Cryptic I antigen activity and Mycoplasma pneumoniae-receptor activity associated with sialoglycoprotein GP-2 of bovine erythrocyte membranes

Author:

Feizi T.1,Gooi H. C.1,Loomes L. M.1,Suzuki Y.2,Suzuki T.2,Matsumoto M.2

Affiliation:

1. Applied Immunochemistry Research Group, Clinical Research Centre, Watford Road, Harrow, Middlesex HA1 3UJ, UK

2. Department of Biochemistry, Shizuoka College of Pharmacy, 2-2-1 Oshika, 422, Shizuoka-Shi, Japan

Abstract

The 250-kDa sialoglycoprotein of bovine erythrocyte membranes, GP-2, has been found to be an exception-ally rich source of branched sialo-oligosaccharides of poly-N-acetyllactosamine (I antigen) type with receptor activity for the human pathogen Mycoplasma pneumoniae. Desialylated GP-2 is the most potent I-active substance thus far tested. Since this gtyco-protein is hydrophobic and can be readily re-incorporated into cell membranes, it should be useful in future studies of the mechanism of production of auto-antibodies to the I antigen which commonly arise following human infection with M. pneumoniae.

Publisher

Portland Press Ltd.

Subject

Cell Biology,Molecular Biology,Biochemistry,Biophysics

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