Compartmentalization of class II antigen presentation: Contribution of cytoplasmic and endosomal processing

Ping Li, Josetta L. Gregg, Nan Wang, Delu Zhou, Patrick O'Donnell, Janice Blum, Victoria L. Crotzer

Research output: Contribution to journalArticle

58 Citations (Scopus)

Abstract

During antigen processing, peptides are generated and displayed in the context of major histocompatibility complex (MHC) class II molecules on the surface of antigen-presenting cells (APCs) to modulate immune responses to foreign antigens and guide self-tolerance. Exogenous and cytoplasmic antigens are processed by distinct routes within APCs to yield class II ligands. Exogenous antigens are internalized, processed, and bound to class II molecules within endosomal and lysosomal compartments of APCs. Studies reviewed here demonstrate the importance of reduction in regulating exogenous antigen presentation. The differential expression of a γ-interferon-inducible lysosomal thiol reductase in professional APCs and melanomas is discussed in the context of tumor immune evasion. Cytoplasmic autoantigens, by contrast, are degraded by the proteasome and other enzymes in the cytosol, with the resulting peptides translocating to endosomal and lysosomal compartments for intersection with class II molecules. Processing and editing of these antigenic peptides within endosomes and lysosomes may be critical in regulating their display via class II proteins. Multiple pathways may regulate the transit of cytosolic peptides to class II molecules. The role of lysosome-associated membrane protein-2a and heat-shock cognate protein 70 in promoting cytoplasmic peptide presentation by MHC class II molecules is discussed.

Original languageEnglish
Pages (from-to)206-217
Number of pages12
JournalImmunological Reviews
Volume207
DOIs
StatePublished - Oct 2005

Fingerprint

Histocompatibility Antigens Class II
Antigen Presentation
Antigen-Presenting Cells
Peptides
Major Histocompatibility Complex
Antigens
HSC70 Heat-Shock Proteins
Lysosome-Associated Membrane Glycoproteins
Tumor Escape
Self Tolerance
Endosomes
Autoantigens
Proteasome Endopeptidase Complex
Surface Antigens
Lysosomes
Sulfhydryl Compounds
Cytosol
Interferons
Melanoma
Oxidoreductases

ASJC Scopus subject areas

  • Immunology

Cite this

Compartmentalization of class II antigen presentation : Contribution of cytoplasmic and endosomal processing. / Li, Ping; Gregg, Josetta L.; Wang, Nan; Zhou, Delu; O'Donnell, Patrick; Blum, Janice; Crotzer, Victoria L.

In: Immunological Reviews, Vol. 207, 10.2005, p. 206-217.

Research output: Contribution to journalArticle

Li, Ping ; Gregg, Josetta L. ; Wang, Nan ; Zhou, Delu ; O'Donnell, Patrick ; Blum, Janice ; Crotzer, Victoria L. / Compartmentalization of class II antigen presentation : Contribution of cytoplasmic and endosomal processing. In: Immunological Reviews. 2005 ; Vol. 207. pp. 206-217.
@article{f888237b19294f2e9fcda9749de67c83,
title = "Compartmentalization of class II antigen presentation: Contribution of cytoplasmic and endosomal processing",
abstract = "During antigen processing, peptides are generated and displayed in the context of major histocompatibility complex (MHC) class II molecules on the surface of antigen-presenting cells (APCs) to modulate immune responses to foreign antigens and guide self-tolerance. Exogenous and cytoplasmic antigens are processed by distinct routes within APCs to yield class II ligands. Exogenous antigens are internalized, processed, and bound to class II molecules within endosomal and lysosomal compartments of APCs. Studies reviewed here demonstrate the importance of reduction in regulating exogenous antigen presentation. The differential expression of a γ-interferon-inducible lysosomal thiol reductase in professional APCs and melanomas is discussed in the context of tumor immune evasion. Cytoplasmic autoantigens, by contrast, are degraded by the proteasome and other enzymes in the cytosol, with the resulting peptides translocating to endosomal and lysosomal compartments for intersection with class II molecules. Processing and editing of these antigenic peptides within endosomes and lysosomes may be critical in regulating their display via class II proteins. Multiple pathways may regulate the transit of cytosolic peptides to class II molecules. The role of lysosome-associated membrane protein-2a and heat-shock cognate protein 70 in promoting cytoplasmic peptide presentation by MHC class II molecules is discussed.",
author = "Ping Li and Gregg, {Josetta L.} and Nan Wang and Delu Zhou and Patrick O'Donnell and Janice Blum and Crotzer, {Victoria L.}",
year = "2005",
month = "10",
doi = "10.1111/j.0105-2896.2005.00297.x",
language = "English",
volume = "207",
pages = "206--217",
journal = "Immunological Reviews",
issn = "0105-2896",
publisher = "Wiley-Blackwell",

