Abstract:
:Immunoglobulins (Ig) require correct folding and assembly of both heavy (H) and light (L) chains to form a functional H2L2 dimer that is secreted from plasma cells. This process is dependent upon the endoplasmic reticulum (ER) chaperone BiP, which targets improperly, folded or assembled Ig molecules for degradation. While investigating the mechanism of low IgG3 secretion, we identified a missense mutation L368P in the Ch3 region of the human gamma3 H-chain that was associated with impaired secretion of intact and functional Ig. The non-secreted H-chains displayed slower electrophoretic migration than secreted H-chains, consistent with them being glycosylated in the ER but not fully processed in the golgi apparatus and secretory pathway. Reversion of the mutated codon to wild type restored secretion of the IgG3, which displayed the same fine specificity for antigen as non-secreted IgG3. However, the non-secreted IgG3 was not opsonic in an in vitro phagocytosis assay. The results indicate that correct IgG3 Ch3 domain folding is essential for secretion and effective function but does not affect specificity for antigen.
journal_name
Mol Immunoljournal_title
Molecular immunologyauthors
McLean GR,Torres M,Trotter B,Noseda M,Bryson S,Pai EF,Schrader JW,Casadevall Adoi
10.1016/j.molimm.2004.11.015subject
Has Abstractpub_date
2005-05-01 00:00:00pages
1111-9issue
9eissn
0161-5890issn
1872-9142pii
S0161-5890(04)00468-7journal_volume
42pub_type
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