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Article ; Online: Correction for Banerjee et al., "

Banerjee, Dithi / Umland, Timothy C / Panepinto, John C

mSphere

2023 Volume 8, Issue 5, Page(s) e0040623

Language	English
Publishing date	2023-09-26
Publishing country	United States
Document type	Journal Article ; Published Erratum
ISSN	2379-5042
ISSN (online)	2379-5042
DOI	10.1128/msphere.00406-23
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Article: De Novo

Banerjee, Dithi / Umland, Timothy C / Panepinto, John C

mSphere

2016 Volume 1, Issue 6

Abstract: The use of amphotericin B (AmB) in conjunction with 5-fluorocytosine (5-FC) is known to be the optimal therapy for treating cryptococcosis, but the mechanism by which 5-FC synergizes with AmB is unknown. In this study, we generated ... ...

Abstract	The use of amphotericin B (AmB) in conjunction with 5-fluorocytosine (5-FC) is known to be the optimal therapy for treating cryptococcosis, but the mechanism by which 5-FC synergizes with AmB is unknown. In this study, we generated a
Language	English
Publishing date	2016-11-16
Publishing country	United States
Document type	Journal Article
ISSN	2379-5042
ISSN	2379-5042
DOI	10.1128/mSphere.00191-16
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Article ; Online: Re-evaluating the approach to drug target discovery in multidrug-resistant Gram-negative bacilli.

Umland, Timothy C / Schultz, L Wayne / Russo, Thomas A

Future microbiology

2014 Volume 9, Issue 10, Page(s) 1113–1116

MeSH term(s)	Anti-Infective Agents/isolation & purification ; Anti-Infective Agents/pharmacology ; Drug Discovery/methods ; Drug Discovery/trends ; Drug Resistance, Multiple, Bacterial ; Genes, Bacterial ; Genes, Essential ; Gram-Negative Bacteria/drug effects
Chemical Substances	Anti-Infective Agents
Language	English
Publishing date	2014
Publishing country	England
Document type	Editorial ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ISSN	1746-0921
ISSN (online)	1746-0921
DOI	10.2217/fmb.14.72
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Article ; Online: Repurposed dihydroorotate dehydrogenase inhibitors with efficacy against drug-resistant

Russo, Thomas A / Umland, Timothy C / Deng, Xiaoyi / El Mazouni, Farah / Kokkonda, Sreekanth / Olson, Ruth / Carlino-MacDonald, Ulrike / Beanan, Janet / Alvarado, Cassandra L / Tomchick, Diana R / Hutson, Alan / Chen, Hong / Posner, Bruce / Rathod, Pradipsinh K / Charman, Susan A / Phillips, Margaret A

Proceedings of the National Academy of Sciences of the United States of America

2022 Volume 119, Issue 51, Page(s) e2213116119

Abstract: New antimicrobials are needed for the treatment of extensively drug- ... ...

Abstract	New antimicrobials are needed for the treatment of extensively drug-resistant
MeSH term(s)	Humans ; Mice ; Animals ; Acinetobacter baumannii ; Dihydroorotate Dehydrogenase ; Microbial Sensitivity Tests ; Meropenem ; Enzyme Inhibitors/pharmacology ; Enzyme Inhibitors/chemistry ; Anti-Bacterial Agents/pharmacology ; Anti-Bacterial Agents/therapeutic use
Chemical Substances	Dihydroorotate Dehydrogenase ; Meropenem (FV9J3JU8B1) ; Enzyme Inhibitors ; Anti-Bacterial Agents
Language	English
Publishing date	2022-12-13
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.2213116119
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Article ; Online: Influenza A polymerase subunit PB2 possesses overlapping binding sites for polymerase subunit PB1 and human MAVS proteins.

Patel, Deendayal / Schultz, L Wayne / Umland, Timothy C

Virus research

2012 Volume 172, Issue 1-2, Page(s) 75–80

Abstract: Influenza A virus is an important human pathogen accounting for widespread morbidity and mortality, with new strains emerging from animal reservoirs possessing the potential to cause pandemics. The influenza A RNA-dependent RNA polymerase complex ... ...

