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  1. Article ; Online: Host range of SARS-CoV-2 and implications for public health

    Joanne M Santini / Sarah J L Edwards

    The Lancet Microbe, Vol 1, Iss 4, Pp e141-e

    2020  Volume 142

    Keywords Medicine (General) ; R5-920 ; Microbiology ; QR1-502
    Language English
    Publishing date 2020-08-01T00:00:00Z
    Publisher Elsevier
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  2. Article ; Online: Anthroponotic risk of SARS-CoV-2, precautionary mitigation, and outbreak management

    Sarah J L Edwards / Joanne M Santini

    The Lancet Microbe, Vol 1, Iss 5, Pp e187-e

    2020  Volume 188

    Keywords Medicine (General) ; R5-920 ; Microbiology ; QR1-502
    Language English
    Publishing date 2020-09-01T00:00:00Z
    Publisher Elsevier
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  3. Article ; Online: Large-scale network analysis captures biological features of bacterial plasmids

    Mislav Acman / Lucy van Dorp / Joanne M. Santini / Francois Balloux

    Nature Communications, Vol 11, Iss 1, Pp 1-

    2020  Volume 11

    Abstract: Plasmids can mediate the exchange of genetic material between bacterial cells. Here, Acman et al. use network analyses to study the population structure and dynamics of over 10,000 plasmids, assigning them into cliques that correlate with gene content, ... ...

    Abstract Plasmids can mediate the exchange of genetic material between bacterial cells. Here, Acman et al. use network analyses to study the population structure and dynamics of over 10,000 plasmids, assigning them into cliques that correlate with gene content, host range, and existing classifications based on replicon and mobility types.
    Keywords Science ; Q
    Language English
    Publishing date 2020-05-01T00:00:00Z
    Publisher Nature Publishing Group
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  4. Article ; Online: Large-scale network analysis captures biological features of bacterial plasmids

    Mislav Acman / Lucy van Dorp / Joanne M. Santini / Francois Balloux

    Nature Communications, Vol 11, Iss 1, Pp 1-

    2020  Volume 11

    Abstract: Plasmids can mediate the exchange of genetic material between bacterial cells. Here, Acman et al. use network analyses to study the population structure and dynamics of over 10,000 plasmids, assigning them into cliques that correlate with gene content, ... ...

    Abstract Plasmids can mediate the exchange of genetic material between bacterial cells. Here, Acman et al. use network analyses to study the population structure and dynamics of over 10,000 plasmids, assigning them into cliques that correlate with gene content, host range, and existing classifications based on replicon and mobility types.
    Keywords Science ; Q
    Language English
    Publishing date 2020-05-01T00:00:00Z
    Publisher Nature Portfolio
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  5. Article ; Online: Detection and enumeration of Lak megaphages in microbiome samples by endpoint and quantitative PCR

    Marco A. Crisci / Paula M. Corsini / Nicola Bordin / Lin-Xing Chen / Jillain F. Banfield / Joanne M. Santini

    STAR Protocols, Vol 3, Iss 1, Pp 101029- (2022)

    2022  

    Abstract: Summary: Lak megaphages are prevalent across diverse gut microbiomes and may potentially impact animal and human health through lysis of Prevotella. Given their large genome size (up to 660 kbp), Lak megaphages are difficult to culture, and their ... ...

    Abstract Summary: Lak megaphages are prevalent across diverse gut microbiomes and may potentially impact animal and human health through lysis of Prevotella. Given their large genome size (up to 660 kbp), Lak megaphages are difficult to culture, and their identification relies on molecular techniques. Here, we present optimized protocols for identifying Lak phages in various microbiome samples, including procedures for DNA extraction, followed by detection and quantification of genes encoding Lak structural proteins using diagnostic endpoint and SYBR green-based quantitative PCR, respectively.For complete details on the use and execution of this protocol, please refer to Crisci et al., (2021).
    Keywords Health Sciences ; Immunology ; Microbiology ; Molecular Biology ; Science (General) ; Q1-390
    Language English
    Publishing date 2022-03-01T00:00:00Z
    Publisher Elsevier
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  6. Article: Comparative proteomics of Acidithiobacillus ferrooxidans grown in the presence and absence of uranium

    Dekker, Linda / Florence Arsène-Ploetze / Joanne M. Santini

    Research in microbiology. 2016 Apr., v. 167, no. 3

    2016  

    Abstract: Acidithiobacillus ferrooxidans is an acidophile that thrives in metal-contaminated environments and tolerates high levels of uranium. To gain a better understanding of the processes involved in U(VI) resistance, comparative proteomics was used. The ... ...

