NDLI: A common SNP in ER aminopeptidase 2 induces a specificity switch that leads to altered antigen processing

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A common SNP in ER aminopeptidase 2 induces a specificity switch that leads to altered antigen processing

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A common SNP in ER aminopeptidase 2 induces a specificity switch that leads to altered antigen processing

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Giastas, Petros Evnouchidou, Irini Birtley, James Georgiadis, Dimitris Amalfitano, Andrea Papakyriakou, Athanasios Zervoudi, Efthalia Stratikos, Efstratios Petrakis, Olivia Panayotou, George Seregin, Sergey Saridakis, Emmanuel Mavridis, Irene M. Samiotaki, Martina
Description	Country affiliation: Greece Author Affiliation: Evnouchidou I ( National Center for Scientific Research Demokritos, 15310 Athens, Greece.)
Abstract	Endoplasmic reticulum aminopeptidases 1 and 2 (ERAP1 and ERAP2) cooperate to trim antigenic peptide precursors for loading onto MHC class I molecules and help regulate the adaptive immune response. Common coding single nucleotide polymorphisms in ERAP1 and ERAP2 have been linked with predisposition to human diseases ranging from viral and bacterial infections to autoimmunity and cancer. It has been hypothesized that altered Ag processing by these enzymes is a causal link to disease etiology, but the molecular mechanisms are obscure. We report in this article that the common ERAP2 single nucleotide polymorphism rs2549782 that codes for amino acid variation N392K leads to alterations in both the activity and the specificity of the enzyme. Specifically, the 392N allele excises hydrophobic N-terminal residues from epitope precursors up to 165-fold faster compared with the 392K allele, although both alleles are very similar in excising positively charged N-terminal amino acids. These effects are primarily due to changes in the catalytic turnover rate (k(cat)) and not in the affinity for the substrate. X-ray crystallographic analysis of the ERAP2 392K allele suggests that the polymorphism interferes with the stabilization of the N terminus of the peptide both directly and indirectly through interactions with key residues participating in catalysis. This specificity switch allows the 392N allele of ERAP2 to supplement ERAP1 activity for the removal of hydrophobic N-terminal residues. Our results provide mechanistic insight to the association of this ERAP2 polymorphism with disease and support the idea that polymorphic variation in Ag processing enzymes constitutes a component of immune response variability in humans.
ISSN	00221767
e-ISSN	15506606
DOI	10.4049/jimmunol.1200918
Journal	The Journal of Immunology
Issue Number	5
Volume Number	189
Language	English
Publisher	The American Association of Immunologists
Publisher Date	2012-09-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Aminopeptidases Genetics Antigen Presentation Immunology Endoplasmic Reticulum Enzymology Immunoglobulin Class Switching Polymorphism, Single Nucleotide Amino Acid Sequence Crystallography, X-ray Enzyme Activation Genetic Variation Hela Cells Molecular Sequence Data Substrate Specificity Research Support, N.i.h., Extramural Research Support, Non-u.s. Gov't Discipline Immunology
Content Type	Text
Resource Type	Article
Subject	Immunology and Allergy Immunology

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