Expression, purification and biological properties of the carboxyl half part of the HTLV-I surface envelope...

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.