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  1. Article ; Online: Reference genome for the Northern bat (Eptesicus nilssonii), a most northern bat species.

    Laine, Veronika N / Pulliainen, Arto T / Lilley, Thomas M

    The Journal of heredity

    2023  Volume 115, Issue 1, Page(s) 149–154

    Abstract: The northern bat (Eptesicus nilssonii) is the most northern bat species in the world. Its distribution covers whole Eurasia, and the species is thus well adapted to different habitat types. However, recent population declines have been reported and rapid ...

    Abstract The northern bat (Eptesicus nilssonii) is the most northern bat species in the world. Its distribution covers whole Eurasia, and the species is thus well adapted to different habitat types. However, recent population declines have been reported and rapid conservation efforts are needed. Here we present a high-quality de novo genome assembly of a female northern bat from Finland (BLF_Eptnil_asm_v1.0). The assembly was generated using a combination of Pacbio and Omni-C technologies. The primary assembly comprises 726 scaffolds spanning 2.0 Gb, represented by a scaffold N50 of 102 Mb, a contig N50 of 66.2 Mb, and a BUSCO completeness score of 93.73%. Annotation of the assembly identified 20,250 genes. This genome will be an important resource for the conservation and evolutionary genomic studies especially in understanding how rapid environmental changes affect northern species.
    MeSH term(s) Animals ; Female ; Chiroptera/genetics ; Genome ; Genomics ; Biological Evolution ; Chromosomes
    Language English
    Publishing date 2023-08-26
    Publishing country United States
    Document type Journal Article
    ZDB-ID 3044-2
    ISSN 1465-7333 ; 0022-1503
    ISSN (online) 1465-7333
    ISSN 0022-1503
    DOI 10.1093/jhered/esad056
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

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  2. Article ; Online: The Chaperonin TRiC/CCT Inhibitor HSF1A Protects Cells from Intoxication with Pertussis Toxin.

    Jia, Jinfang / Zoeschg, Manuel / Barth, Holger / Pulliainen, Arto T / Ernst, Katharina

    Toxins

    2024  Volume 16, Issue 1

    Abstract: Pertussis toxin (PT) is a bacterial ... ...

    Abstract Pertussis toxin (PT) is a bacterial AB
    MeSH term(s) Pertussis Toxin ; Bacterial Toxins/toxicity ; Clostridioides difficile ; Cytosol ; Antibodies, Bacterial ; Chaperonin Containing TCP-1
    Chemical Substances Pertussis Toxin (EC 2.4.2.31) ; Bacterial Toxins ; Antibodies, Bacterial ; Chaperonin Containing TCP-1 (EC 3.6.1.-)
    Language English
    Publishing date 2024-01-10
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2518395-3
    ISSN 2072-6651 ; 2072-6651
    ISSN (online) 2072-6651
    ISSN 2072-6651
    DOI 10.3390/toxins16010036
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  3. Article ; Online: Exotoxin-Targeted Drug Modalities as Antibiotic Alternatives.

    Sakari, Moona / Laisi, Arttu / Pulliainen, Arto T

    ACS infectious diseases

    2022  Volume 8, Issue 3, Page(s) 433–456

    Abstract: The paradigm of antivirulence therapy dictates that bacterial pathogens are specifically disarmed but not killed by neutralizing their virulence factors. Clearance of the invading pathogen by the immune system is promoted. As compared to antibiotics, the ...

    Abstract The paradigm of antivirulence therapy dictates that bacterial pathogens are specifically disarmed but not killed by neutralizing their virulence factors. Clearance of the invading pathogen by the immune system is promoted. As compared to antibiotics, the pathogen-selective antivirulence drugs hold promise to minimize collateral damage to the beneficial microbiome. Also, selective pressure for resistance is expected to be lower because bacterial viability is not directly affected. Antivirulence drugs are being developed for stand-alone prophylactic and therapeutic treatments but also for combinatorial use with antibiotics. This Review focuses on drug modalities that target bacterial exotoxins after the secretion or release-upon-lysis. Exotoxins have a significant and sometimes the primary role as the disease-causing virulence factor, and thereby they are attractive targets for drug development. We describe the key pre-clinical and clinical trial data that have led to the approval of currently used exotoxin-targeted drugs, namely the monoclonal antibodies bezlotoxumab (toxin B/TcdB,
    MeSH term(s) Anti-Bacterial Agents/pharmacology ; Anti-Bacterial Agents/therapeutic use ; Bacillus anthracis ; Bacterial Toxins ; Clostridioides difficile ; Exotoxins
    Chemical Substances Anti-Bacterial Agents ; Bacterial Toxins ; Exotoxins
    Language English
    Publishing date 2022-01-31
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ISSN 2373-8227
    ISSN (online) 2373-8227
    DOI 10.1021/acsinfecdis.1c00296
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: DNA Nanoflower Eye Drops with Antibiotic-Resistant Gene Regulation Ability for MRSA Keratitis Target Treatment.

