scholarly journals Peptide-binding motifs associated with MHC molecules common in Chinese rhesus macaques are analogous to those of human HLA supertypes and include HLA-B27-like alleles

2013 ◽  
Vol 65 (5) ◽  
pp. 371-386 ◽  
Author(s):  
Bianca R. Mothé ◽  
Scott Southwood ◽  
John Sidney ◽  
A. Michelle English ◽  
Amanda Wriston ◽  
...  
2013 ◽  
Vol 65 (12) ◽  
pp. 897-900 ◽  
Author(s):  
Natasja G. de Groot ◽  
Corrine M. C. Heijmans ◽  
Arnoud H. de Ru ◽  
Chopie Hassan ◽  
Nel Otting ◽  
...  

2017 ◽  
Vol 69 (5) ◽  
pp. 351-358
Author(s):  
Tobias Bergmann ◽  
Mikaela Lindvall ◽  
Erin Moore ◽  
Eugene Moore ◽  
John Sidney ◽  
...  

Author(s):  
Marcus Davidsson ◽  
Gang Wang ◽  
Patrick Aldrin-Kirk ◽  
Tiago Cardoso ◽  
Sara Nolbrant ◽  
...  

1996 ◽  
Vol 183 (3) ◽  
pp. 1253-1258 ◽  
Author(s):  
W W Kwok ◽  
M E Domeier ◽  
M L Johnson ◽  
G T Nepom ◽  
D M Koelle

The association of specific HLA-DQ alleles with autoimmunity is correlated with discrete polymorphisms in the HLA-DQ sequence that are localized within sites suitable for peptide recognition. The polymorphism at residue 57 of the DQB1 polypeptide is of particular interest since it may play a major structural role in the formation of a salt bridge structure at one end of the peptide-binding cleft of the DQ molecules. This polymorphism at residue 57 is a recurrent feature of HLA-DQ evolution, occurring in multiple distinct allelic families, which implies a functional selection for maintaining variation at this position in the class II molecule. We directly tested the amino acid polymorphism at this site as a determinant for peptide binding and for antigen-specific T cell stimulation. We found that a single Ala-->Asp amino acid 57 substitution in an HLA-DQ3.2 molecule regulated binding of an HSV-2 VP-16-derived peptide. A complementary single-residue substitution in the peptide abolished its binding to DQ3.2 and converted it to a peptide that can bind to DQ3.1 and DQ3.3 Asp-57-positive MHC molecules. These binding studies were paralleled by specific T cell recognition of the class II-peptide complex, in which the substituted peptide abolished T cell reactivity, which was directed to the DQ3.2-peptide complex, whereas the same T cell clone recognized the substituted peptide presented by DQ3.3, a class II restriction element differing from DQ3.2 only at residue 57. This structural and functional complementarity for residue 57 and a specific peptide residue identifies this interaction as a key controlling determinant of restricted recognition in HLA-DQ-specific immune response.


Toxins ◽  
2015 ◽  
Vol 7 (1) ◽  
pp. 156-169 ◽  
Author(s):  
Rui-Rui Wang ◽  
Ka-Yee Au ◽  
Hong-Yi Zheng ◽  
Liang-Min Gao ◽  
Xuan Zhang ◽  
...  

2020 ◽  
Vol 3 (1) ◽  
pp. 191-215 ◽  
Author(s):  
Morten Nielsen ◽  
Massimo Andreatta ◽  
Bjoern Peters ◽  
Søren Buus

Immunoinformatics is a discipline that applies methods of computer science to study and model the immune system. A fundamental question addressed by immunoinformatics is how to understand the rules of antigen presentation by MHC molecules to T cells, a process that is central to adaptive immune responses to infections and cancer. In the modern era of personalized medicine, the ability to model and predict which antigens can be presented by MHC is key to manipulating the immune system and designing strategies for therapeutic intervention. Since the MHC is both polygenic and extremely polymorphic, each individual possesses a personalized set of MHC molecules with different peptide-binding specificities, and collectively they present a unique individualized peptide imprint of the ongoing protein metabolism. Mapping all MHC allotypes is an enormous undertaking that cannot be achieved without a strong bioinformatics component. Computational tools for the prediction of peptide–MHC binding have thus become essential in most pipelines for T cell epitope discovery and an inescapable component of vaccine and cancer research. Here, we describe the development of several such tools, from pioneering efforts to the current state-of-the-art methods, that have allowed for accurate predictions of peptide binding of all MHC molecules, even including those that have not yet been characterized experimentally.


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