Adenovirus serotype 3 fibre protein is expressed as a trimer in Escherichia coli.
The adenovirus serotype 3 (Ad3) fibre has been expressed in Escherichia coli as an insoluble protein. The protein was solubilized by extraction with urea. Slow removal of urea during the purification procedure resulted in a soluble Ad3 fibre preparation. Polyacrylamide gel analysis of the purified fibre protein, as well as cross-linking experiments performed on cellular debris of expressing cells, suggest that the recombinant Ad3 fibre self-assembles as a trimer from identical polypeptide chains. Gel filtration gave the same exclusion volume for the purified recombinant fibre and for the native fibre in the protein mixture extracted from the Ad3-infected cells. The recombinant fibre was partially resistant to proteolytic degradation, suggesting a folded structure.
Albiges-Rizo
C
C
European Molecular Biology Laboratory, Grenoble, France.
Chroboczek
J
J
D000256:Adenoviridae / Q000235:genetics*; D002213:Capsid / Q000096:biosynthesis / Q000235:genetics / Q000302:isolation & purification*; D036022:Capsid Proteins; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000235:genetics* / Q000378:metabolism; D005814:Genes, Viral; D046911:Macromolecular Substances; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000235:genetics / Q000302:isolation & purification; D012995:Solubility; D014508:Urea
D036022:Capsid Proteins; D046911:Macromolecular Substances; D011994:Recombinant Proteins; C018315:hexon capsid protein, Adenovirus; D014508:Urea