Glycosylation of recombinant chimeric and human serum IgA1

Merry, Anthony H.; Morton, C.J.; Bruce, Jim; Kerr, M. A.; Woof, Jenny M.

doi:10.1042/bst020092s

Cited by 2 publications

(2 citation statements)

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“…Although it is not known currently what alterations in the structure or conformation of the IgA molecule are responsible for these effects, partial deglycosylation by enzymes derived from S. miii.s [20] suggests a role for oligosaccharide chains which constitute approximately 12% of the serum IgA molecule. Comparison between normal serum IgAI and IgAI myeloma proteins reveal different carbohydrate contents of these molecules of normal and pathological origin [32], and a recent report shows that glycosylation of chimeric human-rat antibodies produced in transfectoma cell lines may be abnormal [33]. Studies of many glycoproteins have illustrated the frequent importance of carbohydrate groups for proper folding [34].…”

Section: Discussionmentioning

confidence: 99%

All Forms of Human IgA Antibodies Bound to Antigen Interfere with Complement (C3) Fixation Induced by IgG or by Antigen Alone

1994

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Polyclonal human secretory IgA1 and IgA2 antibodies to a bacterial protein antigen Streptococcus mutans AgI/II, and polyclonal human serum IgA1 and IgA2 antibodies to staphylococcal alpha-toxin, were found to interfere with antigen-mediated C3b fixation. In fluid phase, immune complexes of antigen and IgA failed to fix C3b, whereas antigen-IgG complexes did fix C3b. Partial removal of glycan chains with Streptococcus mitis SK96 glycosidases diminished the capacity of IgA antibodies to interfere with antigen-mediated C3b fixation by the alternative complement pathway. The authors conclude that native serum or secretory IgA antibodies suppress C3b fixation, and that the glycan chains play a significant role in maintaining this property.

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Section: Discussionmentioning

confidence: 99%

All Forms of Human IgA Antibodies Bound to Antigen Interfere with Complement (C3) Fixation Induced by IgG or by Antigen Alone

1994

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“…IgA is a glycoprotein with two to five N-linked glycans present on the heavy chain; O-Linked glycans are present in the hinge region of IgA1. The N-linked glycans present on the α-heavy-chain are exposed on the surface of the molecule (Mattu et al, 1998;Merry et al, 1992). The J-chain and SC are also glycoproteins.…”

Section: Introductionmentioning

confidence: 99%