IDENTIFICATION OF THE LYSOSOMAL MEMBRANE GLYCOPROTEIN LAMP-1 AS A RECEPTOR FOR TYPE-1-FIMBRIATED (MANNOSE-SPECIFIC) ESCHERICHIA-COLI

The presence of several glycosylated sites with high-mannose oligosacc harides on the lysosome-associated membrane glycoproteins (Lamps) comb ined with the fact that neutrophil Lamps are present in mobilizable or ganelles inspired us to investigate their ability to bind type-1 fimbr iated (mannose-binding) Escherichia coli and subsequently define a pot ential function for the Lamps in human neutrophils. Bacterial binding to Lamps purified from chronic myeloic leukemia cells was investigated by separation of the proteins by sodium dodecyl sulfate polyacrylamid e gel electrophoresis, transfer to a blotting membrane and overlay wit h type-1-fimbriated bacteria. The overlays were developed by growth. T he bacteria bound readily to Lamp-1 while there was almost no binding to Lamp-2. Hence, we state that a possible function for neutrophil Lam p-1 is bacterial binding. (C) 1996 Academic Press, Inc.