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  1. Article ; Online: Antibiotic Resistance ABC-F Proteins: Bringing Target Protection into the Limelight.

    Sharkey, Liam K R / O'Neill, Alex J

    ACS infectious diseases

    2018  Volume 4, Issue 3, Page(s) 239–246

    Abstract: Members of the ATP-binding cassette (ABC)-F protein subfamily collectively mediate resistance to a broader range of clinically important antibiotic classes than any other group of resistance proteins and are widespread in pathogenic bacteria. Following ... ...

    Abstract Members of the ATP-binding cassette (ABC)-F protein subfamily collectively mediate resistance to a broader range of clinically important antibiotic classes than any other group of resistance proteins and are widespread in pathogenic bacteria. Following over 25 years' of controversy regarding the mechanism by which these proteins work, it has recently been established that they provide antibiotic resistance through the previously recognized but underappreciated phenomenon of target protection; they bind to the ribosome to effect the release of ribosome-targeted antibiotics, thereby rescuing the translation apparatus from antibiotic-mediated inhibition. Here we review the ABC-F resistance proteins with an emphasis on their mechanism of action, first exploring the history of the debate about how these proteins work and outlining our current state of knowledge and then considering key questions to be addressed in understanding the molecular detail of their function.
    MeSH term(s) ATP-Binding Cassette Transporters/metabolism ; Anti-Bacterial Agents/metabolism ; Bacteria/drug effects ; Bacteria/enzymology ; Drug Resistance, Bacterial ; Protein Biosynthesis ; Ribosomes/metabolism
    Chemical Substances ATP-Binding Cassette Transporters ; Anti-Bacterial Agents
    Language English
    Publishing date 2018-02-07
    Publishing country United States
    Document type Journal Article ; Review
    ISSN 2373-8227
    ISSN (online) 2373-8227
    DOI 10.1021/acsinfecdis.7b00251
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Staphylococcus aureus host interactions and adaptation.

    Howden, Benjamin P / Giulieri, Stefano G / Wong Fok Lung, Tania / Baines, Sarah L / Sharkey, Liam K / Lee, Jean Y H / Hachani, Abderrahman / Monk, Ian R / Stinear, Timothy P

    Nature reviews. Microbiology

    2023  Volume 21, Issue 6, Page(s) 380–395

    Abstract: Invasive Staphylococcus aureus infections are common, causing high mortality, compounded by the propensity of the bacterium to develop drug resistance. S. aureus is an excellent case study of the potential for a bacterium to be commensal, colonizing, ... ...

    Abstract Invasive Staphylococcus aureus infections are common, causing high mortality, compounded by the propensity of the bacterium to develop drug resistance. S. aureus is an excellent case study of the potential for a bacterium to be commensal, colonizing, latent or disease-causing; these states defined by the interplay between S. aureus and host. This interplay is multidimensional and evolving, exemplified by the spread of S. aureus between humans and other animal reservoirs and the lack of success in vaccine development. In this Review, we examine recent advances in understanding the S. aureus-host interactions that lead to infections. We revisit the primary role of neutrophils in controlling infection, summarizing the discovery of new immune evasion molecules and the discovery of new functions ascribed to well-known virulence factors. We explore the intriguing intersection of bacterial and host metabolism, where crosstalk in both directions can influence immune responses and infection outcomes. This Review also assesses the surprising genomic plasticity of S. aureus, its dualism as a multi-mammalian species commensal and opportunistic pathogen and our developing understanding of the roles of other bacteria in shaping S. aureus colonization.
    MeSH term(s) Animals ; Humans ; Staphylococcus aureus/genetics ; Staphylococcal Infections ; Immune Evasion ; Virulence Factors/genetics ; Adaptation, Physiological ; Host-Pathogen Interactions ; Mammals
    Chemical Substances Virulence Factors
    Language English
    Publishing date 2023-01-27
    Publishing country England
    Document type Journal Article ; Review ; Research Support, Non-U.S. Gov't
    ZDB-ID 2139054-X
    ISSN 1740-1534 ; 1740-1526
    ISSN (online) 1740-1534
    ISSN 1740-1526
    DOI 10.1038/s41579-023-00852-y
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Low-Cost, Open-Source Device for High-Performance Fluorescence Detection of Isothermal Nucleic Acid Amplification Reactions.

    Buultjens, Andrew H / Vandelannoote, Koen / Sharkey, Liam K / Howden, Benjamin P / Monk, Ian R / Lee, Jean Y H / Stinear, Timothy P

    ACS biomaterials science & engineering

    2021  Volume 7, Issue 10, Page(s) 4982–4990

    Abstract: The ability to detect SARS-CoV-2 is critical to implementing evidence-based strategies to address the COVID-19 global pandemic. Expanding SARS-CoV-2 diagnostic ability beyond well-equipped laboratories widens the opportunity for surveillance and control ... ...

