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Membrane topology of VacA cytotoxin from H. pylori
Author(s) -
Wang Xiao-Ming,
Wattiez Ruddy,
Paggliacia Cristina,
Telford John L.,
Ruysschaert Jean-Marie,
Cabiaux Véronique
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01978-5
Subject(s) - chemistry , membrane , peptide , proteolysis , monomer , biophysics , membrane protein , topology (electrical circuits) , membrane topology , biochemistry , enzyme , biology , polymer , organic chemistry , mathematics , combinatorics
The interaction of VacA with membranes involves: (i) a low pH activation that induces VacA monomerization in solution, (ii) binding of the monomers to the membrane, (iii) oligomerization and (iv) channel formation. To better understand the structure–activity relationship of VacA, we determined its topology in a lipid membrane by a combination of proteolytic, structural and fluorescence techniques. Residues 40–66, 111–169, 205–266, 548–574 and 723–767 were protected from proteolysis because of their interaction with the membrane. This last peptide was shown to most probably adopt a surface orientation. Both α‐helices and β‐sheets were found in the structure of the protected peptides.