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Title: Humidity control as a strategy for lattice optimization applied to crystals of HLA-A*1101 complexed with variant peptides from dengue virus

Abstract

Crystals of an MHC class I molecule bound to naturally occurring peptide variants from the dengue virus NS3 protein contained high levels of solvent and required optimization of cryoprotectant and dehydration protocols for each complex to yield well ordered diffraction, a process facilitated by the use of a free-mounting system. T-cell recognition of the antigenic peptides presented by MHC class I molecules normally triggers protective immune responses, but can result in immune enhancement of disease. Cross-reactive T-cell responses may underlie immunopathology in dengue haemorrhagic fever. To analyze these effects at the molecular level, the functional MHC class I molecule HLA-A*1101 was crystallized bound to six naturally occurring peptide variants from the dengue virus NS3 protein. The crystals contained high levels of solvent and required optimization of the cryoprotectant and dehydration protocols for each complex to yield well ordered diffraction, a process that was facilitated by the use of a free-mounting system.

Authors:
 [1];  [2]; ;  [3];  [1];  [2]; ; ; ;  [3];  [4];  [5];  [1];  [1];  [2];  [3];  [6]
  1. Department of Immunology, Division of Medicine, Hammersmith Hospital, Imperial College, London (United Kingdom)
  2. (Thailand)
  3. Division of Structural Biology and Oxford Protein Production Facility (OPPF), The Henry Wellcome Building for Genomic Medicine, Roosevelt Drive, Headington, Oxford OX3 7BN (United Kingdom)
  4. Medical Molecular Biology Unit, Faculty of Medicine, Siriraj Hospital, Mahidol University (Thailand)
  5. (BIOTEC), National Science and Technology Development Agency, Pathumthani, Bangkok (Thailand)
  6. (United Kingdom)
Publication Date:
OSTI Identifier:
22360322
Resource Type:
Journal Article
Resource Relation:
Journal Name: Acta Crystallographica. Section F; Journal Volume: 63; Journal Issue: Pt 5; Other Information: PMCID: PMC2334998; PMID: 17565177; PUBLISHER-ID: en5229; OAI: oai:pubmedcentral.nih.gov:2334998; Copyright (c) International Union of Crystallography 2007; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United Kingdom
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; CRYSTALS; DEHYDRATION; DIFFRACTION; MOLECULES; OPTIMIZATION; SOLVENTS; YIELDS

