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  1. Article ; Online: Acinetobacter Metabolism in Infection and Antimicrobial Resistance.

    Ren, Xiaomei / Palmer, Lauren D

    Infection and immunity

    2023  Volume 91, Issue 6, Page(s) e0043322

    Abstract: Acinetobacter infections have high rates of mortality due to an increasing incidence of infections by multidrug-resistant (MDR) and extensively-drug-resistant (XDR) strains. Therefore, new therapeutic strategies for the treatment of Acinetobacter ... ...

    Abstract Acinetobacter infections have high rates of mortality due to an increasing incidence of infections by multidrug-resistant (MDR) and extensively-drug-resistant (XDR) strains. Therefore, new therapeutic strategies for the treatment of Acinetobacter infections are urgently needed. Acinetobacter spp. are Gram-negative coccobacilli that are obligate aerobes and can utilize a wide variety of carbon sources. Acinetobacter baumannii is the main cause of Acinetobacter infections, and recent work has identified multiple strategies A. baumannii uses to acquire nutrients and replicate in the face of host nutrient restriction. Some host nutrient sources also serve antimicrobial and immunomodulatory functions. Hence, understanding Acinetobacter metabolism during infection may provide new insights into novel infection control measures. In this review, we focus on the role of metabolism during infection and in resistance to antibiotics and other antimicrobial agents and discuss the possibility that metabolism may be exploited to identify novel targets to treat Acinetobacter infections.
    MeSH term(s) Humans ; Anti-Bacterial Agents/pharmacology ; Anti-Bacterial Agents/therapeutic use ; Acinetobacter Infections/drug therapy ; Drug Resistance, Bacterial ; Drug Resistance, Multiple, Bacterial ; Cross Infection ; Acinetobacter baumannii
    Chemical Substances Anti-Bacterial Agents
    Language English
    Publishing date 2023-05-16
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 218698-6
    ISSN 1098-5522 ; 0019-9567
    ISSN (online) 1098-5522
    ISSN 0019-9567
    DOI 10.1128/iai.00433-22
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Genetic synergy between

    Noel, Hannah R / Keerthi, Sowmya / Ren, Xiaomei / Winkelman, Jonathan D / Troutman, Jerry M / Palmer, Lauren D

    mBio

    2024  Volume 15, Issue 3, Page(s) e0280423

    Abstract: Acinetobacter ... ...

    Abstract Acinetobacter baumannii
    MeSH term(s) Animals ; Mice ; Anti-Bacterial Agents/pharmacology ; Acinetobacter baumannii ; Drug Resistance, Bacterial ; Cell Wall ; Drug Resistance, Multiple, Bacterial ; Polyisoprenyl Phosphates
    Chemical Substances Anti-Bacterial Agents ; undecaprenyl phosphate (25126-51-6) ; Polyisoprenyl Phosphates
    Language English
    Publishing date 2024-02-16
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2557172-2
    ISSN 2150-7511 ; 2161-2129
    ISSN (online) 2150-7511
    ISSN 2161-2129
    DOI 10.1128/mbio.02804-23
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Mobile genetic elements in Acinetobacter antibiotic-resistance acquisition and dissemination.

    Noel, Hannah R / Petrey, Jessica R / Palmer, Lauren D

    Annals of the New York Academy of Sciences

    2022  Volume 1518, Issue 1, Page(s) 166–182

    Abstract: Pathogenic Acinetobacter species, most notably Acinetobacter baumannii, are a significant cause of healthcare-associated infections worldwide. Acinetobacter infections are of particular concern to global health due to the high rates of multidrug ... ...

    Abstract Pathogenic Acinetobacter species, most notably Acinetobacter baumannii, are a significant cause of healthcare-associated infections worldwide. Acinetobacter infections are of particular concern to global health due to the high rates of multidrug resistance and extensive drug resistance. Widespread genome sequencing and analysis has determined that bacterial antibiotic resistance is often acquired and disseminated through the movement of mobile genetic elements, including insertion sequences (IS), transposons, integrons, and conjugative plasmids. In Acinetobacter specifically, resistance to carbapenems and cephalosporins is highly correlated with IS, as many ISAba elements encode strong outwardly facing promoters that are required for sufficient expression of β-lactamases to confer clinical resistance. Here, we review the role of mobile genetic elements in antibiotic resistance in Acinetobacter species through the framework of the mechanism of resistance acquisition and with a focus on experimentally validated mechanisms.
    MeSH term(s) Humans ; Anti-Bacterial Agents/pharmacology ; Anti-Bacterial Agents/therapeutic use ; Acinetobacter Infections/drug therapy ; Acinetobacter Infections/genetics ; Acinetobacter Infections/microbiology ; Acinetobacter baumannii/genetics ; Acinetobacter baumannii/metabolism ; beta-Lactamases/genetics ; beta-Lactamases/metabolism ; Integrons/genetics ; Drug Resistance, Bacterial/genetics ; DNA Transposable Elements/genetics ; Microbial Sensitivity Tests
    Chemical Substances Anti-Bacterial Agents ; beta-Lactamases (EC 3.5.2.6) ; DNA Transposable Elements
    Language English
    Publishing date 2022-10-31
    Publishing country United States
    Document type Journal Article ; Review ; Research Support, N.I.H., Extramural
    ZDB-ID 211003-9
    ISSN 1749-6632 ; 0077-8923
    ISSN (online) 1749-6632
    ISSN 0077-8923
    DOI 10.1111/nyas.14918
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Cuts Both Ways: Proteases Modulate Virulence of Enterohemorrhagic

