Pseudomonas aeruginosa cytotoxin-binding protein in rabbit erythrocyte membranes. An oligomer of 28 kDa with similarity to transmembrane channel proteins.
Rabbit erythrocyte membrane glycosylated 28-kDa protein was investigated in the membrane-bound as well as in the soluble state on an example of a Pseudomonas aeruginosa cytotoxin-binding component. When membranes were treated with trypsin/N-glycosidase F, a 13.5-kDa-binding active peptide residue is obtained as revealed by a ligand-blot technique after separation by SDS/PAGE under reducing conditions and electrophoretic transfer to nitrocellulose. Target-size analysis of intact membranes by radiation inactivation using 2-450 kGy gave a value of 29, 40 and 60 kDa for the binding-protein structure. This suggests that the native form of the binding peptide is associated as an oligomer. As seen in ligand-blot technique, 125I-cytotoxin binds with high affinity to water-channel integral protein CHIP28 from human erythrocyte membranes. The 20 N-terminal amino acids of the deglycosylated rabbit cytotoxin-binding protein show high similarity to transmembrane channel-like proteins.
Lutz
F
F
Institut für Pharmakologie und Toxikologie, Justus-Liebig-Universität Giessen, Germany.
Mohr
M
M
Grimmig
M
M
Leidolf
R
R
Linder
D
D
D000595:Amino Acid Sequence; D000818:Animals; D051398:Aquaporin 1; D020346:Aquaporins; D001789:Blood Group Antigens; D004910:Erythrocyte Membrane / Q000378:metabolism*; D006801:Humans; D007473:Ion Channels / Q000378:metabolism; D007956:Leukocidins / Q000378:metabolism*; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism*; D008969:Molecular Sequence Data; D011550:Pseudomonas aeruginosa / Q000378:metabolism; D011817:Rabbits; D017386:Sequence Homology, Amino Acid
C496020:AQP1 protein, human; D020346:Aquaporins; D001789:Blood Group Antigens; D007473:Ion Channels; D007956:Leukocidins; D008565:Membrane Proteins; D051398:Aquaporin 1