Abstract	Influenza A virus is an important human pathogen accounting for widespread morbidity and mortality, with new strains emerging from animal reservoirs possessing the potential to cause pandemics. The influenza A RNA-dependent RNA polymerase complex consists of three subunits (PA, PB1, and PB2) and catalyzes viral RNA replication and transcription activities in the nuclei of infected host cells. The PB2 subunit has been implicated in pathogenicity and host adaptation. This includes the inhibition of type I interferon induction through interaction with the host's mitochondrial antiviral signaling protein (MAVS), an adaptor molecule of RIG-I-like helicases. This study reports the identification of the cognate PB2 and MAVS interaction domains necessary for complex formation. Specifically, MAVS residues 1-150, containing both the CARD domain and the N-terminal portion of the proline rich-region, and PB2 residues 1-37 are essential for PB2-MAVS virus-host protein-protein complex formation. The three α-helices constituting PB2 (1-37) were tested to determine their relative influence in complex formation, and Helix3 was observed to promote the primary interaction with MAVS. The PB2 MAVS-binding domain unexpectedly coincided with its PB1-binding domain, indicating an important dual functionality for this region of PB2. Analysis of these interaction domains suggests both virus and host properties that may contribute to host tropism. Additionally, the results of this study suggest a new strategy to develop influenza A therapeutics by simultaneously blocking PB2-MAVS and PB2-PB1 protein-protein interactions and their resulting activities.
MeSH term(s)	Adaptor Proteins, Signal Transducing/metabolism ; Binding Sites ; Cell Line ; Humans ; Influenza A Virus, H1N1 Subtype/physiology ; Protein Binding ; Protein Interaction Domains and Motifs ; Protein Interaction Mapping ; RNA Replicase/metabolism ; Viral Proteins/metabolism
Chemical Substances	Adaptor Proteins, Signal Transducing ; MAVS protein, human ; PB2 protein, Influenzavirus A ; Viral Proteins ; influenza virus polymerase basic protein 1 ; RNA Replicase (EC 2.7.7.48)
Language	English
Publishing date	2012-12-12
Publishing country	Netherlands
Document type	Journal Article ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	605780-9
ISSN	1872-7492 ; 0168-1702
ISSN (online)	1872-7492
ISSN	0168-1702
DOI	10.1016/j.virusres.2012.12.003
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Article ; Online: Crystal structure of 5-enolpyruvylshikimate-3-phosphate (EPSP) synthase from the ESKAPE pathogen Acinetobacter baumannii.

Sutton, Kristin A / Breen, Jennifer / Russo, Thomas A / Schultz, L Wayne / Umland, Timothy C

Acta crystallographica. Section F, Structural biology communications

2016 Volume 72, Issue Pt 3, Page(s) 179–187

Abstract: The enzyme 5-enolpyruvylshikimate-3-phosphate (EPSP) synthase catalyzes the sixth step of the seven-step shikimate pathway. Chorismate, the product of the pathway, is a precursor for the biosynthesis of aromatic amino acids, siderophores and metabolites ... ...

Abstract	The enzyme 5-enolpyruvylshikimate-3-phosphate (EPSP) synthase catalyzes the sixth step of the seven-step shikimate pathway. Chorismate, the product of the pathway, is a precursor for the biosynthesis of aromatic amino acids, siderophores and metabolites such as folate, ubiquinone and vitamin K. The shikimate pathway is present in bacteria, fungi, algae, plants and apicomplexan parasites, but is absent in humans. The EPSP synthase enzyme produces 5-enolpyruvylshikimate 3-phosphate and phosphate from phosphoenolpyruvate and shikimate 3-phosphate via a transferase reaction, and is the target of the herbicide glyphosate. The Acinetobacter baumannii gene encoding EPSP synthase, aroA, has previously been demonstrated to be essential during host infection for the growth and survival of this clinically important drug-resistant ESKAPE pathogen. Prephenate dehydrogenase is also encoded by the bifunctional A. baumannii aroA gene, but its activity is dependent upon EPSP synthase since it operates downstream of the shikimate pathway. As part of an effort to evaluate new antimicrobial targets, recombinant A. baumannii EPSP (AbEPSP) synthase, comprising residues Ala301-Gln756 of the aroA gene product, was overexpressed in Escherichia coli, purified and crystallized. The crystal structure, determined to 2.37 Å resolution, is described in the context of a potential antimicrobial target and in comparison to EPSP synthases that are resistant or sensitive to the herbicide glyphosate.
MeSH term(s)	3-Phosphoshikimate 1-Carboxyvinyltransferase/chemistry ; Acinetobacter baumannii/enzymology ; Amino Acid Sequence ; Bacterial Proteins/chemistry ; Catalytic Domain ; Crystallization ; Crystallography, X-Ray ; Models, Molecular ; Protein Conformation, alpha-Helical ; Shikimic Acid/analogs & derivatives ; Shikimic Acid/chemistry
Chemical Substances	Bacterial Proteins ; Shikimic Acid (29MS2WI2NU) ; shikimic acid-3-phosphate (63959-45-5) ; 3-Phosphoshikimate 1-Carboxyvinyltransferase (EC 2.5.1.19)
Language	English
Publishing date	2016-02-16
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ISSN	2053-230X
ISSN (online)	2053-230X
DOI	10.1107/S2053230X16001114
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Article: The Response Regulator BfmR Is a Potential Drug Target for Acinetobacter baumannii.

