Autoantigenicity of human C1q is associated with increased hydrophobicity due to conformational transitions in the globular heads

作者：Stoyanova Vishnya^*; Bogoeva Vanya; Petrova Lidiya; Tchorbadjieva Magdalena; Petrova Svetla; Georgieva Ventsislava; Georgiev George; Deliyska Boriana; Vasilev Vasil; Tsacheva Ivanka

来源：Molecular Biosystems, 2015, 11(5): 1370-1377.

DOI：10.1039/c5mb00021a

We analyzed the structural features of C1q that underlie its autoantigenicity by means of a model system using the amphiphilic polyzwitterion (PZ), poly(ethylene oxide-b-N, N-dimethyl(methacryloyloxyethyl) ammonium propanesulfonate) in the process of C1q immobilization. The source of anti-C1q auto-antibodies was human sera from patients with Lupus Nephritis (LN). Both analyzed concentrations of PZ, 25 mM and 50 mM, were found to be applicable for inducing conformational transitions which resulted in increased recognition of C1q and the globular domain of its B polypeptide chain, designated ghB, by the LN autoantibodies. The registered conformational transitions displayed a hydrophobic enhancement of the protein microenvironment due to the presence of hydrophobic binding sites in ghB which consequently affected the autoantigenicity of the whole C1q molecule.

• 出版日期2015