    Palmer, Lauren D / Skaar, Eric P

    mBio

    2019  Volume 10, Issue 1

    Abstract: ... ...

    Abstract Enterohemorrhagic
    MeSH term(s) Enterohemorrhagic Escherichia coli ; Escherichia coli Proteins ; Humans ; Microbiota ; Peptide Hydrolases ; Virulence
    Chemical Substances Escherichia coli Proteins ; Peptide Hydrolases (EC 3.4.-)
    Language English
    Publishing date 2019-02-26
    Publishing country United States
    Document type Journal Article ; Comment
    ZDB-ID 2557172-2
    ISSN 2150-7511 ; 2161-2129
    ISSN (online) 2150-7511
    ISSN 2161-2129
    DOI 10.1128/mBio.00115-19
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article: Genetic synergy in

    Noel, Hannah R / Keerthi, Sowmya / Ren, Xiaomei / Winkelman, Jonathan D / Troutman, Jerry M / Palmer, Lauren D

    bioRxiv : the preprint server for biology

    2023  

    Abstract: Acinetobacter ... ...

    Abstract Acinetobacter baumannii
    Language English
    Publishing date 2023-09-22
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2023.09.22.556980
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: Histidine Utilization Is a Critical Determinant of

    Lonergan, Zachery R / Palmer, Lauren D / Skaar, Eric P

    Infection and immunity

    2020  Volume 88, Issue 7

    Abstract: Acinetobacter ... ...

    Abstract Acinetobacter baumannii
    MeSH term(s) Acinetobacter/physiology ; Acinetobacter Infections/metabolism ; Acinetobacter Infections/microbiology ; Animals ; Bacterial Outer Membrane Proteins/genetics ; Bacterial Outer Membrane Proteins/metabolism ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Disease Susceptibility ; Gene Order ; Histidine/metabolism ; Replicon ; Vertebrates
    Chemical Substances Bacterial Outer Membrane Proteins ; Bacterial Proteins ; Histidine (4QD397987E)
    Language English
    Publishing date 2020-06-22
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 218698-6
    ISSN 1098-5522 ; 0019-9567
    ISSN (online) 1098-5522
    ISSN 0019-9567
    DOI 10.1128/IAI.00118-20
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: Transition Metals and Virulence in Bacteria.

    Palmer, Lauren D / Skaar, Eric P

    Annual review of genetics

    2016  Volume 50, Page(s) 67–91

    Abstract: Transition metals are required trace elements for all forms of life. Due to their unique inorganic and redox properties, transition metals serve as cofactors for enzymes and other proteins. In bacterial pathogenesis, the vertebrate host represents a rich ...

    Abstract Transition metals are required trace elements for all forms of life. Due to their unique inorganic and redox properties, transition metals serve as cofactors for enzymes and other proteins. In bacterial pathogenesis, the vertebrate host represents a rich source of nutrient metals, and bacteria have evolved diverse metal acquisition strategies. Host metal homeostasis changes dramatically in response to bacterial infections, including production of metal sequestering proteins and the bombardment of bacteria with toxic levels of metals. In response, bacteria have evolved systems to subvert metal sequestration and toxicity. The coevolution of hosts and their bacterial pathogens in the battle for metals has uncovered emerging paradigms in social microbiology, rapid evolution, host specificity, and metal homeostasis across domains. This review focuses on recent advances and open questions in our understanding of the complex role of transition metals at the host-pathogen interface.
    MeSH term(s) Animals ; Bacteria/metabolism ; Bacteria/pathogenicity ; Bacterial Infections ; Deficiency Diseases/microbiology ; Diet ; Heme/metabolism ; Host-Pathogen Interactions ; Humans ; Iron/metabolism ; Iron Overload/microbiology ; Metals/metabolism ; Siderophores/metabolism
    Chemical Substances Metals ; Siderophores ; Heme (42VZT0U6YR) ; Iron (E1UOL152H7)
    Language English
    Publishing date 2016-09-07
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 207928-8
    ISSN 1545-2948 ; 0066-4170 ; 0066-4197
    ISSN (online) 1545-2948
    ISSN 0066-4170 ; 0066-4197
    DOI 10.1146/annurev-genet-120215-035146
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 1109: Show issues Location:
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  8. Article ; Online: Gram-negative bacteria act as a reservoir for aminoglycoside antibiotics that interact with host factors to enhance bacterial killing in a mouse model of pneumonia.

