The flavivirus envelope protein E: isolation of a soluble form from tick-borne encephalitis virus and its crystallization.
AUTOR(ES)
Heinz, F X
RESUMO
By the use of limited trypsin digestion of purified virions, we generated a membrane anchor-free and crystallizable form of the tick-borne encephalitis virus envelope glycoprotein E. It retained its reactivity with a panel of monoclonal antibodies, and only subtle structural differences from the native protein E were recognized. Treatment with the bifunctional cross-linker dimethylsuberimidate resulted in the formation of a dimer. Crystallization experiments yielded hexagonal rod-shaped crystals suitable for X-ray diffraction analysis.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=249068Documentos Relacionados
- Synthesis and secretion of recombinant tick-borne encephalitis virus protein E in soluble and particulate form.
- Antigenic structure of the flavivirus envelope protein E at the molecular level, using tick-borne encephalitis virus as a model.
- Isolation of Capsid Protein Dimers from the Tick-Borne Encephalitis Flavivirus and In Vitro Assembly of Capsid-Like Particles
- Characterization of a Membrane-Associated Trimeric Low-pH-Induced Form of the Class II Viral Fusion Protein E from Tick-Borne Encephalitis Virus and Its Crystallization
- The shifting landscape of tick-borne zoonoses: tick-borne encephalitis and Lyme borreliosis in Europe.