Mapping of Hsp70‐binding sites on protein antigens
- 1 May 1994
- journal article
- Published by Wiley in European Journal of Biochemistry
- Vol. 222 (1), 65-73
- https://doi.org/10.1111/j.1432-1033.1994.tb18842.x
Abstract
Hsp70-binding sites were mapped on three antigens, the 16-, 19- and 38-kDa proteins of Mycobacterium tuberculosis, using overlapping synthetic peptides in a competitive-binding assay. In each protein, two or three prominent hsp70-binding sites were identified when peptides 20-amino-acid long were used, predominantly in regions containing clusters of aliphatic amino acids. Although there was an overall concordance in the pattern of peptide binding to hsp70 from bacterial (M. tuberculosis) and mammalian sources (immunoglobulin heavy-chain-binding protein), some differences in the specificity of polypeptide binding and the effect of peptides on ATPase activity were observed.Keywords
This publication has 28 references indexed in Scilit:
- Constitutive HSP70: Oligomerization and its dependence on ATP bindingJournal of Cellular Physiology, 1992
- T cell repertoire in tuberculosis: selective anergy to an immunodominant epitope of the 38‐kDa antigen in patients with active diseaseEuropean Journal of Immunology, 1992
- Protein folding in the cellNature, 1992
- Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate proteinNature, 1990
- A peptide binding protein having a role in antigen presentation is a member of the HSP70 heat shock family.The Journal of Experimental Medicine, 1989
- A Role for a 70-Kilodalton Heat Shock Protein in Lysosomal Degradation of Intracellular ProteinsScience, 1989
- Biochemical and antigenic characterization of the Mycobacterium tuberculosis 71 kD antigen, a member of the 70 kD heat‐shock protein familyMolecular Microbiology, 1989
- The Heat-Shock ResponseAnnual Review of Biochemistry, 1986
- Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.Proceedings of the National Academy of Sciences, 1979
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970