}

TY - JOUR

T1 - Compartmentalization of class II antigen presentation

T2 - Contribution of cytoplasmic and endosomal processing

AU - Li, Ping

AU - Gregg, Josetta L.

AU - Wang, Nan

AU - Zhou, Delu

AU - O'Donnell, Patrick

AU - Blum, Janice

AU - Crotzer, Victoria L.

PY - 2005/10

Y1 - 2005/10

N2 - During antigen processing, peptides are generated and displayed in the context of major histocompatibility complex (MHC) class II molecules on the surface of antigen-presenting cells (APCs) to modulate immune responses to foreign antigens and guide self-tolerance. Exogenous and cytoplasmic antigens are processed by distinct routes within APCs to yield class II ligands. Exogenous antigens are internalized, processed, and bound to class II molecules within endosomal and lysosomal compartments of APCs. Studies reviewed here demonstrate the importance of reduction in regulating exogenous antigen presentation. The differential expression of a γ-interferon-inducible lysosomal thiol reductase in professional APCs and melanomas is discussed in the context of tumor immune evasion. Cytoplasmic autoantigens, by contrast, are degraded by the proteasome and other enzymes in the cytosol, with the resulting peptides translocating to endosomal and lysosomal compartments for intersection with class II molecules. Processing and editing of these antigenic peptides within endosomes and lysosomes may be critical in regulating their display via class II proteins. Multiple pathways may regulate the transit of cytosolic peptides to class II molecules. The role of lysosome-associated membrane protein-2a and heat-shock cognate protein 70 in promoting cytoplasmic peptide presentation by MHC class II molecules is discussed.

AB - During antigen processing, peptides are generated and displayed in the context of major histocompatibility complex (MHC) class II molecules on the surface of antigen-presenting cells (APCs) to modulate immune responses to foreign antigens and guide self-tolerance. Exogenous and cytoplasmic antigens are processed by distinct routes within APCs to yield class II ligands. Exogenous antigens are internalized, processed, and bound to class II molecules within endosomal and lysosomal compartments of APCs. Studies reviewed here demonstrate the importance of reduction in regulating exogenous antigen presentation. The differential expression of a γ-interferon-inducible lysosomal thiol reductase in professional APCs and melanomas is discussed in the context of tumor immune evasion. Cytoplasmic autoantigens, by contrast, are degraded by the proteasome and other enzymes in the cytosol, with the resulting peptides translocating to endosomal and lysosomal compartments for intersection with class II molecules. Processing and editing of these antigenic peptides within endosomes and lysosomes may be critical in regulating their display via class II proteins. Multiple pathways may regulate the transit of cytosolic peptides to class II molecules. The role of lysosome-associated membrane protein-2a and heat-shock cognate protein 70 in promoting cytoplasmic peptide presentation by MHC class II molecules is discussed.

UR - http://www.scopus.com/inward/record.url?scp=26244441528&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=26244441528&partnerID=8YFLogxK

U2 - 10.1111/j.0105-2896.2005.00297.x

DO - 10.1111/j.0105-2896.2005.00297.x

M3 - Article

C2 - 16181338

AN - SCOPUS:26244441528

VL - 207

SP - 206

EP - 217

JO - Immunological Reviews

JF - Immunological Reviews

SN - 0105-2896

ER -