Small, anionic, and charge-neutralizing propeptide fragments of zymogens are antimicrobial

被引:65
作者
Brogden, KA
Ackermann, M
Huttner, KM
机构
[1] IOWA STATE UNIV, DEPT VET PATHOL, AMES, IA 50011 USA
[2] BOSTON CHILDRENS HOSP, DEPT MED, JOINT PROGRAM NEONATOL, BOSTON, MA 02115 USA
关键词
D O I
10.1128/AAC.41.7.1615
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Some inactive precursor proteins, or zymogens, contain small, amino terminus, homopolymeric regions of Asp that neutralize the cationic charge of the active protein during synthesis. After posttranslational cleavage, the anionic propeptide fragment may exhibit antimicrobial activity. To demonstrate this, ovine trypsinogen activation peptide, and frog (Xenopus laevis) Pn activation peptide, both containing homopolymeric regions of Asp, were synthesized and tested against previously described surfactant-associated anionic peptide. Peptides inhibited the growth of both gram-negative (MIC, 0.08 to 3.00 mM) and gram-positive (MIC, 0.94 to 2.67 mM) bacteria. Smalt, anionic, and charge-neutralizing propeptide fragments of zymogens form a new class of host-derived antimicrobial peptides important in innate defense.
引用
收藏
页码:1615 / 1617
页数:3
相关论文
共 29 条