Russo, Thomas A / Manohar, Akshay / Beanan, Janet M / Olson, Ruth / MacDonald, Ulrike / Graham, Jessica / Umland, Timothy C

mSphere

2016 Volume 1, Issue 3

Abstract: Identification and validation is the first phase of target-based antimicrobial development. BfmR (RstA), a response regulator in a two-component signal transduction system (TCS) in Acinetobacter baumannii, is an intriguing potential antimicrobial target. ...

Abstract	Identification and validation is the first phase of target-based antimicrobial development. BfmR (RstA), a response regulator in a two-component signal transduction system (TCS) in Acinetobacter baumannii, is an intriguing potential antimicrobial target. A unique characteristic of BfmR is that its inhibition would have the dual benefit of significantly decreasing in vivo survival and increasing sensitivity to selected antimicrobials. Studies on the clinically relevant strain AB307-0294 have shown BfmR to be essential in vivo. Here, we demonstrate that this phenotype in strains AB307-0294 and AB908 is mediated, in part, by enabling growth in human ascites fluid and serum. Further, BfmR conferred resistance to complement-mediated bactericidal activity that was independent of capsular polysaccharide. Importantly, BfmR also increased resistance to the clinically important antimicrobials meropenem and colistin. BfmR was highly conserved among A. baumannii strains. The crystal structure of the receiver domain of BfmR was determined, lending insight into putative ligand binding sites. This enabled an in silico ligand binding analysis and a blind docking strategy to assess use as a potential druggable target. Predicted binding hot spots exist at the homodimer interface and the phosphorylation site. These data support pursuing the next step in the development process, which includes determining the degree of inhibition needed to impact growth/survival and the development a BfmR activity assay amenable to high-throughput screening for the identification of inhibitors. Such agents would represent a new class of antimicrobials active against A. baumannii which could be active against other Gram-negative bacilli that possess a TCS with shared homology. IMPORTANCE Increasing antibiotic resistance in bacteria, particularly Gram-negative bacilli, has significantly affected the ability of physicians to treat infections, with resultant increased morbidity, mortality, and health care costs. In fact, some strains of bacteria are resistant to all available antibiotics, such as Acinetobacter baumannii, which is the focus of this report. Therefore, the development of new antibiotics active against these resistant strains is urgently needed. In this study, BfmR is further validated as an intriguing target for a novel class of antibiotics. Successful inactivation of BfmR would confer the multiple benefits of a decreased ability of A. baumannii to survive in human body fluids, increased sensitivity to complement-mediated bactericidal activity and, importantly, increased sensitivity to other antibiotics. Structural studies support the potential for this "druggable" target, as they identify the potential for small-molecule binding at functionally relevant sites. Next-phase high-throughput screening studies utilizing BfmR are warranted.
Language	English
Publishing date	2016-05-11
Publishing country	United States
Document type	Journal Article
ISSN	2379-5042
ISSN	2379-5042
DOI	10.1128/mSphere.00082-16
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Article ; Online: The short-chain oxidoreductase Q9HYA2 from Pseudomonas aeruginosa PAO1 contains an atypical catalytic center.

