Open AccessHumidity control as a strategy for lattice optimization applied to crystals of HLA‐A*1101 complexed with variant peptides from dengue virus
Author(s) -
Chotiyarnwong Pojchong,
StewartJones Guillaume B.,
Tarry Michael J.,
Dejnirattisai Wanwisa,
Siebold Christian,
Koch Michael,
Stuart David I.,
Harlos Karl,
Malasit Prida,
Screaton Gavin,
Mongkolsapaya Juthathip,
Jones E. Yvonne
Publication year - 2007
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309107013693
Subject(s) - dengue fever , major histocompatibility complex , dengue virus , immune system , human leukocyte antigen , mhc class i , antigen , peptide , biology , chemistry , virology , biochemistry , immunology
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.