Expression, purification and biological properties of the carboxyl half part of the HTLV-I surface envelope glycoprotein.
The carboxyl half of the surface envelope protein of HTLV-I contains the major immunodominant and neutralizable domains. Using two affinity chromatography steps and a combination of high salt concentration and non-ionic detergent, we purified this part of the envelope protein from Escherichia coli. Analysis of some immmunological and biological properties of this protein indicated that it was folded in a way that preserved the correct structure of this domain of the HTLV-I envelope protein. It could be utilized in structural studies to further understand the mechanisms of HTLV-I entry and to better define the component(s) of an effective vaccine.
Tallet
B
B
EP630 CNRS-Université Victor Ségalen Bordeaux 2, France.
Astier-Gin
T
T
Londos-Gagliardi
D
D
Guillemain
B
B
D001419:Bacteria / Q000235:genetics; D002846:Chromatography, Affinity / Q000379:methods; D004591:Electrophoresis, Polyacrylamide Gel; D005822:Genetic Vectors; D015726:Giant Cells / Q000166:cytology; D015481:HTLV-I Antibodies / Q000097:blood; D015368:Human T-lymphotropic virus 1 / Q000737:chemistry*; D006801:Humans; D017510:Protein Folding; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification; D014759:Viral Envelope Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification
D015481:HTLV-I Antibodies; D011994:Recombinant Proteins; D014759:Viral Envelope Proteins