Isolation and structure elucidation of acinetobactin., a novel siderophore from Acinetobacter baumannii

Yamamoto, Satoshi; Okujo, Noriyuki; Sakakibara, Yoshikazu

doi:10.1007/bf00301846

Cited by 96 publications

(132 citation statements)

References 29 publications

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“…In UV-visible spectrum, two peaks were observed; major peak at 250 nm while the minor peak at 317 nm (Figure 4) for sample in methanol which showed an absorption spectrum typical of catecholate compounds. These observations are in agreement with literature (Yamamoto et al, 1994). calcoaceticus showing broad peak at 317 nm and narrow peak at 250 nm -1 revealed the presence of C-O-C for ether linkage of oxazoline.…”

Section: Resultssupporting

confidence: 93%

“…The over all UV-Visible and IR spectra data suggested the similarity between the structure of catecholate type of siderophore i.e. acinetobactin (Yamamoto et al, 1994) and the siderophore sample of A. calcoaceticus.…”

Section: Resultsmentioning

confidence: 80%

“…This indicates that strain under study is distinct and different from siderophore producing clinical isolates of Acinetobacter sp. (Yamamoto et al, 1994). These results are promising for the development of siderophoregenic plant growth promoting Acinetobacter based bio-fertilizer and bio-fungicide.…”

Section: Resultsmentioning

confidence: 87%

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Siderophoregenic Acinetobacter calcoaceticus isolated from wheat rhizosphere with strong PGPR activity

D.¹,

Makarand²,

Bhushan³

et al. 2009

MJM

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Thirty-two bacterial isolates were obtained from wheat rhizosphere in black cotton soils of North Maharashtra region and subsequently tested for in-vitro siderophore production. Wheat isolate SCW1, being a strong siderophore producer, was selected, identified and confirmed as Acinetobacter calcoaceticus. The strain produced catechol type of siderophores during exponential phase which was influenced by iron content of medium. Seed bacterization with siderophoregenic A. calcoaceticus improved plant growth in pot and field studies. Such PGPR activity was attributed to the ability of strain to solubilise phosphates and produce IAA. Siderophore mediated antagonism was observed against common phytopathogens viz., Aspergillus flavus, A. niger, Colletotrichum capsicum and Fusarium oxysporum.

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Section: Resultssupporting

confidence: 93%

Section: Resultsmentioning

confidence: 80%

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Siderophoregenic Acinetobacter calcoaceticus isolated from wheat rhizosphere with strong PGPR activity

D.¹,

Makarand²,

Bhushan³

et al. 2009

MJM

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“…A. baumannii harbors between 21 and 27 TonB-dependent receptors compared to 35 in P. aeruginosa (26). So far, only FhuE (27) and BauA (28), the receptor for the siderophore acinetobactin (29,30), have been characterized in A. baumannii.…”

mentioning

confidence: 99%

Structure and Function of the PiuA and PirA Siderophore-Drug Receptors from Pseudomonas aeruginosa and Acinetobacter baumannii

Moynié

Lüscher

Rolo

et al. 2017

Antimicrob Agents Chemother

106

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The outer membrane of Gram-negative bacteria presents an efficient barrier to the permeation of antimicrobial molecules. One strategy pursued to circumvent this obstacle is to hijack transport systems for essential nutrients, such as iron. BAL30072 and MC-1 are two monobactams conjugated to a dihydroxypyridone siderophore that are active against Pseudomonas aeruginosa and Acinetobacter baumannii. Here, we investigated the mechanism of action of these molecules in A. baumannii. We identified two novel TonB-dependent receptors, termed Ab-PiuA and Ab-PirA, that are required for the antimicrobial activity of both agents. Deletion of either piuA or pirA in A. baumannii resulted in 4-to 8-fold-decreased susceptibility, while their overexpression in the heterologous host P. aeruginosa increased susceptibility to the two siderophore-drug conjugates by 4-to 32-fold. The crystal structures of PiuA and PirA from A. baumannii and their orthologues from P. aeruginosa were determined. The structures revealed similar architectures; however, structural differences between PirA and PiuA point to potential differences between their cognate siderophore ligands. Spontaneous mutants, selected upon exposure to BAL30072, harbored frameshift mutations in either the ExbD3 or the TonB3 protein of A. baumannii, forming the cytoplasmic-membrane complex providing the energy for the siderophore translocation process. The results of this study provide insight for the rational design of novel siderophore-drug conjugates against problematic Gramnegative pathogens.

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“…The iron-regulated production of phenolic and siderophore compounds was tested with the Arnow colorimetric assay (33) and the Chrome azurol S (CAS) reagent (34), respectively, using culture supernatants of bacteria grown in a succinate-based chemically defined medium (35). Acinetobactin production was tested with siderophore cross-feeding bioassays using the A. baumannii ATCC 19606 T t6 (bauA) and s1 (basD) insertion derivatives as reporter strains as described before (10).…”

Section: Methodsmentioning

confidence: 99%

Role of the Carboxy Terminus of SecA in Iron Acquisition, Protein Translocation, and Virulence of the Bacterial Pathogen Acinetobacter baumannii

et al. 2015

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Acinetobacter baumannii is a Gram-negative opportunistic nosocomial pathogen that causes pneumonia and soft tissue and systemic infections. Screening of a transposon insertion library of A. baumannii ATCC 19606 T resulted in the identification of the 2010 derivative, which, although capable of growing well in iron-rich media, failed to prosper under iron chelation. Genetic, molecular, and functional assays showed that 2010's iron utilization-deficient phenotype is due to an insertion within the 3= end of secA, which results in the production of a C-terminally truncated derivative of SecA. SecA plays a critical role in protein translocation through the SecYEG membrane channel. Accordingly, the secA mutation resulted in undetectable amounts of the ferric acinetobactin outer membrane receptor protein BauA while not affecting the production of other acinetobactin membrane protein transport components, such as BauB and BauE, or the secretion of acinetobactin by 2010 cells cultured in the presence of subinhibitory concentrations of the synthetic iron chelator 2,2=-dipyridyl. Outer membrane proteins involved in nutrient transport, adherence, and biofilm formation were also reduced in 2010. The SecA truncation also increased production of 30 different proteins, including proteins involved in adaptation/tolerance responses. Although some of these protein changes could negatively affect the pathobiology of the 2010 derivative, its virulence defect is mainly due to its inability to acquire iron via the acinetobactin-mediated system. These results together indicate that although the C terminus of the A. baumannii ATCC 19606 T SecA is not essential for viability, it plays a critical role in the production and translocation of different proteins and virulence.

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Isolation and structure elucidation of acinetobactin., a novel siderophore from Acinetobacter baumannii

Cited by 96 publications

References 29 publications

Siderophoregenic Acinetobacter calcoaceticus isolated from wheat rhizosphere with strong PGPR activity

Siderophoregenic Acinetobacter calcoaceticus isolated from wheat rhizosphere with strong PGPR activity

Structure and Function of the PiuA and PirA Siderophore-Drug Receptors from Pseudomonas aeruginosa and Acinetobacter baumannii

Role of the Carboxy Terminus of SecA in Iron Acquisition, Protein Translocation, and Virulence of the Bacterial Pathogen Acinetobacter baumannii

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