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  1. Book ; Online ; E-Book: Lyme disease and relapsing fever spirochetes

    Radolf, Justin D. / Samuels, D. Scott

    genomics, molecular biology, host interactions and disease pathogenesis

    2021  

    Abstract: Written by renowned scientists who have made seminal contributions to the field, this book contains an expansive treatment of the options to track live spirochetes and evaluate gene expression in ticks and mice, provides insights into the workings of the ...

    Author's details editor, Justin D. Radolf
    Abstract Written by renowned scientists who have made seminal contributions to the field, this book contains an expansive treatment of the options to track live spirochetes and evaluate gene expression in ticks and mice, provides insights into the workings of the flagellar motor, presents up-to-date research on the modulation of gene expression, and reviews recent studies on the Lyme disease spirochete's networks of regulatory pathways.
    Keywords Lyme disease ; Molecular biology ; Parasitology ; Relapsing fever ; Spirochetes ; Tick-borne diseases
    Subject code 616.9246
    Language English
    Size 1 online resource (769 pages) :, illustrations
    Publisher Caister Academic Press
    Publishing place Norfolk, England
    Document type Book ; Online ; E-Book
    Note Includes index.
    Remark Zugriff für angemeldete ZB MED-Nutzerinnen und -Nutzer
    ISBN 1-913652-62-9 ; 1-913652-61-0 ; 978-1-913652-62-3 ; 978-1-913652-61-6
    Database ZB MED Catalogue: Medicine, Health, Nutrition, Environment, Agriculture

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  2. Book: Pathogenic treponema

    Radolf, Justin D.

    molecular and cellular biology

    2006  

    Author's details ed. by Justin D. Radolf
    Keywords Treponema / pathogenicity ; Treponema
    Subject code 616.9201
    Language English
    Size X, 466 S. : Ill., graph. Darst.
    Publisher Caister
    Publishing place Wymondham
    Publishing country Great Britain
    Document type Book
    HBZ-ID HT014730679
    ISBN 1-904455-10-7 ; 978-1-904455-10-3
    Database Catalogue ZB MED Medicine, Health

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  3. Book: Borrelia

    Samuels, D. Scott / Radolf, Justin D.

    molecular biology, host interaction and pathogenesis

    2010  

    Author's details ed. by D. Scott Samuels and Justin D. Radolf
    Keywords Borrelia / genetics ; Borrelia burgdorferi / genetics ; Lyme Disease
    Language English
    Size XII, 547, A-4 S. : Ill., graph. Darst.
    Publisher Caister
    Publishing place Norfolk
    Publishing country Great Britain
    Document type Book
    HBZ-ID HT016080027
    ISBN 978-1-904455-58-5 ; 1-904455-58-1
    Database Catalogue ZB MED Medicine, Health

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  4. Article ; Online: Editorial: Syphilis infection: clinical, epidemiology, basic science, and behavioral research.

    Zhou, Pingyu / Ye, Meiping / Tucker, Joseph D / Zhang, Lei / Radolf, Justin David

    Frontiers in immunology

    2023  Volume 14, Page(s) 1182069

    MeSH term(s) Humans ; Syphilis/epidemiology ; Behavioral Research ; Risk Factors ; Research
    Language English
    Publishing date 2023-04-06
    Publishing country Switzerland
    Document type Editorial ; Research Support, Non-U.S. Gov't
    ZDB-ID 2606827-8
    ISSN 1664-3224 ; 1664-3224
    ISSN (online) 1664-3224
    ISSN 1664-3224
    DOI 10.3389/fimmu.2023.1182069
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Editorial

    Pingyu Zhou / Meiping Ye / Joseph D. Tucker / Lei Zhang / Justin David Radolf

    Frontiers in Immunology, Vol

    Syphilis infection: clinical, epidemiology, basic science, and behavioral research

    2023  Volume 14

    Keywords syphilis ; clinical research ; epidemiology ; basic science ; behavioral research ; Immunologic diseases. Allergy ; RC581-607
    Language English
    Publishing date 2023-04-01T00:00:00Z
    Publisher Frontiers Media S.A.
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  6. Article ; Online: Pulling the trigger on lyme arthritis.

    Radolf, Justin D

    The Journal of infectious diseases

    2013  Volume 207, Issue 6, Page(s) 877–879

    MeSH term(s) Animals ; Antigens, Bacterial/genetics ; Bacterial Outer Membrane Proteins/genetics ; Borrelia burgdorferi/genetics ; Borrelia burgdorferi/pathogenicity ; Genes, Bacterial ; Lyme Disease/microbiology ; Virulence Factors/genetics
    Chemical Substances Antigens, Bacterial ; Bacterial Outer Membrane Proteins ; Virulence Factors
    Language English
    Publishing date 2013-01-09
    Publishing country United States
    Document type Editorial ; Research Support, N.I.H., Extramural ; Comment
    ZDB-ID 3019-3
    ISSN 1537-6613 ; 0022-1899
    ISSN (online) 1537-6613
    ISSN 0022-1899
    DOI 10.1093/infdis/jis931
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: Host-specific functional compartmentalization within the oligopeptide transporter during the Borrelia burgdorferi enzootic cycle.

