Comparison of pore-forming ability in membranes of a native and a recombinant variant of Sticholysin II from Stichodactyla helianthus.
Sticholysin II (St II) a potent cytolysin from the sea anemone Stichodactyla helianthus was obtained by recombinant procedures exhibiting six histidine residues in its N-terminus (St IIn6H). The functional comparison between St II and St IIn6H showed a lesser pore-forming ability for the recombinant than for the native in human or rat red blood cells (RBC) and in large unilamellar vesicles (LUV) of different phospholipid composition. However, binding of St IIn6H to small unilamellar vesicles (SUV) was higher with regard to St II. The explanation to the different permeabilizing capacity of both protein variants is not clear, but a different anchoring of St IIn6H to the lipid bilayer could delay the organization of the competent pore into membrane.
Departamento de Bioquímica y Centro de Estudio de Proteínas, Facultad de Biología, Universidad de La Habana, Cuba.
I F
IF
Pazos
D
D
Martínez
M
M
Tejuca
A
A
Valle
A
A
del Pozo
C
C
Alvarez
M E
ME
Lanio
E A
EA
Lissi
D019943:Amino Acid Substitution; D000818:Animals; D002462:Cell Membrane / Q000378:metabolism*; D002463:Cell Membrane Permeability / Q000502:physiology; D003064:Cnidarian Venoms / Q000737:chemistry*; D004912:Erythrocytes / Q000378:metabolism / Q000648:ultrastructure; D006460:Hemolysin Proteins / Q000737:chemistry* / Q000378:metabolism / Q000502:physiology*; D006461:Hemolysis / Q000502:physiology*; D006801:Humans; D008051:Lipid Bilayers / Q000737:chemistry / Q000378:metabolism; D008081:Liposomes / Q000378:metabolism; D009994:Osmolar Concentration; D011487:Protein Conformation; D051381:Rats; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D012615:Sea Anemones
D003064:Cnidarian Venoms; D006460:Hemolysin Proteins; D008051:Lipid Bilayers; D008081:Liposomes; D011994:Recombinant Proteins; C404794:sticholysin II