    Ran, Meixin / Sun, Rong / Yan, Jiaqi / Pulliainen, Arto T / Zhang, Yu / Zhang, Hongbo

    Small (Weinheim an der Bergstrasse, Germany)

    2023  Volume 19, Issue 47, Page(s) e2304194

    Abstract: Methicillin-resistant Staphylococcus aureus (MRSA) biofilm-associated bacterial keratitis is highly intractable, with strong resistance to β-lactam antibiotics. Inhibiting the MRSA resistance gene mecR1 to downregulate penicillin-binding protein PBP2a ... ...

    Abstract Methicillin-resistant Staphylococcus aureus (MRSA) biofilm-associated bacterial keratitis is highly intractable, with strong resistance to β-lactam antibiotics. Inhibiting the MRSA resistance gene mecR1 to downregulate penicillin-binding protein PBP2a has been implicated in the sensitization of β-lactam antibiotics to MRSA. However, oligonucleotide gene regulators struggle to penetrate dense biofilms, let alone achieve efficient gene regulation inside bacteria cells. Herein, an eye-drop system capable of penetrating biofilms and targeting bacteria for chemo-gene therapy in MRSA-caused bacterial keratitis is developed. This system employed rolling circle amplification to prepare DNA nanoflowers (DNFs) encoding MRSA-specific aptamers and mecR1 deoxyribozymes (DNAzymes). Subsequently, β-lactam antibiotic ampicillin (Amp) and zinc oxide (ZnO) nanoparticles are sequentially loaded into the DNFs (ZnO/Amp@DNFs). Upon application, ZnO on the surface of the nanosystem disrupts the dense structure of biofilm and fully exposes free bacteria. Later, bearing encoded aptamer, the nanoflower system is intensively endocytosed by bacteria, and releases DNAzyme under acidic conditions to cleave the mecR1 gene for PBP2a down-regulation, and ampicillin for efficient MRSA elimination. In vivo tests showed that the system effectively cleared bacterial and biofilm in the cornea, suppressed proinflammatory cytokines interleukin 1β （IL-1β） and tumor neocrosis factor-alpha （TNF-α）, and is safe for corneal epithelial cells. Overall, this design offers a promising approach for treating MRSA-induced keratitis.
    MeSH term(s) Humans ; Anti-Bacterial Agents/pharmacology ; Methicillin-Resistant Staphylococcus aureus/genetics ; Zinc Oxide ; DNA/metabolism ; Ampicillin/metabolism ; Ampicillin/pharmacology ; beta-Lactams/metabolism ; beta-Lactams/pharmacology ; Keratitis/drug therapy ; Keratitis/genetics ; Microbial Sensitivity Tests ; Bacterial Proteins/metabolism
    Chemical Substances Anti-Bacterial Agents ; Zinc Oxide (SOI2LOH54Z) ; DNA (9007-49-2) ; Ampicillin (7C782967RD) ; beta-Lactams ; Bacterial Proteins
    Language English
    Publishing date 2023-07-25
    Publishing country Germany
    Document type Journal Article
    ZDB-ID 2168935-0
    ISSN 1613-6829 ; 1613-6810
    ISSN (online) 1613-6829
    ISSN 1613-6810
    DOI 10.1002/smll.202304194
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  5. Article ; Online: Human Peptides α-Defensin-1 and -5 Inhibit Pertussis Toxin.

    Kling, Carolin / Pulliainen, Arto T / Barth, Holger / Ernst, Katharina

    Toxins

    2021  Volume 13, Issue 7

    Abstract: Bordetella ... ...

