Important note: Information in this article was accurate in 2000. The state of the art may have changed since the publication date.
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J Chromatogr B Biomed Sci Appl. 2000 Jan 14;737(1-2):85-95. Unique Identifier : AIDSLINE MED/20143280
Tallet B; Astier-Gin T; Londos-Gagliardi D; Guillemain B; EP630 CNRS-Universite Victor Segalen Bordeaux 2, France.
Abstract: 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.
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