scholarly journals Iron-Utilization System in Vibrio vulnificus M2799

Marine Drugs ◽  
2021 ◽  
Vol 19 (12) ◽  
pp. 710
Author(s):  
Katsushiro Miyamoto ◽  
Hiroaki Kawano ◽  
Naoko Okai ◽  
Takeshi Hiromoto ◽  
Nao Miyano ◽  
...  
Keyword(s):  
Outer Membrane ◽  
Vibrio Vulnificus ◽  
Binding Protein ◽  
Membrane Receptors ◽  
Outer Membrane Receptor ◽  
Ferric Ions ◽  
Periplasmic Binding Protein ◽  
Serious Infections ◽  
Periplasmic Binding Proteins ◽  
Export System

Vibrio vulnificus is a Gram-negative pathogenic bacterium that causes serious infections in humans and requires iron for growth. A clinical isolate, V. vulnificus M2799, secretes a catecholate siderophore, vulnibactin, that captures ferric ions from the environment. In the ferric-utilization system in V. vulnificus M2799, an isochorismate synthase (ICS) and an outer membrane receptor, VuuA, are required under low-iron conditions, but alternative proteins FatB and VuuB can function as a periplasmic-binding protein and a ferric-chelate reductase, respectively. The vulnibactin-export system is assembled from TolCV1 and several RND proteins, including VV1_1681. In heme acquisition, HupA and HvtA serve as specific outer membrane receptors and HupB is a sole periplasmic-binding protein, unlike FatB in the ferric-vulnibactin utilization system. We propose that ferric-siderophore periplasmic-binding proteins and ferric-chelate reductases are potential targets for drug discovery in infectious diseases.

TonB or not TonB: is that the question?This paper is one of a selection of papers published in a Special Issue entitled CSBMCB 53rd Annual Meeting — Membrane Proteins in Health and Disease, and has undergone the Journal’s usual peer review process.

2011 ◽  
Vol 89 (2) ◽  
pp. 87-97 ◽  
Author(s):  
Karla D. Krewulak ◽  
Hans J. Vogel
Keyword(s):  
Outer Membrane ◽  
Metal Ion ◽  
Peer Review Process ◽  
Three Dimensional ◽  
Membrane Receptor ◽  
Membrane Receptors ◽  
Dimensional Structure ◽  
Outer Membrane Receptor ◽  
Different Strains ◽  
Low Molecular Weight Iron

Bacteria are able to survive in low-iron environments by sequestering this metal ion from iron-containing proteins and other biomolecules such as transferrin, lactoferrin, heme, hemoglobin, or other heme-containing proteins. In addition, many bacteria secrete specific low molecular weight iron chelators termed siderophores. These iron sources are transported into the Gram-negative bacterial cell through an outer membrane receptor, a periplasmic binding protein (PBP), and an inner membrane ATP-binding cassette (ABC) transporter. In different strains the outer membrane receptors can bind and transport ferric siderophores, heme, or Fe3+ as well as vitamin B12, nickel complexes, and carbohydrates. The energy that is required for the active transport of these substrates through the outer membrane receptor is provided by the TonB/ExbB/ExbD complex, which is located in the cytoplasmic membrane. In this minireview, we will briefly examine the three-dimensional structure of TonB and the current models for the mechanism of TonB-dependent energy transduction. Additionally, the role of TonB in colicin transport will be discussed.

scholarly journals Gonococcal transferrin-binding protein 1 is required for transferrin utilization and is homologous to TonB-dependent outer membrane receptors.

1992 ◽  
Vol 174 (18) ◽  
pp. 5788-5797 ◽  
Author(s):  
C N Cornelissen ◽  
G D Biswas ◽  
J Tsai ◽  
D K Paruchuri ◽  
S A Thompson ◽  
...  
Keyword(s):  
Outer Membrane ◽  
Binding Protein ◽  
Membrane Receptors

scholarly journals TonB Interacts with Nonreceptor Proteins in the Outer Membrane of Escherichia coli

