NDLI: Recombinant human IgA expressed in insect cells.

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Recombinant human IgA expressed in insect cells.

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Recombinant human IgA expressed in insect cells.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Max, E. E. Capra, J. D. Carayannopoulos, L.
Description	Author Affiliation: Carayannopoulos L ( Program in Molecular Biophysics, University of Texas, Southwestern Medical Center, Dallas 75235-9048.);
Abstract	IgA serves as the first line of humoral defense at all mucosal surfaces and is present in large quantities in serum. To map the sites of interaction of immune effector molecules with the IgA constant region (C alpha), we have expressed soluble, chimeric human IgA in insect cells using recombinant baculoviruses. This antibody is correctly assembled into heavy chain/light chain heterodimers, N-glycosylated, and secreted by the insect cells; further, when coexpressed with a human J chain, the antibodies can assemble into dimers. The recombinant protein is authentic by a number of criteria, including antigen-binding, recognition by monoclonal antibodies, complement fixation via the alternative pathway, and specific binding to the monocyte IgA Fc receptor. We have also constructed viruses which encode structurally altered IgA heavy chains. Using one of these variant viruses, we have shown that glycosylation of the second domain of C alpha is required for interaction with the monocyte IgA Fc receptor. This system should prove useful in further characterization of the structure-function relationships in human C alpha.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	18
Volume Number	91
Language	English
Publisher	National Academy of Sciences
Publisher Date	1994-10-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Immunoglobulin A Genetics Animals Baculoviridae Complement C3 Metabolism Genes, Immunoglobulin Genetic Vectors Glycosylation Immunoglobulin J-Chains Immunoglobulin Alpha-Chains Immunoglobulin Kappa-Chains Mice Moths Protein Processing, Post-Translational Receptors, Fc Recombinant Fusion Proteins Immunology Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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