novel antibacterial activity of β2-microglobulin in human amniotic fluid新颖的抗菌活性β2-microglobulin人类羊水.pdfVIP

Novel Antibacterial Activity of b -Microglobulin in 2 Human Amniotic Fluid 1 1 1 2 3 Jin-Young Kim , Seong-Cheol Park , Jong-Kook Lee , Sang Joon Choi , Kyung-Soo Hahm , Yoonkyung Park1,4* 1 Research Center for Proteinaceous Materials, Chosun University, Kwangju, Korea, 2 Department of Obstetrics and Gynecology, School of Medicine, Chosun University, Kwangju, Korea, 3 Bioleaders Corporation, Yusong-Ku, Daejeon, Korea, 4 Department of Biotechnology, Chosun University, Kwangju, Korea Abstract An antibacterial protein (about 12 kDa) was isolated from human amniotic fluid through dialysis, ultrafiltration and C18 reversed-phase HPLC steps. Automated Edman degradation showed that the N-terminal sequence of the antibacterial protein was NH2-Ile-Gln-Arg-Thr-Pro-Lys-Ile-Gln-Val-Tyr-Ser-Arg-His-Pro-Ala-Glu-Asn-Gly-. The N-terminal sequence of the antibacterial protein was found to be identical to that of b2-microglobulin, a component of MHC class I molecules, which are present on all nucleated cells. Matrix-assisted laser desorption ionization mass spectrometry (MALDI-MS) revealed that the molecular mass of the antibacterial protein was 11,631 Da. This antibacterial protein, b2M, possessed potent antibacterial activity against pathogenic bacteria. Specially, antibacterial activity was observed in potassium buffer, and potassium ion was found to be critical for the antibacterial activity. Interestingly, the antibacterial action of b2M was associated with dissipation of the transmembrane potential, but the protein did not cause damage to the membrane that would result in SYTOX green uptake. In addition, stimu