Studies on β2-Glycoprotein Ⅰ Recognizing Molecules from a Phage Peptide Library

β2-Glycoprotein I(β2-GPI) has been identified as a cofactor in the recognition of phospholipid Ag cardiolipin (CL) by anticardiolipin Ab(aCL) purified from patients' serum with autoimmune disease. However, there is a considerable controversy as to the anti-β2-GPI -antibodies occurred in aCL. In order to select β2-GPI recognizing molecules, β2-GPI was used as a probe to screen affinity phage clones panned from a phage peptide library. After four cycles of selection, the phage recovery increased from 2.4×10-5% to 1.1×10-3%, indicating that a specific enrichment had been achieved. In order to characterize these phage clones, we investigated their specific binding to β2-GPI and their inhibition of β2-GPI binding to anti-β2-GPI antibodies. Almost 40 percent of clones reflected considerable binding abilities and inhibitory activities towards anti-β2-GPI antibodies. A group of related peptides were identified by DNA sequencing, in which there were seven related peptide sequences, with four of them representing more than once. These peptide sequences display similarities at several positions. Sequence motif (-F-S-L-) was evident in most of the peptides. It suggests that these peptides may specifically block the anti-β2-GPI antibodies binding to β2-GPI. Our result supports the idea that β2-GPI acts as a Ag for these anti-β2-GPI antibodies occurred in the aCL.