دورية أكاديمية
أعرض في EDS

Purification and structural characterization of siderophore (corynebactin) from Corynebacterium diphtheriae.

التفاصيل البيبلوغرافية
العنوان: Purification and structural characterization of siderophore (corynebactin) from Corynebacterium diphtheriae.
المؤلفون: Sheryl Zajdowicz, Jon C Haller, Amy E Krafft, Steve W Hunsucker, Colin T Mant, Mark W Duncan, Robert S Hodges, David N M Jones, Randall K Holmes
المصدر: PLoS ONE, Vol 7, Iss 4, p e34591 (2012)
بيانات النشر: Public Library of Science (PLoS), 2012.
سنة النشر: 2012
المجموعة: LCC:Medicine
LCC:Science
مصطلحات موضوعية: Medicine, Science
الوصف: During infection, Corynebacterium diphtheriae must compete with host iron-sequestering mechanisms for iron. C. diphtheriae can acquire iron by a siderophore-dependent iron-uptake pathway, by uptake and degradation of heme, or both. Previous studies showed that production of siderophore (corynebactin) by C. diphtheriae is repressed under high-iron growth conditions by the iron-activated diphtheria toxin repressor (DtxR) and that partially purified corynebactin fails to react in chemical assays for catecholate or hydroxamate compounds. In this study, we purified corynebactin from supernatants of low-iron cultures of the siderophore-overproducing, DtxR-negative mutant strain C. diphtheriae C7(β) ΔdtxR by sequential anion-exchange chromatography on AG1-X2 and Source 15Q resins, followed by reverse-phase high-performance liquid chromatography (RP-HPLC) on Zorbax C8 resin. The Chrome Azurol S (CAS) chemical assay for siderophores was used to detect and measure corynebactin during purification, and the biological activity of purified corynebactin was shown by its ability to promote growth and iron uptake in siderophore-deficient mutant strains of C. diphtheriae under iron-limiting conditions. Mass spectrometry and NMR analysis demonstrated that corynebactin has a novel structure, consisting of a central lysine residue linked through its α- and ε- amino groups by amide bonds to the terminal carboxyl groups of two different citrate residues. Corynebactin from C. diphtheriae is structurally related to staphyloferrin A from Staphylococcus aureus and rhizoferrin from Rhizopus microsporus in which d-ornithine or 1,4-diaminobutane, respectively, replaces the central lysine residue that is present in corynebactin.
نوع الوثيقة: article
وصف الملف: electronic resource
اللغة: English
تدمد: 1932-6203
Relation: http://europepmc.org/articles/PMC3326035?pdf=render; https://doaj.org/toc/1932-6203
DOI: 10.1371/journal.pone.0034591
URL الوصول: https://doaj.org/article/71d2dd2f74cf44348ba71f7c3cb1ef4b
رقم الأكسشن: edsdoj.71d2dd2f74cf44348ba71f7c3cb1ef4b
قاعدة البيانات: Directory of Open Access Journals
الوصف
تدمد:19326203
DOI:10.1371/journal.pone.0034591