The flavivirus envelope protein E: isolation of a soluble form from tick-borne encephalitis virus and its crystallization.
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.
Heinz
F X
FX
Institute of Virology, University of Vienna, Austria.
Mandl
C W
CW
Holzmann
H
H
Kunz
C
C
Harris
B A
BA
Rey
F
F
Harrison
S C
SC
D000595:Amino Acid Sequence; D002852:Chromatography, Ion Exchange; D003460:Crystallization; D004591:Electrophoresis, Polyacrylamide Gel; D004669:Encephalitis Viruses, Tick-Borne / Q000737:chemistry*; D004797:Enzyme-Linked Immunosorbent Assay; D000939:Epitopes / Q000032:analysis; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000302:isolation & purification; D011487:Protein Conformation; D014357:Trypsin; D014759:Viral Envelope Proteins / Q000276:immunology / Q000302:isolation & purification*; D014771:Virion / Q000737:chemistry*
D000939:Epitopes; D010446:Peptide Fragments; D014759:Viral Envelope Proteins; C065696:glycoprotein E, Flavivirus; D014357:Trypsin