Huether, Robert / Mao, Qilong / Duax, William L / Umland, Timothy C

Protein science : a publication of the Protein Society

2010 Volume 19, Issue 5, Page(s) 1097–1103

Abstract: The characteristic oxidation or reduction reaction mechanisms of short-chain oxidoreductase (SCOR) enzymes involve a highly conserved Asp-Ser-Tyr-Lys catalytic tetrad. The SCOR enzyme Q9HYA2 from the pathogenic bacterium Pseudomonas aeruginosa was ... ...

Abstract	The characteristic oxidation or reduction reaction mechanisms of short-chain oxidoreductase (SCOR) enzymes involve a highly conserved Asp-Ser-Tyr-Lys catalytic tetrad. The SCOR enzyme Q9HYA2 from the pathogenic bacterium Pseudomonas aeruginosa was recognized to possess an atypical catalytic tetrad composed of Lys118-Ser146-Thr159-Arg163. Orthologs of Q9HYA2 containing the unusual catalytic tetrad along with conserved substrate and cofactor recognition residues were identified in 27 additional species, the majority of which are bacterial pathogens. However, this atypical catalytic tetrad was not represented within the Protein Data Bank. The crystal structures of unligated and NADPH-complexed Q9HYA2 were determined at 2.3 A resolution. Structural alignment to a polyketide ketoreductase (KR), a typical SCOR, demonstrated that Q9HYA2's Lys118, Ser146, and Arg163 superimposed upon the KR's catalytic Asp114, Ser144, and Lys161, respectively. However, only the backbone of Q9HYA2's Thr159 overlapped KR's catalytic Tyr157. The Thr159 hydroxyl in apo Q9HYA2 is poorly positioned for participating in catalysis. In the Q9HYA2-NADPH complex, the Thr159 side chain was modeled in two alternate rotamers, one of which is positioned to interact with other members of the tetrad and the bound cofactor. A chloride ion is bound at the position normally occupied by the catalytic tyrosine hydroxyl. The putative active site of Q9HYA2 contains a chemical moiety at each catalytically important position of a typical SCOR enzyme. This is the first observation of a SCOR protein with this alternate catalytic center that includes threonine replacing the catalytic tyrosine and an ion replacing the hydroxyl moiety of the catalytic tyrosine.
MeSH term(s)	Amino Acid Sequence ; Bacterial Proteins/chemistry ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Catalytic Domain ; Conserved Sequence ; Crystallography, X-Ray ; Databases, Protein ; Escherichia coli/genetics ; Models, Molecular ; Molecular Sequence Data ; NADP/chemistry ; NADP/metabolism ; Oxidoreductases/chemistry ; Oxidoreductases/genetics ; Oxidoreductases/metabolism ; Protein Binding ; Pseudomonas aeruginosa/enzymology ; Pseudomonas aeruginosa/genetics ; Sequence Alignment
Chemical Substances	Bacterial Proteins ; NADP (53-59-8) ; Oxidoreductases (EC 1.-)
Language	English
Publishing date	2010-03-27
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	1106283-6
ISSN	1469-896X ; 0961-8368
ISSN (online)	1469-896X
ISSN	0961-8368
DOI	10.1002/pro.384
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Zs.A 3407: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: Crystallization and X-ray diffraction analysis of the beta-ketoacyl-acyl carrier protein reductase FabG from Aquifex aeolicus VF5.

Mao, Qilong / Duax, William L / Umland, Timothy C

Acta crystallographica. Section F, Structural biology and crystallization communications

2007 Volume 63, Issue Pt 2, Page(s) 106–109

Abstract: The gene product of fabG from Aquifex aeolicus has been heterologously expressed in Escherichia coli. Purification of the protein took place using anion-exchange and size-exclusion chromatography and the protein was then crystallized. Diffraction data ... ...

