scholarly journals Structural Factors Contributing to DM Susceptibility of MHC Class II/Peptide Complexes

2002 ◽  
Vol 169 (9) ◽  
pp. 5109-5117 ◽  
Author(s):  
Michael P. Belmares ◽  
Robert Busch ◽  
Kai W. Wucherpfennig ◽  
Harden M. McConnell ◽  
Elizabeth D. Mellins
Keyword(s):  
Mhc Class Ii ◽  
Class Ii ◽  
Structural Factors ◽  
Peptide Complexes

scholarly journals The impact of DM on MHC class II–restricted antigen presentation can be altered by manipulation of MHC–peptide kinetic stability

2006 ◽  
Vol 203 (5) ◽  
pp. 1319-1328 ◽  
Author(s):  
Christopher A. Lazarski ◽  
Francisco A. Chaves ◽  
Andrea J. Sant
Keyword(s):  
Immune Response ◽  
Mhc Class Ii ◽  
Class Ii ◽  
Kinetic Stability ◽  
Histocompatibility Complex ◽  
Peptide Interactions ◽  
Peptide Complexes ◽  
Antigen Presenting ◽  
Intrinsic Kinetic ◽  
The Impact

DM edits the peptide repertoire presented by major histocompatibility complex class II molecules by professional antigen-presenting cells (APCs), favoring presentation of some peptides over others. Despite considerable research by many laboratories, there is still significant uncertainty regarding the biochemical attributes of class II–peptide complexes that govern their susceptibility to DM editing. Here, using APCs that either do or do not express DM and a set of unrelated antigens, we found that the intrinsic kinetic stability of class II–peptide complexes is tightly correlated with the effects of DM editing within APCs. Furthermore, through the use of kinetic stability variants of three independent peptides, we demonstrate that increasing or decreasing the kinetic stability of class II–peptide complexes causes a corresponding alteration in DM editing. Finally, we show that the spontaneous kinetic stability of class II complexes correlates directly with the efficiency of presentation by DM+ APCs and the immunodominance of that class II–peptide complex during an immune response. Collectively, these results suggest that the pattern of DM editing in APCs can be intentionally changed by modifying class II–peptide interactions, leading to the desired hierarchy of presentation on APCs, thereby promoting recruitment of CD4 T cells specific for the preferred peptides during an immune response.

scholarly journals Lung dendritic cells are primed by inhaled particulate antigens, and retain MHC class II/antigenic peptide complexes in hilar lymph nodes for a prolonged period of time

Immunology ◽  
2002 ◽  
Vol 105 (4) ◽  
pp. 488-498 ◽  
Author(s):  
Quynh Vu ◽  
Karin M. McCarthy ◽  
Joanne M. McCormack ◽  
Eveline E. Schneeberger
Keyword(s):  
Dendritic Cells ◽  
Lymph Nodes ◽  
Mhc Class Ii ◽  
Class Ii ◽  
Antigenic Peptide ◽  
Peptide Complexes

A new method for the production of MHC class II/peptide complexes associated by FOS and JUN dimerization domains

2002 ◽  
Vol 63 (10) ◽  
pp. S4
Author(s):  
Junbao Yang ◽  
Ruili Shi ◽  
Jeremy Goodman ◽  
T Mohanakumar
Keyword(s):  
Mhc Class Ii ◽  
Class Ii ◽  
New Method ◽  
Peptide Complexes

scholarly journals MHC Class II-Peptide Complexes and APC Lipid Rafts Accumulate at the Immunological Synapse

2003 ◽  
Vol 170 (3) ◽  
pp. 1329-1338 ◽  
Author(s):  
Elizabeth M. Hiltbold ◽  
Neil J. Poloso ◽  
Paul A. Roche
Keyword(s):  
Lipid Rafts ◽  
Mhc Class Ii ◽  
Immunological Synapse ◽  
Class Ii ◽  
Peptide Complexes

scholarly journals Major Histocompatibility Complex Class II Compartments in Human and Mouse B Lymphoblasts Represent Conventional Endocytic Compartments

1997 ◽  
Vol 139 (3) ◽  
pp. 639-649 ◽  
Author(s):  
Monique J. Kleijmeer ◽  
Stanislaw Morkowski ◽  
Janice M. Griffith ◽  
Alexander Y. Rudensky ◽  
Hans J. Geuze
Keyword(s):  
Major Histocompatibility Complex ◽  
B Cells ◽  
Mhc Class Ii ◽  
Class Ii ◽  
Invariant Chain ◽  
Histocompatibility Complex ◽  
Peptide Complexes ◽  
Endocytic Compartments ◽  
Human And Mouse ◽  
Mhc Class Ii Molecules

In most human and mouse antigen-presenting cells, the majority of intracellular major histocompatibility complex (MHC) class II molecules resides in late endocytic MHC class II compartments (MIICs), thought to function in antigen processing and peptide loading. However, in mouse A20 B cells, early endocytic class II-containing vesicles (CIIVs) have been reported to contain most of the intracellular MHC class II molecules and have also been implicated in formation of MHC class II–peptide complexes. To address this discrepancy, we have studied in great detail the endocytic pathways of both a human (6H5.DM) and a mouse (A20.Ab) B cell line. Using quantitative immunoelectron microscopy on cryosections of cells that had been pulse–chased with transferrin-HRP or BSA-gold as endocytic tracers, we have identified up to six endocytic subcompartments including an early MIIC type enriched in invariant chain, suggesting that it serves as an important entrance to the endocytic pathway for newly synthesized MHC class II/invariant chain complexes. In addition, early MIICs represented the earliest endocytic compartment containing MHC class II– peptide complexes, as shown by using an antibody against an abundant endogenous class II–peptide complex. The early MIIC exhibited several though not all of the characteristics reported for the CIIV and was situated just downstream of early endosomes. We have not encountered any special class II-containing endocytic structures besides those normally present in nonantigen-presenting cells. Our results therefore suggest that B cells use conventional endocytic compartments rather than having developed a unique compartment to accomplish MHC class II presentation.

Sign in / Sign up

Export Citation Format

Share Document