    Abstract Acidithiobacillus ferrooxidans is an acidophile that thrives in metal-contaminated environments and tolerates high levels of uranium. To gain a better understanding of the processes involved in U(VI) resistance, comparative proteomics was used. The proteome of A. ferrooxidans was grown in the presence and absence of 0.5 mM U(VI); expression of 17 proteins was upregulated and one was downregulated. Most proteins with increased expression are part of the general stress response or are involved in reactive oxygen species detoxification. Four novel proteins showed increased expression in the presence of U(VI) and may contribute to U(VI) resistance via thiol homoeostasis and U(VI) binding.
    Keywords Acidithiobacillus ferrooxidans ; gene expression regulation ; proteins ; proteome ; proteomics ; reactive oxygen species ; stress response ; thiols ; uranium
    Language English
    Dates of publication 2016-04
    Size p. 234-239.
    Publishing place Elsevier Masson SAS
    Document type Article
    ZDB-ID 1004220-9
    ISSN 1769-7123 ; 0923-2508
    ISSN (online) 1769-7123
    ISSN 0923-2508
    DOI 10.1016/j.resmic.2016.01.007
    Database NAL-Catalogue (AGRICOLA)

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    Z 63/179 A/B: Show issues

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  7. Article ; Online: The active site structure and catalytic mechanism of arsenite oxidase

    Thomas P. Warelow / M. Jake Pushie / Julien J. H. Cotelesage / Joanne M. Santini / Graham N. George

    Scientific Reports, Vol 7, Iss 1, Pp 1-

    2017  Volume 9

    Abstract: Abstract Arsenite oxidase is thought to be an ancient enzyme, originating before the divergence of the Archaea and the Bacteria. We have investigated the nature of the molybdenum active site of the arsenite oxidase from the Alphaproteobacterium Rhizobium ...

    Abstract Abstract Arsenite oxidase is thought to be an ancient enzyme, originating before the divergence of the Archaea and the Bacteria. We have investigated the nature of the molybdenum active site of the arsenite oxidase from the Alphaproteobacterium Rhizobium sp. str. NT-26 using a combination of X-ray absorption spectroscopy and computational chemistry. Our analysis indicates an oxidized Mo(VI) active site with a structure that is far from equilibrium. We propose that this is an entatic state imposed by the protein on the active site through relative orientation of the two molybdopterin cofactors, in a variant of the Rây-Dutt twist of classical coordination chemistry, which we call the pterin twist hypothesis. We discuss the implications of this hypothesis for other putatively ancient molybdopterin-based enzymes.
    Keywords Medicine ; R ; Science ; Q
    Language English
    Publishing date 2017-05-01T00:00:00Z
    Publisher Nature Portfolio
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  8. Article: Electrochemically driven catalysis of Rhizobium sp. NT-26 arsenite oxidase with its native electron acceptor cytochrome c552

    Kalimuthu, Palraj / Matthew D. Heath / Joanne M. Santini / Ulrike Kappler / Paul V. Bernhardt

    Biochimica et biophysica acta. 2014 Jan., v. 1837, no. 1

    2014  

    Abstract: We describe the catalytic voltammograms of the periplasmic arsenite oxidase (Aio) from the chemolithoautotrophic bacterium Rhizobium sp. str. NT-26 that oxidizes arsenite to arsenate. Electrochemistry of the enzyme was accomplished using its native ... ...

    Abstract We describe the catalytic voltammograms of the periplasmic arsenite oxidase (Aio) from the chemolithoautotrophic bacterium Rhizobium sp. str. NT-26 that oxidizes arsenite to arsenate. Electrochemistry of the enzyme was accomplished using its native electron transfer partner, cytochrome c552 (cyt c552), as a mediator. The protein cyt c552 adsorbed on a mercaptoundecanoic acid (MUA) modified Au electrode exhibited a stable, reversible one-electron voltammetric response at +275mV vs NHE (pH6). In the presence of arsenite and Aio the voltammetry of cyt c552 is transformed from a transient response to an amplified sigmoidal (steady state) wave consistent with an electro-catalytic system. Digital simulation was performed using a single set of parameters for all catalytic voltammetries obtained at different sweep rates and various substrate concentrations. The obtained kinetic constants from digital simulation provide new insight into the kinetics of the NT-26 Aio catalytic mechanism.
    Keywords Rhizobium ; arsenates ; arsenites ; bacteria ; catalytic activity ; computer simulation ; electrochemistry ; electrodes ; electron transfer ; gold
    Language English
    Dates of publication 2014-01
    Size p. 112-120.
    Publishing place Elsevier B.V.
    Document type Article
    ZDB-ID 282711-6
    ISSN 0005-2728 ; 0304-4173
    ISSN 0005-2728 ; 0304-4173
    DOI 10.1016/j.bbabio.2013.07.010
    Database NAL-Catalogue (AGRICOLA)

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    In stock of ZB MED Cologne/Königswinter

    Uc I Zs.247: Show issues Location:
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  9. Article ; Online: Closely related Lak megaphages replicate in the microbiomes of diverse animals

