Abstract
The interaction forces and binding kinetics between SIRPα and CD47 were investigated by single-molecule force spectroscopy (SMFS) on both fresh and experimentally aged human red blood cells (hRBCs). We found that CD47 experienced a conformation change after oxidation, which influenced the interaction force and the position of the energy barrier between SIRPα and CD47. Our results are significant for understanding the mechanism of phagocytosis of red blood cells at the single molecule level.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Antigens, Differentiation / chemistry*
-
Antigens, Differentiation / ultrastructure
-
Binding Sites
-
CD47 Antigen / chemistry*
-
CD47 Antigen / ultrastructure
-
Cells, Cultured
-
Erythrocyte Membrane / chemistry*
-
Erythrocyte Membrane / ultrastructure
-
Humans
-
Kinetics
-
Microscopy, Atomic Force / methods*
-
Protein Binding
-
Protein Interaction Mapping / methods*
-
Receptors, Immunologic / chemistry*
-
Receptors, Immunologic / ultrastructure
-
Stress, Mechanical
Substances
-
Antigens, Differentiation
-
CD47 Antigen
-
CD47 protein, human
-
Receptors, Immunologic
-
SIRPA protein, human