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The topology of the S protein in the yeast-derived hepatitis B surface antigen particles.

par Sonveaux, Nathalie ;Conrath, Katja;Capiau, Carine ;Brasseur, Robert ;Goormaghtigh, Erik ;Ruysschaert, Jean Marie
Référence The Journal of biological chemistry, 269, 41, page (25637-25645)
Publication Publié, 1994-10

Article révisé par les pairs

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Résumé :

Hepatitis B surface antigen particles are highly immunogenic and have been shown to provide a suitable support for the presentation of foreign epitopes. More information about the topology of their constitutive protein, the S (small envelope) protein, is a prerequisite to any rational attempt to replace region of this protein with foreign epitopes without modifying the assembly of the particle. The topology of the S protein within the lipid membrane was investigated here by combining extensive proteolysis of the external protein domains with proteinase K and (FTIR-ATR). The proteolytic hydrolysis of the S protein and the identification of the digestion products allowed characterization of the membrane-protected regions of the protein. FTIR spectra of the digested hepatitis B particles revealed that the peptides associated with the particles are rich in alpha-helix structure. The kinetic of 2H/H exchange provided evidence that a large fraction of the native S protein is poorly accessible to the aqueous medium.