Projects funded by the NCN


Information on the principal investigator and host institution

Information of the project and the call

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Preparation and characterization of enzymatic activity and crystal structure of phage proteins capable to degrade the bacterial polysaccharides of Klebsiella strains

2015/19/N/NZ1/00014

Keywords:

bacteriophages depolymerase biofilm

Descriptors:

  • NZ1_5: Genetic engineering
  • NZ1_10: Microbiology
  • NZ6_5: Virology

Panel:

NZ1 - Molecular biology, structural biology, biotechnology: molecular biology, structural biology, biotechnology

Host institution :

Uniwersytet Wrocławski, Wydział Nauk Biologicznych

woj. dolnośląskie

Other projects carried out by the institution 

Principal investigator (from the host institution):

Agnieszka Łątka 

Number of co-investigators in the project: 2

Call: PRELUDIUM 10 - announced on 2015-09-15

Amount awarded: 149 760 PLN

Project start date (Y-m-d): 2016-07-11

Project end date (Y-m-d): 2020-01-10

Project duration:: 42 months (the same as in the proposal)

Project status: Project settled

Project description

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Note - project descriptions were prepared by the authors of the applications themselves and placed in the system in an unchanged form.

Information in the final report

  • Publication in academic press/journals (7)
  1. Advantages and limitations of microtiter biofilm assays in the model of antibiofilm activity of Klebsiella phage KP34 and its depolymerase.
    Authors:
    Latka A, Drulis-Kawa Z.
    Academic press:
    Scientific Reports (rok: 2020, tom: 10, strony: 20338), Wydawca: Nature
    Status:
    Published
    DOI:
    10.1038/s41598-020-77198-5. - link to the publication
  2. Capsule-Targeting Depolymerase, Derived from Klebsiella KP36 Phage, as a Tool for the Development of Anti-Virulent Strategy
    Authors:
    Majkowska-Skrobek G, Łątka A, Berisio R, Maciejewska B, Squeglia F, Romano M, Lavigne R, Struve C, Drulis-Kawa Z
    Academic press:
    Viruses (rok: 2016, tom: Dec 1;8(12)., strony: pii: E324.), Wydawca: MDPI
    Status:
    Published
    DOI:
    10.3390/v8120324 - link to the publication
  3. Modeling the Architecture of Depolymerase-Containing Receptor Binding Proteins in Klebsiella Phages
    Authors:
    Latka A, Leiman PG, Drulis-Kawa Z, Briers Y
    Academic press:
    Frontiers in Microbiology (rok: 2019, tom: 10, strony: 2649), Wydawca: Frontiers
    Status:
    Published
    DOI:
    10.3389/fmicb.2019.02649 - link to the publication
  4. Engineering the Modular Receptor-Binding Proteins of Klebsiella Phages Switches Their Capsule Serotype Specificity.
    Authors:
    Latka A, Lemire S, Grimon D, Dams D, Maciejewska B, Lu T, Drulis-Kawa Z, Briers Y.
    Academic press:
    mBio (rok: 2021, tom: 12, strony: e00455-21), Wydawca: ASM Journals
    Status:
    Published
    DOI:
    10.1128/mBio.00455-21. - link to the publication
  5. Phage-Borne Depolymerases Decrease Klebsiella pneumoniae Resistance to Innate Defense Mechanisms.
    Authors:
    Majkowska-Skrobek G, Latka A, Berisio R, Squeglia F, Maciejewska B, Briers Y, Drulis-Kawa Z.
    Academic press:
    Frontiers in Microbiology (rok: 2018, tom: 9, strony: 2517), Wydawca: Frontiers
    Status:
    Published
    DOI:
    10.3389/fmicb.2018.02517 - link to the publication
  6. Bacteriophage-encoded virion-associated enzymes to overcome the carbohydrate barriers during the infection process
    Authors:
    Latka A, Maciejewska B, Majkowska-Skrobek G, Briers Y, Drulis-Kawa Z
    Academic press:
    Applied Microbiology and Biotechnology (rok: 2017, tom: Apr;101(8), strony: 3103-3119), Wydawca: Springer-Nature
    Status:
    Published
    DOI:
    10.1007/s00253-017-8224-6. - link to the publication
  7. Structural and Functional Studies of a Klebsiella Phage Capsule Depolymerase Tailspike: Mechanistic Insights into Capsular Degradation.
    Authors:
    Squeglia F, Maciejewska B, Latka A, Ruggiero A, Briers Y, Drulis-Kawa Z, Berisio R
    Academic press:
    Structure (rok: 2020, tom: 28, strony: 613-624), Wydawca: Cell Press
    Status:
    Published
    DOI:
    10.1016/j.str.2020.04.015. - link to the publication