2002 ◽  
Vol 184 (6) ◽  
pp. 1640-1648 ◽  
Author(s):  
Penelope I. Higgs ◽  
Tracy E. Letain ◽  
Kelley K. Merriam ◽  
Neal S. Burke ◽  
HaJeung Park ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Outer Membrane ◽  
Cytoplasmic Membrane ◽  
Outer Membrane Proteins ◽  
Membrane Receptors ◽  
Strong Interactions ◽  
Cross Linking ◽  
Outer Membrane Receptor ◽  
Outer Membranes

ABSTRACT The Escherichia coli TonB protein serves to couple the cytoplasmic membrane proton motive force to active transport of iron-siderophore complexes and vitamin B12 across the outer membrane. Consistent with this role, TonB has been demonstrated to participate in strong interactions with both the cytoplasmic and outer membranes. The cytoplasmic membrane determinants for that interaction have been previously characterized in some detail. Here we begin to examine the nature of TonB interactions with the outer membrane. Although the presence of the siderophore enterochelin (also known as enterobactin) greatly enhanced detectable cross-linking between TonB and the outer membrane receptor, FepA, the absence of enterochelin did not prevent the localization of TonB to the outer membrane. Furthermore, the absence of FepA or indeed of all the iron-responsive outer membrane receptors did not alter this association of TonB with the outer membrane. This suggested that TonB interactions with the outer membrane were not limited to the TonB-dependent outer membrane receptors. Hydrolysis of the murein layer with lysozyme did not alter the distribution of TonB, suggesting that peptidoglycan was not responsible for the outer membrane association of TonB. Conversely, the interaction of TonB with the outer membrane was disrupted by the addition of 4 M NaCl, suggesting that these interactions were proteinaceous. Subsequently, two additional contacts of TonB with the outer membrane proteins Lpp and, putatively, OmpA were identified by in vivo cross-linking. These contacts corresponded to the 43-kDa and part of the 77-kDa TonB-specific complexes described previously. Surprisingly, mutations in these proteins individually did not appear to affect TonB phenotypes. These results suggest that there may be multiple redundant sites where TonB can interact with the outer membrane prior to transducing energy to the outer membrane receptors.

scholarly journals Activities of the Serratia marcescens Heme Receptor HasR and Isolated Plug and β-Barrel Domains: the β-Barrel Forms a Heme-Specific Channel

2005 ◽  
Vol 187 (13) ◽  
pp. 4637-4645 ◽  
Author(s):  
Sylvie Létoffé ◽  
Karine Wecker ◽  
Muriel Delepierre ◽  
Philippe Delepelaire ◽  
Cécile Wandersman
Keyword(s):  
Serratia Marcescens ◽  
Outer Membrane ◽  
Three Dimensional ◽  
Membrane Receptors ◽  
Outer Membrane Receptor ◽  
Heme Uptake ◽  
Amino Terminal ◽  
Exogenous Compounds

ABSTRACT The Serratia marcescens hemophore-specific outer membrane receptor HasR is a member of the TonB-dependent family of autoregulated receptors. It can transport either heme itself or heme bound to the hemophore HasA. On the basis of sequence and functional similarities with other TonB-dependent outer membrane receptors whose three-dimensional structures have been determined, a HasR structure model was proposed. The mature HasR protein comprises a 99-residue amino-terminal extension necessary for hasR transcription, followed by a plug domain of 139 amino acids and a β-barrel domain inserted in the outer membrane, the lumen of which is closed by the plug. This model was used to generate hasR deletions encoding HasR proteins with the native signal peptides but lacking either the N-terminal regulatory extension or encoding the plug or the β-barrel alone. The protein lacking the N-terminal extension, HasR Δ11-91, was incorporated in the outer membrane and was fully functional for active uptake of free and hemophore-bound heme. The HasR β-barrel, Δ11-192, was also incorporated in the outer membrane and bound the hemophore but expressed no active heme transport properties. The HasR plug remained in the periplasm. Coexpression of the plug and the β-barrel allowed partial plug insertion in the outer membrane, demonstrating that these two HasR domains interact in vivo. The β-barrel and the plug also interact in vitro. Nevertheless, the two domains did not complement each other to reconstitute an active TonB-dependent receptor for free or hemophore-bound heme uptake. Production of the β-barrel alone selectively increased passive diffusion of heme but not of other exogenous compounds. A mutation at histidine 603, which is required for heme uptake through the wild-type receptor, abolished heme diffusion, showing that HasR Δ11-192 forms a specific heme channel.