Abstract	The gene product of fabG from Aquifex aeolicus has been heterologously expressed in Escherichia coli. Purification of the protein took place using anion-exchange and size-exclusion chromatography and the protein was then crystallized. Diffraction data were collected to a maximum resolution of 1.8 A and the initial phases were determined by molecular replacement. The A. aeolicus FabG protein is a putative beta-ketoacyl-acyl carrier protein reductase. Structure-function studies of this protein are being performed as part of a larger project investigating naturally occurring deviations from highly conserved residues within the short-chain oxidoreductase (SCOR) family.
MeSH term(s)	Alcohol Oxidoreductases/chemistry ; Alcohol Oxidoreductases/genetics ; Bacteria/enzymology ; Bacteria/genetics ; Bacterial Proteins/chemistry ; Bacterial Proteins/genetics ; Carrier Proteins/chemistry ; Carrier Proteins/genetics ; Cloning, Molecular ; Crystallization ; Crystallography, X-Ray ; Electrophoresis, Polyacrylamide Gel ; Escherichia coli/chemistry ; Escherichia coli/genetics ; Escherichia coli/metabolism
Chemical Substances	Bacterial Proteins ; Carrier Proteins ; Alcohol Oxidoreductases (EC 1.1.-) ; acetoacetyl-CoA reductase (EC 1.1.1.36)
Language	English
Publishing date	2007-01-17
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
ISSN	1744-3091
ISSN (online)	1744-3091
DOI	10.1107/S1744309107000103
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Article ; Online: Structure of shikimate kinase, an in vivo essential metabolic enzyme in the nosocomial pathogen Acinetobacter baumannii, in complex with shikimate.

Sutton, Kristin A / Breen, Jennifer / MacDonald, Ulrike / Beanan, Janet M / Olson, Ruth / Russo, Thomas A / Schultz, L Wayne / Umland, Timothy C

Acta crystallographica. Section D, Biological crystallography

2015 Volume 71, Issue Pt 8, Page(s) 1736–1744

Abstract: Acinetobacter baumannii is an opportunistic Gram-negative pathogen that is an important cause of healthcare-associated infections exhibiting high mortality rates. Clinical isolates of multidrug-resistant (MDR) and extremely drug-resistant (XDR) A. ... ...

Abstract	Acinetobacter baumannii is an opportunistic Gram-negative pathogen that is an important cause of healthcare-associated infections exhibiting high mortality rates. Clinical isolates of multidrug-resistant (MDR) and extremely drug-resistant (XDR) A. baumannii strains are increasingly being observed. Compounding this concern is the dearth of new antibacterial agents in late-stage development that are effective against MDR and XDR A. baumannii. As part of an effort to address these concerns, two genes (aroA and aroC) of the shikimate pathway have previously been determined to be essential for the growth and survival of A. baumannii during host infection (i.e. to be essential in vivo). This study expands upon these results by demonstrating that the A. baumannii aroK gene, encoding shikimate kinase (SK), is also essential in vivo in a rat soft-tissue infection model. The crystal structure of A. baumannii SK in complex with the substrate shikimate and a sulfate ion that mimics the binding interactions expected for the β-phosphate of ATP was then determined to 1.91 Å resolution and the enzyme kinetics were characterized. The flexible shikimate-binding domain and LID region are compared with the analogous regions in other SK crystal structures. The impact of structural differences and sequence divergence between SKs from pathogenic bacteria that may influence antibiotic-development efforts is discussed.
MeSH term(s)	Acinetobacter Infections/metabolism ; Acinetobacter Infections/microbiology ; Acinetobacter baumannii/chemistry ; Acinetobacter baumannii/enzymology ; Acinetobacter baumannii/growth & development ; Acinetobacter baumannii/metabolism ; Animals ; Crystallography, X-Ray ; Humans ; Models, Molecular ; Phosphotransferases (Alcohol Group Acceptor)/chemistry ; Phosphotransferases (Alcohol Group Acceptor)/metabolism ; Protein Conformation ; Rats ; Shikimic Acid/metabolism ; Signal Transduction
Chemical Substances	Shikimic Acid (29MS2WI2NU) ; Phosphotransferases (Alcohol Group Acceptor) (EC 2.7.1.-) ; shikimate kinase (EC 2.7.1.71)
Language	English
Publishing date	2015-08
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	2020492-9
ISSN	1399-0047 ; 2059-7983 ; 0907-4449
ISSN (online)	1399-0047 ; 2059-7983
ISSN	0907-4449
DOI	10.1107/S139900471501189X
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