Effect of Salmonella typhimurium porins on biological activities of human polymorphonuclear leukocytes.
The effect of Salmonella typhimurium porins on human polymorphonuclear leukocytes (PMNs) was studied. Labeled porins were shown to bind to the PMNs, and could be completely displaced by unlabeled porins. The binding caused modifications of membrane integrity and of the physico-chemical characteristics of the PMN surface, e.g. decreased oxidative burst, decreased hydrophobicity and altered cell morphology. The porins acted as both chemotaxins and chemotaxinogens. When PMNs were preincubated with porins their migration in the presence of commonly used chemoattractants (serum activated by zymosan or N-formyl-L-methionyl-L-leucyl-L-phenylalanine) was inhibited.
Tufano
M A
MA
Istituto di Microbiologia, I Facoltà di Medicina e Chirurgia, Napoli, Italy.
Ianniello
R
R
Galdiero
M
M
De Martino
L
L
Galdiero
F
F
D001425:Bacterial Outer Membrane Proteins / Q000378:metabolism / Q000494:pharmacology*; D002462:Cell Membrane / Q000648:ultrastructure; D002478:Cells, Cultured; D002634:Chemotaxis, Leukocyte; D006801:Humans; D007700:Kinetics; D016177:Macrophage-1 Antigen; D009504:Neutrophils / Q000187:drug effects* / Q000378:metabolism / Q000648:ultrastructure; D018272:Porins; D011951:Receptors, Complement / Q000378:metabolism; D011961:Receptors, Fc / Q000378:metabolism; D012486:Salmonella typhimurium / Q000378:metabolism*
D001425:Bacterial Outer Membrane Proteins; D016177:Macrophage-1 Antigen; D018272:Porins; D011951:Receptors, Complement; D011961:Receptors, Fc