scholarly journals A New Class of Cobalamin Transport Mutants (btuF) Provides Genetic Evidence for a Periplasmic Binding Protein in Salmonella typhimurium

1999 ◽  
Vol 181 (17) ◽  
pp. 5539-5541 ◽  
Author(s):  
Michael Van Bibber ◽  
Clive Bradbeer ◽  
Nica Clark ◽  
John R. Roth
Keyword(s):  
Salmonella Typhimurium ◽  
Membrane Transport ◽  
Abc Transporters ◽  
Signal Sequence ◽  
Binding Protein ◽  
Periplasmic Binding Protein ◽  
New Class ◽  
Periplasmic Binding Proteins ◽  
Transport Mutants ◽  
New Mutations

ABSTRACT No periplasmic binding protein has been demonstrated for the ATP-binding cassette (ABC)-type cobalamin transporter BtuCD. New mutations (btuF) are described that affect inner-membrane transport. The BtuF protein has a signal sequence and resembles the periplasmic binding proteins of several other ABC transporters.

The role of vicinal tyrosine residues in the function of Haemophilus influenzae ferric-binding protein A

2010 ◽  
Vol 432 (1) ◽  
pp. 57-67 ◽  
Author(s):  
Husain K. Khambati ◽  
Trevor F. Moraes ◽  
Jagroop Singh ◽  
Stephen R. Shouldice ◽  
Rong-hua Yu ◽  
...  
Keyword(s):  
Haemophilus Influenzae ◽  
Outer Membrane ◽  
Binding Protein ◽  
Protein A ◽  
Membrane Receptor ◽  
Receptor Complex ◽  
Iron Binding ◽  
Outer Membrane Receptor ◽  
Tyrosine Residues ◽  
Ferric Binding Protein

The periplasmic FbpA (ferric-binding protein A) from Haemophilus influenzae plays a critical role in acquiring iron from host transferrin, shuttling iron from the outer-membrane receptor complex to the inner-membrane transport complex responsible for transporting iron into the cytoplasm. In the present study, we report on the properties of a series of site-directed mutants of two adjacent tyrosine residues involved in iron co-ordination, and demonstrate that, in contrast with mutation of equivalent residues in the N-lobe of human transferrin, the mutant FbpAs retain significant iron-binding affinity regardless of the nature of the replacement amino acid. The Y195A and Y196A FbpAs are not only capable of binding iron, but are proficient in mediating periplasm-to-cytoplasm iron transport in a reconstituted FbpABC pathway in a specialized Escherichia coli reporter strain. This indicates that their inability to mediate iron acquisition from transferrin is due to their inability to compete for iron with receptor-bound transferrin. Wild-type iron-loaded FbpA could be crystalized in a closed or open state depending upon the crystallization conditions. The synergistic phosphate anion was not present in the iron-loaded open form, suggesting that initial anchoring of iron was mediated by the adjacent tyrosine residues and that alternate pathways for iron and anion binding and release may be considered. Collectively, these results demonstrate that the presence of a twin-tyrosine motif common to many periplasmic iron-binding proteins is critical for initially capturing the ferric ion released by the outer-membrane receptor complex.

scholarly journals Free and Hemophore-Bound Heme Acquisitions through the Outer Membrane Receptor HasR Have Different Requirements for the TonB-ExbB-ExbD Complex

2004 ◽  
Vol 186 (13) ◽  
pp. 4067-4074 ◽  
Author(s):  
Sylvie Létoffé ◽  
Philippe Delepelaire ◽  
Cécile Wandersman
Keyword(s):  
Outer Membrane ◽  
Energy Requirement ◽  
Membrane Receptor ◽  
Membrane Receptors ◽  
Gram Negative Bacteria ◽  
Outer Membrane Receptor ◽  
Heme Uptake ◽  
Heme Transport ◽  
Carbonyl Cyanide ◽  
Free Heme