    Groshong, Ashley M / McLain, Melissa A / Radolf, Justin D

    PLoS pathogens

    2021  Volume 17, Issue 1, Page(s) e1009180

    Abstract: Borrelia burgdorferi must acquire all of its amino acids (AAs) from its arthropod vector and vertebrate host. Previously, we determined that peptide uptake via the oligopeptide (Opp) ABC transporter is essential for spirochete viability in vitro and ... ...

    Abstract Borrelia burgdorferi must acquire all of its amino acids (AAs) from its arthropod vector and vertebrate host. Previously, we determined that peptide uptake via the oligopeptide (Opp) ABC transporter is essential for spirochete viability in vitro and during infection. Our prior study also suggested that B. burgdorferi employs temporal regulation in concert with structural variation of oligopeptide-binding proteins (OppAs) to meet its AA requirements in each biological niche. Herein, we evaluated the contributions to the B. burgdorferi enzootic cycle of three of the spirochete's five OppAs (OppA1, OppA2, and OppA5). An oppA1 transposon (tn) mutant lysed in the hyperosmolar environment of the feeding tick, suggesting that OppA1 imports amino acids required for osmoprotection. The oppA2tn mutant displayed a profound defect in hematogenous dissemination in mice, yet persisted within skin while inducing only a minimal antibody response. These results, along with slightly decreased growth of the oppA2tn mutant within DMCs, suggest that OppA2 serves a minor nutritive role, while its dissemination defect points to an as yet uncharacterized signaling function. Previously, we identified a role for OppA5 in spirochete persistence within the mammalian host. We now show that the oppA5tn mutant displayed no defect during the tick phase of the cycle and could be tick-transmitted to naïve mice. Instead of working in tandem, however, OppA2 and OppA5 appear to function in a hierarchical manner; the ability of OppA5 to promote persistence relies upon the ability of OppA2 to facilitate dissemination. Structural homology models demonstrated variations within the binding pockets of OppA1, 2, and 5 indicative of different peptide repertoires. Rather than being redundant, B. burgdorferi's multiplicity of Opp binding proteins enables host-specific functional compartmentalization during the spirochete lifecycle.
    MeSH term(s) Animals ; Bacterial Proteins/metabolism ; Biological Transport ; Borrelia burgdorferi/physiology ; Female ; Gene Expression Regulation, Bacterial ; Host-Pathogen Interactions ; Ixodes/microbiology ; Lyme Disease/genetics ; Lyme Disease/metabolism ; Lyme Disease/microbiology ; Membrane Transport Proteins/metabolism ; Mice ; Mice, Inbred C3H ; Oligopeptides/metabolism ; Rats ; Rats, Sprague-Dawley ; Virulence
    Chemical Substances Bacterial Proteins ; Membrane Transport Proteins ; Oligopeptides
    Language English
    Publishing date 2021-01-11
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2205412-1
    ISSN 1553-7374 ; 1553-7366
    ISSN (online) 1553-7374
    ISSN 1553-7366
    DOI 10.1371/journal.ppat.1009180
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: BosR and PlzA reciprocally regulate RpoS function to sustain Borrelia burgdorferi in ticks and mammals.

    Grassmann, André A / Tokarz, Rafal / Golino, Caroline / McLain, Melissa A / Groshong, Ashley M / Radolf, Justin D / Caimano, Melissa J

    The Journal of clinical investigation

    2023  Volume 133, Issue 5

    Abstract: The RNA polymerase alternative σ factor RpoS in Borrelia burgdorferi (Bb), the Lyme disease pathogen, is responsible for programmatic-positive and -negative gene regulation essential for the spirochete's dual-host enzootic cycle. RpoS is expressed during ...