    Abstract Bordetella pertussis
    MeSH term(s) Animals ; Anti-Infective Agents/pharmacology ; Antimicrobial Peptides ; Bordetella pertussis/metabolism ; Child ; Humans ; Pertussis Toxin/antagonists & inhibitors ; Pertussis Toxin/metabolism ; Virulence Factors, Bordetella ; Whooping Cough ; alpha-Defensins/pharmacology
    Chemical Substances Anti-Infective Agents ; Antimicrobial Peptides ; Virulence Factors, Bordetella ; alpha-Defensins ; human neutrophil peptide 1 ; Pertussis Toxin (EC 2.4.2.31)
    Language English
    Publishing date 2021-07-11
    Publishing country Switzerland
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2518395-3
    ISSN 2072-6651 ; 2072-6651
    ISSN (online) 2072-6651
    ISSN 2072-6651
    DOI 10.3390/toxins13070480
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  6. Article ; Online: Crystal structures of pertussis toxin with NAD

    Sakari, Moona / Tran, Mai T / Rossjohn, Jamie / Pulliainen, Arto T / Beddoe, Travis / Littler, Dene R

    The Journal of biological chemistry

    2022  Volume 298, Issue 5, Page(s) 101892

    Abstract: Bordetella pertussis is the causative agent of whooping cough, a highly contagious respiratory disease. Pertussis toxin (PT), a major virulence factor secreted by B. pertussis, is an AB5-type protein complex topologically related to cholera toxin. The PT ...

    Abstract Bordetella pertussis is the causative agent of whooping cough, a highly contagious respiratory disease. Pertussis toxin (PT), a major virulence factor secreted by B. pertussis, is an AB5-type protein complex topologically related to cholera toxin. The PT protein complex is internalized by host cells and follows a retrograde trafficking route to the endoplasmic reticulum, where it subsequently dissociates. The released enzymatic S1 subunit is then translocated from the endoplasmic reticulum into the cytosol and subsequently ADP-ribosylates the inhibitory alpha-subunits (Gαi) of heterotrimeric G proteins, thus promoting dysregulation of G protein-coupled receptor signaling. However, the mechanistic details of the ADP-ribosylation activity of PT are not well understood. Here, we describe crystal structures of the S1 subunit in complex with nicotinamide adenine dinucleotide (NAD+), with NAD+ hydrolysis products ADP-ribose and nicotinamide, with NAD+ analog PJ34, and with a novel NAD+ analog formed upon S1 subunit crystallization with 3-amino benzamide and NAD+, which we name benzamide amino adenine dinucleotide. These crystal structures provide unprecedented insights into pre- and post-NAD+ hydrolysis steps of the ADP-ribosyltransferase activity of PT. We propose that these data may aid in rational drug design approaches and further development of PT-specific small-molecule inhibitors.
    MeSH term(s) ADP-Ribosylation ; Adenosine Diphosphate Ribose/metabolism ; Bordetella pertussis ; Cytosol/metabolism ; NAD/metabolism ; Pertussis Toxin/chemistry ; Virulence Factors, Bordetella/chemistry
    Chemical Substances Virulence Factors, Bordetella ; NAD (0U46U6E8UK) ; Adenosine Diphosphate Ribose (20762-30-5) ; Pertussis Toxin (EC 2.4.2.31)
    Language English
    Publishing date 2022-04-01
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1016/j.jbc.2022.101892
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    Uc I Zs.108: Show issues Location:
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  7. Article ; Online: Domperidone Inhibits

    Jia, Jinfang / Braune-Yan, Maria / Lietz, Stefanie / Wahba, Mary / Pulliainen, Arto T / Barth, Holger / Ernst, Katharina

    Toxins

    2023  Volume 15, Issue 7

    Abstract: Bordetella ... ...

    Abstract Bordetella pertussis
    MeSH term(s) Animals ; Humans ; Bordetella pertussis/metabolism ; Domperidone/pharmacology ; Botulinum Toxins/toxicity ; Bacterial Toxins/metabolism ; Pertussis Toxin ; ADP Ribose Transferases/metabolism
    Chemical Substances botulinum toxin type C (FPM7829VMX) ; Domperidone (5587267Z69) ; Botulinum Toxins (EC 3.4.24.69) ; Bacterial Toxins ; Pertussis Toxin (EC 2.4.2.31) ; ADP Ribose Transferases (EC 2.4.2.-)
    Language English
    Publishing date 2023-06-25
    Publishing country Switzerland
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2518395-3
    ISSN 2072-6651 ; 2072-6651
    ISSN (online) 2072-6651
    ISSN 2072-6651
    DOI 10.3390/toxins15070412
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  8. Article ; Online: Host poly(ADP-ribose) polymerases (PARPs) in acute and chronic bacterial infections.