    Wijers, Christiaan D M / Pham, Ly / Douglass, Martin V / Skaar, Eric P / Palmer, Lauren D / Noto, Michael J

    FEMS microbes

    2022  Volume 3, Page(s) xtac016

    Abstract: ... In ... ...

    Abstract In vitro
    Language English
    Publishing date 2022-05-13
    Publishing country England
    Document type Journal Article
    ISSN 2633-6685
    ISSN (online) 2633-6685
    DOI 10.1093/femsmc/xtac016
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article: Staphylococcus aureus Glucose-Induced Biofilm Accessory Protein A (GbaA) Is a Monothiol-Dependent Electrophile Sensor

    Ray, Abhinaba / Edmonds, Katherine A / Palmer, Lauren D / Skaar, Eric P / Giedroc, David P

    Biochemistry. 2020 July 22, v. 59, no. 31

    2020  

    Abstract: Staphylococcus aureus is a commensal pathogen that has evolved to protect itself from unfavorable conditions by forming complex community structures termed biofilms. The regulation of the formation of these structures is multifactorial and in S. aureus ... ...

    Abstract Staphylococcus aureus is a commensal pathogen that has evolved to protect itself from unfavorable conditions by forming complex community structures termed biofilms. The regulation of the formation of these structures is multifactorial and in S. aureus involves a number of transcriptional regulators. GbaA (glucose-induced biofilm accessory protein A) is a tetracycline repressor (TetR) family regulator that harbors two conserved Cys residues (C55 and C104) and impacts the regulation of formation of poly-N-acetylglucosamine-based biofilms in many methicillin-resistant S. aureus (MRSA) strains. Here, we show that GbaA-regulated transcription of a divergently transcribed operon in a MRSA strain can be induced by potent electrophiles, N-ethylmaleimide and methylglyoxal. Strikingly, induction of transcription in cells requires C55 or C104, but not both. These findings are consistent with in vitro small-angle X-ray scattering, chemical modification, and DNA operator binding experiments, which reveal that both reduced and intraprotomer (C55–C104) disulfide forms of GbaA have very similar overall structures and each exhibits a high affinity for the DNA operator, while DNA binding is strongly inhibited by derivatization of one or the other Cys residues via formation of a mixed disulfide with bacillithiol disulfide or a monothiol derivatization adduct with NEM. While both Cys residues are reactive toward electrophiles, C104 in the regulatory domain is the more reactive thiolate. These characteristics enhance the inducer specificity of GbaA and would preclude sensing of generalized cellular oxidative stress via disulfide bond formation. The implications of the findings for GbaA function in MRSA strains are discussed.
    Keywords DNA ; Lewis acids ; biofilm ; cells ; community structure ; derivatization ; disulfide bonds ; disulfides ; exhibitions ; methicillin-resistant Staphylococcus aureus ; operon ; oxidative stress ; pathogens ; small-angle X-ray scattering ; strains ; tetracycline ; transcription factors
    Language English
    Dates of publication 2020-0722
    Size p. 2882-2895.
    Publishing place American Chemical Society
    Document type Article
    Note NAL-light
    ZDB-ID 1108-3
    ISSN 1520-4995 ; 0006-2960
    ISSN (online) 1520-4995
    ISSN 0006-2960
    DOI 10.1021/acs.biochem.0c00347
    Database NAL-Catalogue (AGRICOLA)

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  10. Article ; Online: Staphylococcus aureus

    Ray, Abhinaba / Edmonds, Katherine A / Palmer, Lauren D / Skaar, Eric P / Giedroc, David P

    Biochemistry

    2020  Volume 59, Issue 31, Page(s) 2882–2895

    Abstract: Staphylococcus ... ...

    Abstract Staphylococcus aureus
    MeSH term(s) Amino Acid Sequence ; Bacterial Proteins/chemistry ; Bacterial Proteins/metabolism ; Biofilms ; Fluorescence Polarization ; Models, Molecular ; Operon/genetics ; Protein Conformation ; Staphylococcus aureus/genetics ; Staphylococcus aureus/metabolism ; Staphylococcus aureus/physiology ; Sulfhydryl Compounds/metabolism
    Chemical Substances Bacterial Proteins ; Sulfhydryl Compounds
    Language English
    Publishing date 2020-07-29
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 1108-3
    ISSN 1520-4995 ; 0006-2960
    ISSN (online) 1520-4995
    ISSN 0006-2960
    DOI 10.1021/acs.biochem.0c00347
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