    Abstract The RNA polymerase alternative σ factor RpoS in Borrelia burgdorferi (Bb), the Lyme disease pathogen, is responsible for programmatic-positive and -negative gene regulation essential for the spirochete's dual-host enzootic cycle. RpoS is expressed during tick-to-mammal transmission and throughout mammalian infection. Although the mammalian-phase RpoS regulon is well described, its counterpart during the transmission blood meal is unknown. Here, we used Bb-specific transcript enrichment by tick-borne disease capture sequencing (TBDCapSeq) to compare the transcriptomes of WT and ΔrpoS Bb in engorged nymphs and following mammalian host-adaptation within dialysis membrane chambers. TBDCapSeq revealed dramatic changes in the contours of the RpoS regulon within ticks and mammals and further confirmed that RpoS-mediated repression is specific to the mammalian-phase of Bb's enzootic cycle. We also provide evidence that RpoS-dependent gene regulation, including repression of tick-phase genes, is required for persistence in mice. Comparative transcriptomics of engineered Bb strains revealed that the Borrelia oxidative stress response regulator (BosR), a noncanonical Fur family member, and the cyclic diguanosine monophosphate (c-di-GMP) effector PlzA reciprocally regulate the function of RNA polymerase complexed with RpoS. BosR is required for RpoS-mediated transcription activation and repression in addition to its well-defined role promoting transcription of rpoS by the RNA polymerase alternative σ factor RpoN. During transmission, ligand-bound PlzA antagonizes RpoS-mediated repression, presumably acting through BosR.
    MeSH term(s) Mice ; Animals ; Borrelia burgdorferi/genetics ; Borrelia/metabolism ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Ticks/genetics ; Sigma Factor/genetics ; Sigma Factor/metabolism ; Lyme Disease/genetics ; Mammals/metabolism ; Gene Expression Regulation, Bacterial
    Chemical Substances Bacterial Proteins ; Sigma Factor
    Language English
    Publishing date 2023-03-01
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 3067-3
    ISSN 1558-8238 ; 0021-9738
    ISSN (online) 1558-8238
    ISSN 0021-9738
    DOI 10.1172/JCI166710
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: Lyme Disease in Humans.

    Radolf, Justin D / Strle, Klemen / Lemieux, Jacob E / Strle, Franc

    Current issues in molecular biology

    2020  Volume 42, Page(s) 333–384

    Abstract: Lyme disease (Lyme borreliosis) is a tick-borne, zoonosis of adults and children caused by genospecies of ... ...

    Abstract Lyme disease (Lyme borreliosis) is a tick-borne, zoonosis of adults and children caused by genospecies of the
    MeSH term(s) Animals ; Arthropod Vectors/microbiology ; Borrelia burgdorferi/genetics ; Borrelia burgdorferi/growth & development ; Disease Management ; Disease Susceptibility ; Host-Pathogen Interactions/immunology ; Humans ; Life Cycle Stages ; Lyme Disease/diagnosis ; Lyme Disease/epidemiology ; Lyme Disease/microbiology ; Lyme Disease/transmission ; Organ Specificity ; Ticks/microbiology
    Language English
    Publishing date 2020-12-11
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2000024-8
    ISSN 1467-3045 ; 1467-3037
    ISSN (online) 1467-3045
    ISSN 1467-3037
    DOI 10.21775/cimb.042.333
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: Host-specific functional compartmentalization within the oligopeptide transporter during the Borrelia burgdorferi enzootic cycle.

    Ashley M Groshong / Melissa A McLain / Justin D Radolf

    PLoS Pathogens, Vol 17, Iss 1, p e

    2021  Volume 1009180

    Abstract: Borrelia burgdorferi must acquire all of its amino acids (AAs) from its arthropod vector and vertebrate host. Previously, we determined that peptide uptake via the oligopeptide (Opp) ABC transporter is essential for spirochete viability in vitro and ... ...

    Abstract Borrelia burgdorferi must acquire all of its amino acids (AAs) from its arthropod vector and vertebrate host. Previously, we determined that peptide uptake via the oligopeptide (Opp) ABC transporter is essential for spirochete viability in vitro and during infection. Our prior study also suggested that B. burgdorferi employs temporal regulation in concert with structural variation of oligopeptide-binding proteins (OppAs) to meet its AA requirements in each biological niche. Herein, we evaluated the contributions to the B. burgdorferi enzootic cycle of three of the spirochete's five OppAs (OppA1, OppA2, and OppA5). An oppA1 transposon (tn) mutant lysed in the hyperosmolar environment of the feeding tick, suggesting that OppA1 imports amino acids required for osmoprotection. The oppA2tn mutant displayed a profound defect in hematogenous dissemination in mice, yet persisted within skin while inducing only a minimal antibody response. These results, along with slightly decreased growth of the oppA2tn mutant within DMCs, suggest that OppA2 serves a minor nutritive role, while its dissemination defect points to an as yet uncharacterized signaling function. Previously, we identified a role for OppA5 in spirochete persistence within the mammalian host. We now show that the oppA5tn mutant displayed no defect during the tick phase of the cycle and could be tick-transmitted to naïve mice. Instead of working in tandem, however, OppA2 and OppA5 appear to function in a hierarchical manner; the ability of OppA5 to promote persistence relies upon the ability of OppA2 to facilitate dissemination. Structural homology models demonstrated variations within the binding pockets of OppA1, 2, and 5 indicative of different peptide repertoires. Rather than being redundant, B. burgdorferi's multiplicity of Opp binding proteins enables host-specific functional compartmentalization during the spirochete lifecycle.
    Keywords Immunologic diseases. Allergy ; RC581-607 ; Biology (General) ; QH301-705.5
    Subject code 570
    Language English
    Publishing date 2021-01-01T00:00:00Z
    Publisher Public Library of Science (PLoS)
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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