Unique Iron Coordination in Iron-chelating Molecule Vibriobactin Helps Vibrio cholerae Evade Mammalian Siderocalin-mediated Immune Response

Li, Ning; Zhang, Conggang; Li, Bingqing; Li, Xiuhua; Huang, Yan; Xu, Sujuan; Gu, Lichuan

doi:10.1074/jbc.m111.316034

Cited by 34 publications

(38 citation statements)

References 36 publications

(18 reference statements)

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…In addition, a comparison of secondary structure element positions for the apo and holo forms of ViuP with FepB reveal a match of 85 and 80% (86), respectively, despite the poorly defined ␤-sheets in FepB. The crystal structures for ViuP were only recently reported (54), and this PBP binds the catecholate-type siderophore ferric vibriobactin (FeVib; [Fe III (Vib)] 2Ϫ ). FeVib has a 2-charge and coordinates iron with five ligands from its catecholate groups, whereas FeEnt has a 3-charge and provides six hard ligands to Fe 3ϩ (87).…”

Section: Discussionmentioning

confidence: 99%

The Solution Structure, Binding Properties, and Dynamics of the Bacterial Siderophore-binding Protein FepB

Chu

Otten

Krewulak

et al. 2014

Journal of Biological Chemistry

View full text Add to dashboard Cite

Background: FepB is a periplasmic binding protein that transports the catecholate siderophore enterobactin. Results: The solution NMR structures of apo-and holo-FepB were solved revealing a unique siderophore binding mechanism. Conclusion: Enterobactin binding involves the ordering of dynamic loop residues. Significance: The binding of enterobactin by FepB does not proceed by the typical Venus flytrap scheme.

show abstract

Section: Discussionmentioning

confidence: 99%

The Solution Structure, Binding Properties, and Dynamics of the Bacterial Siderophore-binding Protein FepB

Chu

Otten

Krewulak

et al. 2014

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…V. cholerae produces a unique catechol siderophore called vibriobactin from dihydroxybenzoate, threonine, and norspermidine via the VibBDEFH system (118–120). Ferric vibriobactin is recognized by the outer membrane protein ViuA and its movement across the outer membrane is facilitated by both of V. cholerae ’s TonB-ExbBD complexes, which harness the proton motive force to power the import of substrates (121, 122).…”

Section: Mechanisms Of Environmental Survival and Factors Influencingmentioning

confidence: 99%

Staying Alive: Vibrio cholerae ’s Cycle of Environmental Survival, Transmission, and Dissemination

et al. 2016

View full text Add to dashboard Cite

Infectious diseases kill nearly 9 million people annually. Bacterial pathogens are responsible for a large proportion of these diseases and the bacterial agents of pneumonia, diarrhea, and tuberculosis are leading causes of death and disability worldwide (1). Increasingly, the crucial role of non-host environments in the life cycle of bacterial pathogens is being recognized. Heightened scrutiny has been given to the biological processes impacting pathogen dissemination and survival in the natural environment, as these processes are essential for the transmission of pathogenic bacteria to new hosts. This chapter focuses on the model environmental pathogen, Vibrio cholerae, to describe recent advances in our understanding of how pathogens survive between hosts and highlight the processes necessary to support the cycle of environmental survival, transmission, and dissemination. We describe the physiological and molecular responses of V. cholerae to changing environmental conditions, focusing on its survival in aquatic reservoirs between hosts and its entry and exit from human hosts.

show abstract

“…Some SBPs have been cocrystallized with Fe-siderophores. It is known that several SBPs in Gram-positive bacteria and periplasmic SBPs in Gram-negative bacteria, such as B. subtilis FeuA, S. aureus HtsA, and Vibrio cholerae ViuP recognize oxygen atoms that coordinate with iron, and the siderophores seem to nearly fill the binding pocket (21,22,30). It is possible that apo-siderophores also fill the binding pocket.…”

Section: μM Dfomentioning

confidence: 99%

Gram-positive siderophore-shuttle with iron-exchange from Fe-siderophore to apo-siderophore by Bacillus cereus YxeB

Fukushima

Allred

Sia

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

Small molecule iron-chelators, siderophores, are very important in facilitating the acquisition of Fe(III), an essential element for pathogenic bacteria. Many Gram-negative outer-membrane transporters and Gram-positive lipoprotein siderophore-binding proteins have been characterized, and the binding ability of outer-membrane transporters and siderophore-binding proteins for Fe-siderophores has been determined. However, there is little information regarding the binding ability of these proteins for apo-siderophores, the ironfree chelators. Here we report that Bacillus cereus YxeB facilitates iron-exchange from Fe-siderophore to apo-siderophore bound to the protein, the first Gram-positive siderophore-shuttle system. YxeB binds ferrioxamine B (FO, Fe-siderophore)/desferrioxamine B (DFO, apo-siderophore) in vitro. Disc-diffusion assays and growth assays using the yxeB mutant reveal that YxeB is responsible for importing the FO. Cr-DFO (a FO analog) is bound by YxeB in vitro and B. cereus imports or binds Cr-DFO in vivo. In vivo uptake assays using Cr-DFO and FO and growth assays using DFO and Cr-DFO show that B. cereus selectively imports and uses FO when DFO is present. Moreover, in vitro competition assays using Cr-DFO and FO clearly demonstrate that YxeB binds only FO, not Cr-DFO, when DFO is bound to the protein. Iron-exchange from FO to DFO bound to YxeB must occur when DFO is initially bound by YxeB. Because the metal exchange rate is generally first order in replacement ligand concentration, protein binding of the apo-siderophore acts to dramatically enhance the iron exchange rate, a key component of the Gram-positive siderophore-shuttle mechanism.

show abstract

Unique Iron Coordination in Iron-chelating Molecule Vibriobactin Helps Vibrio cholerae Evade Mammalian Siderocalin-mediated Immune Response

Cited by 34 publications

References 36 publications

The Solution Structure, Binding Properties, and Dynamics of the Bacterial Siderophore-binding Protein FepB

The Solution Structure, Binding Properties, and Dynamics of the Bacterial Siderophore-binding Protein FepB

Staying Alive: Vibrio cholerae ’s Cycle of Environmental Survival, Transmission, and Dissemination

Gram-positive siderophore-shuttle with iron-exchange from Fe-siderophore to apo-siderophore by Bacillus cereus YxeB

Contact Info

Product

Resources

About