Identification and characterization of a periplasmic trilactone esterase, Cee, revealed unique features of ferric enterobactin acquisition in Campylobacter
文献类型： 外文期刊
作者： Zeng, Ximin 1 ; Mo, Yiming 1 ; Xu, Fuzhou 1 ; Lin, Jun 1 ;
作者机构： 1.Univ Tennessee, Dept Anim Sci, Knoxville, TN 37996 USA
2.Beijing Acad Agr & Forestry Sci, Inst Anim Sci & Vet Med, Beijing 100097, Peoples R China
期刊名称：MOLECULAR MICROBIOLOGY （ 影响因子：3.501； 五年影响因子：3.996 ）
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收录情况： SCI
摘要： Ferric enterobactin (FeEnt) acquisition is a highly efficient and conserved iron scavenging system in Gram-negative bacteria. Recently, we have characterized two FeEnt receptors (CfrA and CfrB) in Campylobacter jejuni and C. coli, the enteric human pathogens that do not produce any siderophores. In this study, whole-genome sequencing and comparative genomic analysis identified a unique Ent trilactone esterase Cee (Cj1376) in C.jejuni. Genomic analysis and biochemical assay strongly suggested that Cee is the sole trilactone esterase in C.jejuni. Thin-layer chromatography and HPLC analyses showed high efficiency of the purified Cee to hydrolyse Ent. Three Cee homologues previously characterized from other bacteria (IroE, IroD and Fes) were also purified and analysed together with Cee, indicating that Cee, Fes and IroD displayed similar hydrolysis dynamics for both apo and ferric forms of Ent while IroE catalysed Ent inefficiently. Unlike cytoplasmic Fes and IroD, Cee is localized in the periplasm as demonstrated by immunoblotting using Cee-specific antibodies. Genetic manipulation of diverse Campylobacter strains demonstrated that Cee is not only essential for CfrB-dependent FeEnt acquisition but also involved in CfrA-dependent pathway. Together, this study identified and characterized a novel periplasmic trilactone esterase and suggested a new model of FeEnt acquisition in Campylobacter.
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