Shi J, Ross C R, Chengappa M M, Sylte M J, McVey D S, Blecha F
Department of Anatomy and Physiology, College of Veterinary Medicine, Kansas State University, Manhattan 66506, USA.
Antimicrob Agents Chemother. 1996 Jan;40(1):115-21. doi: 10.1128/AAC.40.1.115.
PR-39 is a proline-arginine-rich (PR) neutrophil antibacterial peptide originally identified and purified from the porcine small intestine. We report on the synthesis of a functional antibacterial domain of PR-39, the first 26 amino acid residues of the NH2 terminus. PR-26 was as potent as or more potent than PR-39 against enteric gram-negative bacteria. This truncated form of PR-39 potentiated neutrophil phagocytosis of Salmonella choleraesuis and decreased the level of S. typhimurium invasion into intestinal epithelial cells. Scanning electron microscopy confirmed that these peptides did not lyse cells by pore-forming mechanisms; however, they potentiated the antibacterial capabilities of a pore-forming peptide, magainin A. In addition, PR-26 was not toxic to epithelial cells at concentrations several times greater than its bactericidal concentration. These data suggest that PR-39 and its functional domain, PR-26, may potentiate the host's defense capabilities against gram-negative infections.
PR-39是一种富含脯氨酸-精氨酸(PR)的中性粒细胞抗菌肽,最初是从猪小肠中鉴定并纯化出来的。我们报道了PR-39功能性抗菌结构域(NH2末端的前26个氨基酸残基)的合成。PR-26对肠道革兰氏阴性菌的抗菌能力与PR-39相当或更强。这种PR-39的截短形式增强了中性粒细胞对猪霍乱沙门氏菌的吞噬作用,并降低了鼠伤寒沙门氏菌侵入肠道上皮细胞的水平。扫描电子显微镜证实,这些肽不是通过形成孔道的机制裂解细胞;然而,它们增强了一种形成孔道的肽——马盖宁A的抗菌能力。此外,PR-26在浓度比其杀菌浓度高几倍时对上皮细胞无毒。这些数据表明,PR-39及其功能性结构域PR-26可能增强宿主对革兰氏阴性菌感染的防御能力。