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.
Effect of Salmonella typhimurium porins on biological activities of human polymorphonuclear leukocytes / Tufano, Ma; Ianniello, R; Galdiero, M; DE MARTINO, Luisa; Galdiero, F.. - In: MICROBIAL PATHOGENESIS. - ISSN 0882-4010. - STAMPA. - 7:5(1989), pp. 337-346.
Effect of Salmonella typhimurium porins on biological activities of human polymorphonuclear leukocytes.
DE MARTINO, LUISA;
1989
Abstract
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.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