    Abstract The ability to detect SARS-CoV-2 is critical to implementing evidence-based strategies to address the COVID-19 global pandemic. Expanding SARS-CoV-2 diagnostic ability beyond well-equipped laboratories widens the opportunity for surveillance and control efforts. However, such advances are predicated on the availability of rapid, scalable, accessible, yet high-performance diagnostic platforms. Methods to detect viral RNA using reverse transcription loop-mediated isothermal amplification (RT-LAMP) show promise as rapid and field-deployable tests; however, the per-unit costs of the required diagnostic hardware can be a barrier for scaled deployment. Here, we describe a diagnostic hardware configuration for LAMP technology, named the
    MeSH term(s) COVID-19/diagnosis ; Humans ; Molecular Diagnostic Techniques ; Nucleic Acid Amplification Techniques ; RNA, Viral/genetics ; RNA, Viral/isolation & purification ; SARS-CoV-2
    Chemical Substances RNA, Viral
    Language English
    Publishing date 2021-09-14
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 2373-9878
    ISSN (online) 2373-9878
    DOI 10.1021/acsbiomaterials.1c01105
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: ABC-F Proteins Mediate Antibiotic Resistance through Ribosomal Protection.

    Sharkey, Liam K R / Edwards, Thomas A / O'Neill, Alex J

    mBio

    2016  Volume 7, Issue 2, Page(s) e01975

    Abstract: Members of the ABC-F subfamily of ATP-binding cassette proteins mediate resistance to a broad array of clinically important antibiotic classes that target the ribosome of Gram-positive pathogens. The mechanism by which these proteins act has been a ... ...

    Abstract Members of the ABC-F subfamily of ATP-binding cassette proteins mediate resistance to a broad array of clinically important antibiotic classes that target the ribosome of Gram-positive pathogens. The mechanism by which these proteins act has been a subject of long-standing controversy, with two competing hypotheses each having gained considerable support: antibiotic efflux versus ribosomal protection. Here, we report on studies employing a combination of bacteriological and biochemical techniques to unravel the mechanism of resistance of these proteins, and provide several lines of evidence that together offer clear support to the ribosomal protection hypothesis. Of particular note, we show that addition of purified ABC-F proteins to anin vitrotranslation assay prompts dose-dependent rescue of translation, and demonstrate that such proteins are capable of displacing antibiotic from the ribosomein vitro To our knowledge, these experiments constitute the first direct evidence that ABC-F proteins mediate antibiotic resistance through ribosomal protection.IMPORTANCEAntimicrobial resistance ranks among the greatest threats currently facing human health. Elucidation of the mechanisms by which microorganisms resist the effect of antibiotics is central to understanding the biology of this phenomenon and has the potential to inform the development of new drugs capable of blocking or circumventing resistance. Members of the ABC-F family, which includelsa(A),msr(A),optr(A), andvga(A), collectively yield resistance to a broader range of clinically significant antibiotic classes than any other family of resistance determinants, although their mechanism of action has been controversial since their discovery 25 years ago. Here we present the first direct evidence that proteins of the ABC-F family act to protect the bacterial ribosome from antibiotic-mediated inhibition.
    MeSH term(s) ATP-Binding Cassette Transporters/metabolism ; Anti-Bacterial Agents/metabolism ; Anti-Bacterial Agents/pharmacology ; Drug Resistance, Bacterial ; Gram-Positive Bacteria/drug effects ; Microbial Sensitivity Tests ; Protein Biosynthesis/drug effects ; Ribosomes/drug effects ; Ribosomes/metabolism
    Chemical Substances ATP-Binding Cassette Transporters ; Anti-Bacterial Agents
    Language English
    Publishing date 2016-03-22
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2557172-2
    ISSN 2150-7511 ; 2161-2129
    ISSN (online) 2150-7511
    ISSN 2161-2129
    DOI 10.1128/mBio.01975-15
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: The two-component system WalKR provides an essential link between cell wall homeostasis and DNA replication in

    Sharkey, Liam K R / Guerillot, Romain / Walsh, Calum J / Turner, Adrianna M / Lee, Jean Y H / Neville, Stephanie L / Klatt, Stephan / Baines, Sarah L / Pidot, Sacha J / Rossello, Fernando J / Seemann, Torsten / McWilliam, Hamish E G / Cho, Ellie / Carter, Glen P / Howden, Benjamin P / McDevitt, Christopher A / Hachani, Abderrahman / Stinear, Timothy P / Monk, Ian R

    mBio

    2023  , Page(s) e0226223

    Abstract: Among the 16 two-component systems in the opportunistic human ... ...

