The MHC class II cofactor, HLA-DM, interacts with immunoglobulin in B cells

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Abstract/Contents

Abstract
B cells internalize antigen bound to membrane immunoglobulin and load antigen-derived peptides onto MHC class II proteins. How these pathways intersect is not well understood. We found that HLA-DM, a catalyst for peptide loading onto MHC class II, regulates immunoglobulin levels in human B cells and co-precipitates with immunoglobulin. In intact cells, HLA-DM and immunoglobulin are found in close proximity, and these complexes are in post-Golgi compartments. In vitro, in the endosomal pH range, the luminal domain of soluble HLA-DM (sDM) directly and specifically interacts with the immunoglobulin Fab domain, and sDM increases the amount of antigen released from immune complexes. These observations support a model in which HLA-DM facilitates the hand-off of antigen from immunoglobulin to MHC class II.

Description

Type of resource text
Form electronic; electronic resource; remote
Extent 1 online resource.
Publication date 2013
Issuance monographic
Language English

Creators/Contributors

Associated with Strohman, Michael John
Associated with Stanford University, Program in Immunology.
Primary advisor Mellins, Elizabeth
Thesis advisor Mellins, Elizabeth
Thesis advisor Davis, Mark M
Thesis advisor Jardetzky, Theodore
Thesis advisor Jones, Patricia P
Thesis advisor Miklos, David (David B.)
Advisor Davis, Mark M
Advisor Jardetzky, Theodore
Advisor Jones, Patricia P
Advisor Miklos, David (David B.)

Subjects

Genre Theses

Bibliographic information

Statement of responsibility Michael John Strohman.
Note Submitted to the Program in Immunology.
Thesis Thesis (Ph.D.)--Stanford University, 2013.
Location electronic resource

Access conditions

Copyright
© 2013 by Michael John Strohman

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