Citation Formats

Chotiyarnwong, Pojchong, Medical Molecular Biology Unit, Faculty of Medicine, Siriraj Hospital, Mahidol University, Stewart-Jones, Guillaume B., Tarry, Michael J., Dejnirattisai, Wanwisa, Medical Molecular Biology Unit, Faculty of Medicine, Siriraj Hospital, Mahidol University, Siebold, Christian, Koch, Michael, Stuart, David I., Harlos, Karl, Malasit, Prida, Medical Biotechnology Unit, National Center for Genetic Engineering and Biotechnology, Screaton, Gavin, Mongkolsapaya, Juthathip, E-mail: j.mongkolsapaya@imperial.ac.uk, Medical Molecular Biology Unit, Faculty of Medicine, Siriraj Hospital, Mahidol University, Jones, E. Yvonne, E-mail: j.mongkolsapaya@imperial.ac.uk, and Department of Immunology, Division of Medicine, Hammersmith Hospital, Imperial College, London. Humidity control as a strategy for lattice optimization applied to crystals of HLA-A*1101 complexed with variant peptides from dengue virus. United Kingdom: N. p., 2007. Web. doi:10.1107/S1744309107013693.
Chotiyarnwong, Pojchong, Medical Molecular Biology Unit, Faculty of Medicine, Siriraj Hospital, Mahidol University, Stewart-Jones, Guillaume B., Tarry, Michael J., Dejnirattisai, Wanwisa, Medical Molecular Biology Unit, Faculty of Medicine, Siriraj Hospital, Mahidol University, Siebold, Christian, Koch, Michael, Stuart, David I., Harlos, Karl, Malasit, Prida, Medical Biotechnology Unit, National Center for Genetic Engineering and Biotechnology, Screaton, Gavin, Mongkolsapaya, Juthathip, E-mail: j.mongkolsapaya@imperial.ac.uk, Medical Molecular Biology Unit, Faculty of Medicine, Siriraj Hospital, Mahidol University, Jones, E. Yvonne, E-mail: j.mongkolsapaya@imperial.ac.uk, & Department of Immunology, Division of Medicine, Hammersmith Hospital, Imperial College, London. Humidity control as a strategy for lattice optimization applied to crystals of HLA-A*1101 complexed with variant peptides from dengue virus. United Kingdom. doi:10.1107/S1744309107013693.
Chotiyarnwong, Pojchong, Medical Molecular Biology Unit, Faculty of Medicine, Siriraj Hospital, Mahidol University, Stewart-Jones, Guillaume B., Tarry, Michael J., Dejnirattisai, Wanwisa, Medical Molecular Biology Unit, Faculty of Medicine, Siriraj Hospital, Mahidol University, Siebold, Christian, Koch, Michael, Stuart, David I., Harlos, Karl, Malasit, Prida, Medical Biotechnology Unit, National Center for Genetic Engineering and Biotechnology, Screaton, Gavin, Mongkolsapaya, Juthathip, E-mail: j.mongkolsapaya@imperial.ac.uk, Medical Molecular Biology Unit, Faculty of Medicine, Siriraj Hospital, Mahidol University, Jones, E. Yvonne, E-mail: j.mongkolsapaya@imperial.ac.uk, and Department of Immunology, Division of Medicine, Hammersmith Hospital, Imperial College, London. Tue . "Humidity control as a strategy for lattice optimization applied to crystals of HLA-A*1101 complexed with variant peptides from dengue virus". United Kingdom. doi:10.1107/S1744309107013693.
@article{osti_22360322,
title = {Humidity control as a strategy for lattice optimization applied to crystals of HLA-A*1101 complexed with variant peptides from dengue virus},
author = {Chotiyarnwong, Pojchong and Medical Molecular Biology Unit, Faculty of Medicine, Siriraj Hospital, Mahidol University and Stewart-Jones, Guillaume B. and Tarry, Michael J. and Dejnirattisai, Wanwisa and Medical Molecular Biology Unit, Faculty of Medicine, Siriraj Hospital, Mahidol University and Siebold, Christian and Koch, Michael and Stuart, David I. and Harlos, Karl and Malasit, Prida and Medical Biotechnology Unit, National Center for Genetic Engineering and Biotechnology and Screaton, Gavin and Mongkolsapaya, Juthathip, E-mail: j.mongkolsapaya@imperial.ac.uk and Medical Molecular Biology Unit, Faculty of Medicine, Siriraj Hospital, Mahidol University and Jones, E. Yvonne, E-mail: j.mongkolsapaya@imperial.ac.uk and Department of Immunology, Division of Medicine, Hammersmith Hospital, Imperial College, London},
abstractNote = {Crystals of an MHC class I molecule bound to naturally occurring peptide variants from the dengue virus NS3 protein contained high levels of solvent and required optimization of cryoprotectant and dehydration protocols for each complex to yield well ordered diffraction, a process facilitated by the use of a free-mounting system. T-cell recognition of the antigenic peptides presented by MHC class I molecules normally triggers protective immune responses, but can result in immune enhancement of disease. Cross-reactive T-cell responses may underlie immunopathology in dengue haemorrhagic fever. To analyze these effects at the molecular level, the functional MHC class I molecule HLA-A*1101 was crystallized bound to six naturally occurring peptide variants from the dengue virus NS3 protein. The crystals contained high levels of solvent and required optimization of the cryoprotectant and dehydration protocols for each complex to yield well ordered diffraction, a process that was facilitated by the use of a free-mounting system.},
doi = {10.1107/S1744309107013693},
journal = {Acta Crystallographica. Section F},
number = Pt 5,
volume = 63,
place = {United Kingdom},
year = {Tue May 01 00:00:00 EDT 2007},
month = {Tue May 01 00:00:00 EDT 2007}
}