Abstract
Helper T cells are stimulated to fight infections or diseases upon recognition of peptides from antigens that are processed and presented by the proteins of Major Histocompatibility Complex (MHC) Class II molecules. Degradation of a full protein into small peptide fragments is a lengthy process consisting of many steps and chaperones. Malfunctions during any step of antigen processing could lead to the development of self-reactive T cells or defective immune response to pathogens. Although much has been accomplished regarding how antigens are processed and presented to T cells, many questions still remain unanswered, preventing the design of therapeutics for direct intervention with antigen processing. Here, we review published work on the discovery and function of a MHC class II molecular chaperone, HLA-DO, in human, and its mouse analog H2-O, herein called DO. While DO was originally discovered decades ago, elucidating its function has proven challenging. DO was discovered in association with another chaperone HLA-DM (DM) but unlike DM, its distribution is more tissue specific, and its function more subtle.
Highlights
Major Histocompatibility Complex (MHC) Class II molecules are heterodimeric glycoproteins consisting of one α-chain of approximately 34 kDa and one β-chain of approximately 28 kDa [1]
We know that DO is a highly evolutionarily conserved molecule [48,49,50], but unlike the classical MHC genes, DO is not polymorphic
It has even been reported that a point mutation in the human HLADOα gene was linked to a susceptibility to rheumatoid arthritis (RA) [51], suggesting that the effects of DO are far reaching
Summary
Major Histocompatibility Complex (MHC) Class II molecules are heterodimeric glycoproteins consisting of one α-chain of approximately 34 kDa and one β-chain of approximately 28 kDa [1]. Polymorphic classical MHC class II molecules bind and present peptide antigens.
Sign-in/Register to view highlights & summary Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
