Analysis of the receptor of an antibacterial peptide on human neutrophils.

抗菌肽KLKLLLLKLK-NH_2(L5)对感染MRSA的小鼠具有明显的体内化疗活性。我们发现L5激活了人的中性粒细胞，导致了超氧化物的产生。利用与L5偶联的亲和柱层析，从人中性粒细胞膜蛋白中纯化出分子量为55 kDa的结合蛋白。百日咳毒素抑制L5对中性粒细胞的激活，提示L5进入中性粒细胞的信号是通过GTP结合蛋白介导的。这种分子质量为55 kDa的结合蛋白有望成为寻找治疗某些传染病有效药物的靶向分子。

An antibacterial peptide, KLKLLLLLKLK-NH_2 (L5) showed significant chemotherapeutic activity in MRSA-infected mice in vivo. We found that L5 activated the human neutrophil, resulting the production of superoxide. The binding protein with a molecular mass of 55 kDa was purified from membrane proteins of human neutrophil using affinity column chromatography conjugated with L5. The pertussis toxzin inhibited the activation of L5 to the neutrophil, suggesting that the signal of L5 into the neutrophil is mediated via GTP-binding protein. The binding protein with a molecular mass of 55 kDa is expected to be the target molecule to search for effective drugs for some infectious diseases.