glycosylated receptors

Iain B. H. Wilson iwilson at molbiol.ox.ac.uk
Wed Dec 7 04:57:28 EST 1994

Roy Jefferis (r.jefferis at bham.ac.uk) wrote:

>My interest is glycosylation of secreted antibody molecules and its
>influence on effector functions.However,I want to be able to quote studies
>in which it has been shown that glycosylation is essential to the function
 >of receptor molecules; any receptor not just antibodies.
>Also, I frequently assert that IgG antibodies are unique (so far !) inhaving 
>an oligosaccaride moiety which is essentially "sequestered" within the 
>quaternary structure of the molecule,the CH2 domains of the Fc region.
>Would anyone like to contest this assertion ? Please give details with 
>publications, if possible.
>Kind regards, ROY.

Dear Roy,
	I'm not too sure whether any glycosylation (of receptor or ligand) is 
really absolutely essential for receptor function. Ajit Varki's review 
(Glycobiology [1993] 3:97-130) has a large number of references on the subject
of oligosaccharide function. I just scanned Table I (effect of lack or 
alteration of
oligosaccharides) and see:

Decreased biological activity of erythropoietin;
Removal of IgD glycosylation causes loss of binding to receptors;
Loss of ability of haptoglobulin to form a complex with haemoglobin;
Decreased transferrin receptor binding affinity in intact cells.

I've not looked at any of the references so I can't tell whether these are 
suitable for your purpose! As for the IgG question - have enough crystal 
structures been done to challenge your assertion?


iwilson at molbiol.ox.ac.uk
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Iain Wilson                                  Dyson Perrins Laboratory
Tel: +44-1865-275696                         University of Oxford
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E-mail: iwilson at molbiol.ox.ac.uk             Oxford, OX1 3QY, UK

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