Àá½Ã¸¸ ±â´Ù·Á ÁÖ¼¼¿ä. ·ÎµùÁßÀÔ´Ï´Ù.
KMID : 0357119950170010033
Korean Journal of Immunology
1995 Volume.17 No. 1 p.33 ~ p.40
Analysis of HLA-A2-restricted Epitope Peotides of Hepatitis B Virus Proteins
ÀÌÈñ±¸
ÀÓÁ¾¼®/±è½Â¸ñ/À̱⿵/±èÈñ¼ö/±è½ÂÈ£/±ÇÅÂÁ¾/ÃÖÀμº/ÀåÅÂÈ­
Abstract
The cytotoxic T lymphocyte (CTL) are important component in host defense mechanism against viral infection. They can recongnize virus-derived peptides presented by the Class I MHC molecule at the infected cells. On searching for effective CTL
epitopes
of hepatitis B virus(HBV), we synthesized a distinct set of 9-10 mer peptide containing amino acid sequence of hepatitis B virus surface protein that are selected on the basis of a computer modeling and the prevously described HLA-A2 specific
motifs.
Binding assay of the synthetic peptides to HLA-A2 molecules using human antigen processing defectant T2 cells showed that 3 out of 4 synthetic peptides wenhanced the expression of HLA-A2 molecule on T2 cell surface. Two anchor positions, namely
P2
and
P9( or P10) appeared to play a decisive role for binding. Structural characteristics of the peptides addressed by molecular dynamics simulation was analysed and compared. These peptides also partially triggered CTL isolated from human peripheral
blood
mononuclear cells of HBVS positive patients, and the response was peptide-spcific. These results showed that negatively-charged amino acid residue at P2 hampered binding affinity of the peptides to HLA-A2 molecules, and that binding affinity of
the
peptides are not always reflected by teir immunogenicity among natural T cell repertoire.
KEYWORD
FullTexts / Linksout information
Listed journal information
KoreaMed ´ëÇÑÀÇÇÐȸ ȸ¿ø