    Marco A. Crisci / Lin-Xing Chen / Audra E. Devoto / Adair L. Borges / Nicola Bordin / Rohan Sachdeva / Adrian Tett / Allison M. Sharrar / Nicola Segata / Francesco Debenedetti / Mick Bailey / Rachel Burt / Rhiannon M. Wood / Lewis J. Rowden / Paula M. Corsini / Steven van Winden / Mark A. Holmes / Shufei Lei / Jillian F. Banfield /
    Joanne M. Santini

    iScience, Vol 24, Iss 8, Pp 102875- (2021)

    2021  

    Abstract: Summary: Lak phages with alternatively coded ∼540 kbp genomes were recently reported to replicate in Prevotella in microbiomes of humans that consume a non-Western diet, baboons, and pigs. Here, we explore Lak phage diversity and broader distribution ... ...

    Abstract Summary: Lak phages with alternatively coded ∼540 kbp genomes were recently reported to replicate in Prevotella in microbiomes of humans that consume a non-Western diet, baboons, and pigs. Here, we explore Lak phage diversity and broader distribution using diagnostic polymerase chain reaction and genome-resolved metagenomics. Lak phages were detected in 13 animal types, including reptiles, and are particularly prevalent in pigs. Tracking Lak through the pig gastrointestinal tract revealed significant enrichment in the hindgut compared to the foregut. We reconstructed 34 new Lak genomes, including six curated complete genomes, all of which are alternatively coded. An anomalously large (∼660 kbp) complete genome reconstructed for the most deeply branched Lak from a horse microbiome is also alternatively coded. From the Lak genomes, we identified proteins associated with specific animal species; notably, most have no functional predictions. The presence of closely related Lak phages in diverse animals indicates facile distribution coupled to host-specific adaptation.
    Keywords Virology ; Microbiome ; Omics ; Science ; Q
    Subject code 630
    Language English
    Publishing date 2021-08-01T00:00:00Z
    Publisher Elsevier
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  10. Article: Electron transfer through arsenite oxidase: Insights into Rieske interaction with cytochrome c

    Watson, Cameron / Dimitri Niks / Russ Hille / Marta Vieira / Barbara Schoepp-Cothenet / Alexandra T. Marques / Maria João Romão / Teresa Santos-Silva / Joanne M. Santini

    Biochimica et biophysica acta. 2017 Oct., v. 1858, no. 10

    2017  

    Abstract: Arsenic is a widely distributed environmental toxin whose presence in drinking water poses a threat to >140 million people worldwide. The respiratory enzyme arsenite oxidase from various bacteria catalyses the oxidation of arsenite to arsenate and is ... ...

    Abstract Arsenic is a widely distributed environmental toxin whose presence in drinking water poses a threat to >140 million people worldwide. The respiratory enzyme arsenite oxidase from various bacteria catalyses the oxidation of arsenite to arsenate and is being developed as a biosensor for arsenite. The arsenite oxidase from Rhizobium sp. str. NT-26 (a member of the Alphaproteobacteria) is a heterotetramer consisting of a large catalytic subunit (AioA), which contains a molybdenum centre and a 3Fe-4S cluster, and a small subunit (AioB) containing a Rieske 2Fe-2S cluster. Stopped-flow spectroscopy and isothermal titration calorimetry (ITC) have been used to better understand electron transfer through the redox-active centres of the enzyme, which is essential for biosensor development. Results show that oxidation of arsenite at the active site is extremely fast with a rate of >4000s−1 and reduction of the electron acceptor is rate-limiting. An AioB-F108A mutation results in increased activity with the artificial electron acceptor DCPIP and decreased activity with cytochrome c, which in the latter as demonstrated by ITC is not due to an effect on the protein-protein interaction but instead to an effect on electron transfer. These results provide further support that the AioB F108 is important in electron transfer between the Rieske subunit and cytochrome c and its absence in the arsenite oxidases from the Betaproteobacteria may explain the inability of these enzymes to use this electron acceptor.
    Keywords Rhizobium ; arsenates ; arsenic ; arsenites ; bacteria ; beta-Proteobacteria ; biosensors ; calorimetry ; cytochrome c ; drinking water ; electron transfer ; energy metabolism ; enzymes ; molybdenum ; mutation ; oxidation ; people ; protein subunits ; protein-protein interactions ; spectroscopy ; titration
    Language English
    Dates of publication 2017-10
    Size p. 865-872.
    Publishing place Elsevier B.V.
    Document type Article
    ZDB-ID 282711-6
    ISSN 0005-2728 ; 0304-4173
    ISSN 0005-2728 ; 0304-4173
    DOI 10.1016/j.bbabio.2017.08.003
    Database NAL-Catalogue (AGRICOLA)

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    In stock of ZB MED Cologne/Königswinter

    Uc I Zs.247: Show issues Location:
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