Present yourself! By MHC class I and MHC class II molecules

KL Rock, E Reits, J Neefjes - Trends in immunology, 2016 - cell.com
Since the discovery of MHC molecules, it has taken 40 years to arrive at a coherent picture
of how MHC class I and MHC class II molecules really work. This is a story of the proteases …

[HTML][HTML] Antigen processing and presentation in cancer immunotherapy

MY Lee, JW Jeon, C Sievers… - Journal for immunotherapy …, 2020 - ncbi.nlm.nih.gov
Background Knowledge about and identification of T cell tumor antigens may inform the
development of T cell receptor-engineered adoptive cell transfer or personalized cancer …

The role of antigen processing and presentation in cancer and the efficacy of immune checkpoint inhibitor immunotherapy

A Mpakali, E Stratikos - Cancers, 2021 - mdpi.com
Simple Summary A new class of drugs, termed Immune Checkpoint Inhibitors, has
revolutionized cancer therapy during the last few years. Unfortunately, these drugs are only …

Exploiting non-canonical translation to identify new targets for T cell-based cancer immunotherapy

CM Laumont, C Perreault - Cellular and molecular life sciences, 2018 - Springer
Cryptic MHC I-associated peptides (MAPs) are produced via two mechanisms: translation of
protein-coding genes in non-canonical reading frames and translation of allegedly non …

Structural mechanism of tapasin-mediated MHC-I peptide loading in antigen presentation

J Jiang, DK Taylor, EJ Kim, LF Boyd, J Ahmad… - Nature …, 2022 - nature.com
Loading of MHC-I molecules with peptide by the catalytic chaperone tapasin in the peptide
loading complex plays a critical role in antigen presentation and immune recognition …

Structure of the TAPBPR–MHC I complex defines the mechanism of peptide loading and editing

C Thomas, R Tampé - Science, 2017 - science.org
Adaptive immunity is shaped by a selection of peptides presented on major
histocompatibility complex class I (MHC I) molecules. The chaperones Tapasin (Tsn) and …

Crystal structure of a TAPBPR–MHC I complex reveals the mechanism of peptide editing in antigen presentation

J Jiang, K Natarajan, LF Boyd, GI Morozov, MG Mage… - Science, 2017 - science.org
Central to CD8+ T cell–mediated immunity is the recognition of peptide–major
histocompatibility complex class I (p–MHC I) proteins displayed by antigen-presenting cells …

Xeno interactions between MHC-I proteins and molecular chaperones enable ligand exchange on a broad repertoire of HLA allotypes

Y Sun, GF Papadaki, CA Devlin, JN Danon… - Science …, 2023 - science.org
Immunological chaperones tapasin and TAP binding protein, related (TAPBPR) play key
roles in antigenic peptide optimization and quality control of nascent class I major …

Structure of an MHC I–tapasin–ERp57 editing complex defines chaperone promiscuity

IK Müller, C Winter, C Thomas, RM Spaapen… - Nature …, 2022 - nature.com
Adaptive immunity depends on cell surface presentation of antigenic peptides by major
histocompatibility complex class I (MHC I) molecules and on stringent ER quality control in …

MHC I assembly and peptide editing—chaperones, clients, and molecular plasticity in immunity

C Thomas, R Tampé - Current opinion in immunology, 2021 - Elsevier
Peptides presented on MHC I molecules allow the immune system to detect diseased cells.
The displayed peptides typically stem from proteasomal degradation of cytoplasmic proteins …