    Miettinen, Moona / Vedantham, Madhukar / Pulliainen, Arto T

    Microbes and infection

    2019  Volume 21, Issue 10, Page(s) 423–431

    Abstract: Protein ADP-ribosylation is a reversible post-translational modification, which alters protein activity, localization, interactome or stability, leading to perturbation of cell signaling. This review summarizes the emerging data indicating that host cell ...

    Abstract Protein ADP-ribosylation is a reversible post-translational modification, which alters protein activity, localization, interactome or stability, leading to perturbation of cell signaling. This review summarizes the emerging data indicating that host cell ADP-ribosylating enzymes, poly(ADP-ribose) polymerases (PARPs), influence the course of a bacterial infection, in parallel to ADP-ribosylating bacterial toxins. Host cell PARP targeting could be an efficient therapeutic approach to treat certain bacterial infections, possibly by repurposing the approved or clinical trial PARP inhibitors developed for cancer therapy.
    MeSH term(s) ADP-Ribosylation/drug effects ; Animals ; Bacteria/classification ; Bacteria/metabolism ; Bacterial Infections/drug therapy ; Bacterial Infections/enzymology ; Bacterial Infections/immunology ; Bacterial Infections/metabolism ; Host-Pathogen Interactions/drug effects ; Host-Pathogen Interactions/immunology ; Humans ; Inflammation/drug therapy ; Inflammation/enzymology ; Inflammation/immunology ; Poly(ADP-ribose) Polymerase Inhibitors/pharmacology ; Poly(ADP-ribose) Polymerase Inhibitors/therapeutic use ; Poly(ADP-ribose) Polymerases/immunology ; Poly(ADP-ribose) Polymerases/metabolism ; Signal Transduction/drug effects ; Signal Transduction/immunology
    Chemical Substances Poly(ADP-ribose) Polymerase Inhibitors ; Poly(ADP-ribose) Polymerases (EC 2.4.2.30)
    Language English
    Publishing date 2019-06-15
    Publishing country France
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 1465093-9
    ISSN 1769-714X ; 1286-4579
    ISSN (online) 1769-714X
    ISSN 1286-4579
    DOI 10.1016/j.micinf.2019.06.002
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    Zs.A 5014: Show issues Location:
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  9. Article ; Online: iGIST-A Kinetic Bioassay for Pertussis Toxin Based on Its Effect on Inhibitory GPCR Signaling.

    Paramonov, Valeriy M / Sahlgren, Cecilia / Rivero-Müller, Adolfo / Pulliainen, Arto T

    ACS sensors

    2020  Volume 5, Issue 11, Page(s) 3438–3448

    Abstract: Detection of pertussis toxin (PTX) activity is instrumental for the development and manufacturing of pertussis vaccines. These quality and safety measures require thousands of mice annually. Here, we ... ...

    Abstract Detection of pertussis toxin (PTX) activity is instrumental for the development and manufacturing of pertussis vaccines. These quality and safety measures require thousands of mice annually. Here, we describe
    MeSH term(s) Animals ; Biological Assay ; CHO Cells ; Cricetinae ; Cricetulus ; HEK293 Cells ; Humans ; Mice ; Pertussis Toxin ; Receptors, G-Protein-Coupled/metabolism ; Signal Transduction
    Chemical Substances Receptors, G-Protein-Coupled ; Pertussis Toxin (EC 2.4.2.31)
    Language English
    Publishing date 2020-11-04
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 2379-3694
    ISSN (online) 2379-3694
    DOI 10.1021/acssensors.0c01340
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  10. Article ; Online: Inhibition of Pertussis Toxin by Human α-Defensins-1 and -5: Differential Mechanisms of Action.

    Kling, Carolin / Sommer, Anja / Almeida-Hernandez, Yasser / Rodríguez, Armando / Perez-Erviti, Julio A / Bhadane, Rajendra / Ständker, Ludger / Wiese, Sebastian / Barth, Holger / Pupo-Meriño, Mario / Pulliainen, Arto T / Sánchez-García, Elsa / Ernst, Katharina

    International journal of molecular sciences

    2023  Volume 24, Issue 13

    Abstract: Whooping cough is a severe childhood disease, caused by the ... ...

    Abstract Whooping cough is a severe childhood disease, caused by the bacterium
    MeSH term(s) Humans ; Child ; Pertussis Toxin/pharmacology ; Whooping Cough/microbiology ; Bordetella pertussis ; Proteins ; Cell Line
    Chemical Substances Pertussis Toxin (EC 2.4.2.31) ; Proteins
    Language English
    Publishing date 2023-06-23
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms241310557
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