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
really
suitable for your purpose! As for the IgG question - have enough crystal
structures been done to challenge your assertion?
Regards,
Iain
iwilson at molbiol.ox.ac.uk
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