick
- Gerald A. Eddy
- Robert M. Rice
- Robert R. Rosato
- Sashi B. Mohanty
Organizations
- United States Army Medical Research Institute of Infectious Diseases