    Abstract Among the 16 two-component systems in the opportunistic human pathogen
    Language English
    Publishing date 2023-10-16
    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.02262-23
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: Accessible Platform for High-Throughput COVID-19 Molecular Diagnostics and Genome Sequencing Using a Repurposed 3D Printer for RNA Extraction.

    Vandelannoote, Koen / Buultjens, Andrew H / Li, Lucy / Sharkey, Liam K / Herisse, Marion / Pidot, Sacha J / Hoang, Tuyet / Howden, Benjamin P / Monk, Ian R / Seemann, Torsten / Lee, Jean Y H / Stinear, Timothy P

    ACS biomaterials science & engineering

    2021  Volume 7, Issue 9, Page(s) 4669–4676

    Abstract: The COVID-19 pandemic has exposed the dependence of diagnostic laboratories on a handful of large corporations with market monopolies on the worldwide supply of reagents, consumables, and hardware for molecular diagnostics. Global shortages of key ... ...

    Abstract The COVID-19 pandemic has exposed the dependence of diagnostic laboratories on a handful of large corporations with market monopolies on the worldwide supply of reagents, consumables, and hardware for molecular diagnostics. Global shortages of key consumables for RT-qPCR detection of SARS-CoV-2 RNA have impaired the ability to run essential, routine diagnostic services. Here, we describe a workflow for rapid detection of SARS-CoV-2 RNA in upper respiratory samples including nasal swabs and saliva, utilizing low-cost equipment and readily accessible reagents. Using repurposed
    MeSH term(s) COVID-19 ; Humans ; Pandemics ; Pathology, Molecular ; RNA, Viral/genetics ; SARS-CoV-2
    Chemical Substances RNA, Viral
    Language English
    Publishing date 2021-08-26
    Publishing country United States
    Document type Journal Article
    ISSN 2373-9878
    ISSN (online) 2373-9878
    DOI 10.1021/acsbiomaterials.1c00775
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: Zinc-binding to the cytoplasmic PAS domain regulates the essential WalK histidine kinase of Staphylococcus aureus.

    Monk, Ian R / Shaikh, Nausad / Begg, Stephanie L / Gajdiss, Mike / Sharkey, Liam K R / Lee, Jean Y H / Pidot, Sacha J / Seemann, Torsten / Kuiper, Michael / Winnen, Brit / Hvorup, Rikki / Collins, Brett M / Bierbaum, Gabriele / Udagedara, Saumya R / Morey, Jacqueline R / Pulyani, Neha / Howden, Benjamin P / Maher, Megan J / McDevitt, Christopher A /
    King, Glenn F / Stinear, Timothy P

    Nature communications

    2019  Volume 10, Issue 1, Page(s) 3067

    Abstract: WalKR (YycFG) is the only essential two-component regulator in the human pathogen Staphylococcus aureus. WalKR regulates peptidoglycan synthesis, but this function alone does not explain its essentiality. Here, to further understand WalKR function, we ... ...

    Abstract WalKR (YycFG) is the only essential two-component regulator in the human pathogen Staphylococcus aureus. WalKR regulates peptidoglycan synthesis, but this function alone does not explain its essentiality. Here, to further understand WalKR function, we investigate a suppressor mutant that arose when WalKR activity was impaired; a histidine to tyrosine substitution (H271Y) in the cytoplasmic Per-Arnt-Sim (PAS
    MeSH term(s) Amino Acid Substitution ; Bacterial Proteins/chemistry ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Cations, Divalent/metabolism ; Histidine/genetics ; Histidine Kinase/chemistry ; Histidine Kinase/genetics ; Histidine Kinase/metabolism ; Molecular Dynamics Simulation ; Mutation ; Protein-Serine-Threonine Kinases/chemistry ; Protein-Serine-Threonine Kinases/genetics ; Protein-Serine-Threonine Kinases/metabolism ; Regulon/genetics ; Staphylococcus aureus/genetics ; Staphylococcus aureus/metabolism ; Tyrosine/genetics ; Zinc/metabolism
    Chemical Substances Bacterial Proteins ; Cations, Divalent ; YycF protein, Bacteria ; Tyrosine (42HK56048U) ; Histidine (4QD397987E) ; PAS domain kinases (EC 2.7.1.11) ; Protein-Serine-Threonine Kinases (EC 2.7.11.1) ; Histidine Kinase (EC 2.7.13.1) ; Zinc (J41CSQ7QDS)
    Language English
    Publishing date 2019-07-11
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2553671-0
    ISSN 2041-1723 ; 2041-1723
    ISSN (online) 2041-1723
    ISSN 2041-1723
    DOI 10.1038/s41467-019-10932-4
    Database MEDical Literature Analysis and Retrieval System OnLINE

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