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J. Biol. Chem., Vol. 269, Issue 41, 25637-25645, Oct, 1994
N Sonveaux, K Conrath, C Capiau, R Brasseur, E Goormaghtigh and JM Ruysschaert
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.
The topology of the S protein in the yeast-derived hepatitis B surface antigen particles
Laboratoire de Chimie-Physique des Macromolecules aux Interfaces, Universite Libre de Bruxelles, Belgium.
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