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Structural Relatedness of Distinct Determinants Recognized by Monoclonal Antibody TP25.99 on β2-Microglobulin-Associated and β2-Microglobulin-Free HLA Class I Heavy Chains
- Source :
- The Journal of Immunology. 165:3275-3283
- Publication Year :
- 2000
- Publisher :
- The American Association of Immunologists, 2000.
-
Abstract
- The association of HLA class I heavy chains with β2-microglobulin (β2m) changes their antigenic profile. As a result, Abs react with either β2m-free or β2m-associated HLA class I heavy chains. An exception to this rule is the mAb TP25.99, which reacts with both β2m-associated and β2m-free HLA class I heavy chains. The reactivity with β2m-associated HLA class I heavy chains is mediated by a conformational determinant expressed on all HLA-A, -B, and -C Ags. This determinant has been mapped to amino acid residues 194–198 in the α3 domain. The reactivity with β2m-free HLA class I heavy chains is mediated by a linear determinant expressed on all HLA-B Ags except the HLA-B73 allospecificity and on
- Subjects :
- Protein Conformation
medicine.drug_class
Molecular Sequence Data
Immunology
Human leukocyte antigen
Monoclonal antibody
Peptides, Cyclic
Antigen-Antibody Reactions
Epitopes
Mice
Antigen
HLA Antigens
Peptide Library
medicine
Animals
Humans
Immunology and Allergy
Bacteriophages
Amino Acid Sequence
Amino acid residue
Sequence Homology, Amino Acid
Beta-2 microglobulin
Chemistry
Histocompatibility Antigens Class I
Antibodies, Monoclonal
Peptide Fragments
Biochemistry
Binding Sites, Antibody
beta 2-Microglobulin
Subjects
Details
- ISSN :
- 15506606 and 00221767
- Volume :
- 165
- Database :
- OpenAIRE
- Journal :
- The Journal of Immunology
- Accession number :
- edsair.doi.dedup.....0794985942b80b35573329e4ab16232f