Immunoglobulin Structure Immunoglobulin Classes Biological Effector Functions of Immunoglobulins Receptors for Immunoglobulin Structural Biology of Immunoglobulins and Immunoglobulin Receptors Cellular Basis of Antibody Production Immunoglobulin Genes and Antibody Diversity Immunotechnology: Generation and Uses of Monoclonal Antibodies

Immunoglobulin superfamily

Surface Immunoglobulin

10.1002/9780470688618.taw0097

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Studies on the Site and Mechanism of Attachment of Phosphorylcholine to a Filarial Nematode Secreted Glycoprotein

Journal of Biological Chemistry (1997)

Katrina M. Houston William Cushley William Harnett

We have recently shown that the immunomodulatory substance phosphorylcholine (PC) is covalently attached to ES-62, a major secreted protein of the filarial nematode parasite Acanthocheilonema viteae, via an N-linked glycan. Linkage of PC to N-glycans is previously unreported, and hence we have investigated the biochemical events underlying it. PC addition was found by pulse-chase experiments to be a fairly early event during intracellular transport, occurring within 40-60 min of protein synthesis. Biosynthetic labeling/immunoprecipitation experiments revealed that addition of PC to ES-62 was blocked by (i) brefeldin A, an inhibitor of trafficking of newly synthesized proteins from the endoplasmic reticulum (ER) to the Golgi, (ii) 1-deoxynorijirimycin, an inhibitor of glucosidase activity in the ER, and (iii) 1-deoxymannojirimycin, an inhibitor of mannosidase I in the cis Golgi. Swainsonine, an inhibitor of mannosidase II in the medial Golgi, did not affect PC addition. Taken together these data indicate that PC attachment is a post-ER event which is dependent on generation of an appropriate substrate during oligosaccharide processing. Furthermore, they strongly suggest that PC addition takes place in the medial Golgi and that the substrate for addition is the 3-linked branch of Man₅GlcNAc₃ or Man₃GLcNAc₃.

Brefeldin A

Phosphorylcholine

Immunoprecipitation

Mannosidase

10.1074/jbc.272.3.1527

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Acetylated galactosamine is a receptor for the influenza C virus glycoprotein

Archives of Virology (1988)

Peter Luther William Cushley C. H�lzer Ulrich Desselberger John Oxford

Neuraminic acid

Galactosamine