Molecular Simulation Study on the Interaction between Porcine CR1-like and C3b

• Published in: Molecules (Basel, Switzerland) Switzerland), 2023-02, Vol.28 (5), p.2183
• Main Authors: Hou, Zhen, Yin, Wei, Hao, Zhili, Fan, Kuohai, Sun, Na, Sun, Panpan, Li, Hongquan
• Format: Article
• Language: English
• Subjects: Adhesion; Alanine; Alzheimer's disease; Amino acids; Analysis; Animals; Antigens; C3b; Cell membranes; Complement component C3; Complement component C3b; CR1-like; Crystal structure; Erythrocytes; Erythrocytes - metabolism; Homology; immune adhesion; Interaction models; Molecular docking; Molecular Docking Simulation; Molecular dynamics; Molecular structure; Mutation; Optimization; Peptides; Proteins; Receptors, Complement - metabolism; Residues; Simulation; Swine
• ISSN: 1420-3049; 1420-3049
• DOI: 10.3390/molecules28052183

The molecular basis of porcine red blood cell immune adhesion function stems from the complement receptor type 1-like (CR1-like) on its cell membrane. The ligand for CR1-like is C3b, which is produced by the cleavage of complement C3; however, the molecular mechanism of the immune adhesion of porcine erythrocytes is still unclear. Here, homology modeling was used to construct three-dimensional models of C3b and two fragments of CR1-like. An interaction model of C3b-CR1-like was constructed by molecular docking, and molecular structure optimization was achieved using molecular dynamics simulation. A simulated alanine mutation scan revealed that the amino acids Tyr761, Arg763, Phe765, Thr789, and Val873 of CR1-like SCR 12-14 and the amino acid residues Tyr1210, Asn1244, Val1249, Thr1253, Tyr1267, Val1322, and Val1339 of CR1-like SCR 19-21 are key residues involved in the interaction of porcine C3b with CR1-like. This study investigated the interaction between porcine CR1-like and C3b using molecular simulation to clarify the molecular mechanism of the immune adhesion of porcine erythrocytes.