HLA-E monoclonal antibody MEM-E/02 binds to discontinuous but shared peptide sequences on HLA B & C heavy chains not treated by acid

Molecular Immunology

Volumn 47, Issue 9, 2010, Pages 1663-1664

  Ravindranath, Mepur H ^a   Kaneku, Hugo ^a   El Awar, Nadim ^b  

^a TERASAKI FOUNDATION LABORATORY   (United States)

^b One Lambda Inc   (United States)

Author keywords

2 Microglobulin ( 2m); Discontinuous epitope; Heavy chain; HLA class Ia (HLA Ia); HLA E; Linear epitope; MAb MEM E 02

Indexed keywords

ACID; HLA B ANTIGEN; HLA C ANTIGEN; HLA E ANTIGEN; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY MEM E 02; UNCLASSIFIED DRUG;

ALLOIMMUNITY; AMINO ACID SEQUENCE; ANTIGEN BINDING; BINDING AFFINITY; CROSS REACTION; HEAVY CHAIN; HUMAN; LETTER; MOLECULAR DYNAMICS; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DENATURATION; SEQUENCE HOMOLOGY; STEREOSPECIFICITY;

EID: 77952320499     PISSN: 01615890     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molimm.2010.02.003     Document Type: Letter

References (3)

1. 2m and surface expression in the absence of HLA class I signal sequence-derived peptides. J. Immunol. 2008, 181:5442-5450.
2. 2m-defective Daudi cells. J. Immunol. 2009, 182:3609-3617.
3. O'Callaghan C.A., Tormo J., Willcox B.E., Braud V.M., Jakobsen B.K., Stuart D.I., McMichael A.J., Bell J.I., Jones E.Y. Structural features impose tight peptide binding specificity in the nonclassical MHC molecule HLA-E. Mol. Cell. 1998, 1(4):531-541.