Humidity control as a strategy for lattice optimization applied to crystals of HLA-A*1101 complexed with variant peptides from dengue virus.
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.
Chotiyarnwong
Pojchong
P
Department of Immunology, Division of Medicine, Hammersmith Hospital, Imperial College, London, England.
Stewart-Jones
Guillaume B
GB
Tarry
Michael J
MJ
Dejnirattisai
Wanwisa
W
Siebold
Christian
C
Koch
Michael
M
Stuart
David I
DI
Harlos
Karl
K
Malasit
Prida
P
Screaton
Gavin
G
Mongkolsapaya
Juthathip
J
Jones
E Yvonne
EY
D000595:Amino Acid Sequence; D002850:Chromatography, Gel; D003460:Crystallization; D018360:Crystallography, X-Ray; D003716:Dengue Virus / Q000737:chemistry*; D015234:HLA-A Antigens / Q000737:chemistry*; D006813:Humidity; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D014764:Viral Proteins / Q000737:chemistry*
D015234:HLA-A Antigens; D010455:Peptides; D014764:Viral Proteins