ABSTRACT Many gram-negative bacteria have specific outer membrane receptors for free heme, hemoproteins, and hemophores. Heme is a major iron source and is taken up intact, whereas hemoproteins and hemophores are not transported: the iron-containing molecule has to be stripped off at the cell surface, with only the heme moiety being taken up. The Serratia marcescens hemophore-specific outer membrane receptor HasR can transport either heme itself or heme bound to the hemophore HasA. This second mechanism is much more efficient and requires a higher TonB-ExbB-ExbD (TonB complex) concentration than does free or hemoglobin-bound heme uptake. This requirement for more of the TonB complex is associated with a higher energy requirement. Indeed, the sensitivity of heme-hemophore uptake to the protonophore carbonyl cyanide m-chlorophenyl hydrazone is higher than that of heme uptake from hemoglobin. We show that a higher TonB complex concentration is required for hemophore dissociation from the receptor. This dissociation is concomitant with heme uptake. We propose that increasing the TonB complex concentration drives more energy to the outer membrane receptor and speeds up the release of empty hemophores, which, if they remained on receptors, would inhibit heme transport.

scholarly journals Cloning and Characterization of vuuA, a Gene Encoding the Vibrio vulnificus Ferric Vulnibactin Receptor

2000 ◽  
Vol 68 (2) ◽  
pp. 526-534 ◽  
Author(s):  
Athena C. D. Webster ◽  
Christine M. Litwin
Keyword(s):  
Transcriptional Regulation ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Outer Membrane ◽  
Dna Sequence ◽  
Vibrio Vulnificus ◽  
Membrane Receptors ◽  
Gene Encoding ◽  
Infant Mouse

ABSTRACT The ability of Vibrio vulnificus to acquire iron from the host has been shown to correlate with virulence. Many iron transport genes are regulated by iron, and in V. vulnificus, transcriptional regulation by iron depends on thefur gene. The N-terminal amino acid sequence of a 72-kDa iron-regulated outer membrane protein purified from a V. vulnificus fur mutant had 53% homology with the first 15 amino acids of the mature protein of the Vibrio choleraevibriobactin receptor, ViuA. In this report, we describe the cloning, DNA sequence, mutagenesis, and analysis of transcriptional regulation of the structural gene for VuuA, the vulnibactin receptor of V. vulnificus. Analysis of the DNA sequence of the vuuApromoter region demonstrated a sequence identical to the upstream Fur box of V. cholerae viuA. Northern blot analysis showed that the transcript was strongly regulated by iron. The amino acid sequence of VuuA was 74% identical to the sequence of V. choleraeViuA and was homologous to those of several TonB-dependent outer membrane receptors. An internal deletion of the V. vulnificus vuuA gene resulted in the loss of expression of the 72-kDa protein and the loss of the ability to use transferrin or vulnibactin as a source of iron. This mutant showed reduced virulence in an infant mouse model. Introduction of a plasmid containing the completeviuA coding sequence and 342 bp of upstream DNA into the mutant restored ferric vulnibactin and ferric transferrin utilization to the mutant.

scholarly journals Expression, purification, crystallization and X-ray crystallographic analysis of the periplasmic binding protein VatD fromVibrio vulnificusM2799

2015 ◽  
Vol 71 (8) ◽  
pp. 1078-1082
Author(s):  
Nao Miyano ◽  
Tomoko Igarashi ◽  
Hiroaki Kawano ◽  
Katsushiro Miyamoto ◽  
Takahiro Tsuchiya ◽  
...  
Keyword(s):  
Vibrio Vulnificus ◽  
Binding Protein ◽  
Crystallographic Analysis ◽  
Marine Microorganism ◽  
Periplasmic Binding Protein ◽  
Crystal Forms ◽  
Space Group ◽  
X Ray ◽  
Desferrioxamine B ◽  
The Difference

Vibrio vulnificusis a halophilic marine microorganism which causes gastroenteritis and primary septicaemia in humans. An important factor that determines the survival ofV. vulnificusin the human body is its ability to acquire iron. VatD is a periplasmic siderophore-binding protein fromV. vulnificusM2799. The current study reports the expression, purification and crystallization of VatD. Crystals of both apo VatD and a VatD–desferrioxamine B–Fe3+(VatD–FOB) complex were obtained. The crystal of apo VatD belonged to space groupP6422, while the crystal of the VatD–FOB complex belonged to space groupP21. The difference in the two crystal forms could be caused by the binding of FOB to VatD.

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