Abstract
Granule matrix proteins secreted from human neutrophils after ionomycin stimulation were separated by SDS-PAGE, blotted onto a polyvinylidene diflouride (PVDF) membrane and overlaid with the mannose-binding lectin concanavalin A (Con A) orEscherichia coli bacteria exposing type-1-fimbriae. Four proteins of approximately 30, 40, 70 and 80 kD, respectively, derived from both the azurophil and the specific granules were shown to expose mannose-containing stuctures by binding of Con A. Such reactivity was also shown for a 90-kD protein from the light membrane fraction enriched in plasma membrane and secretory vesicles. When blots of granule matrix proteins were exposed to type-1-fimbriated bacteria, a total of seven proteins was recognized; four of the five Con A-binding proteins (40. 70, 80 and 90 kD) was detected also by the bacteria in addition to three proteins not detected by Con A (50, 60 and 100 kD). The role of the secreted type-1-fimbriae binding proteins as anti-adhesin candidates is discussed.
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Karlsson, A., Dahlgren, C. Secretion of type-1-fimbriae binding proteins from human neutrophil granulocytes. Inflammation 20, 389–400 (1996). https://doi.org/10.1007/BF01486741
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DOI: https://doi.org/10.1007/BF01486741