All

What are you looking for?

All
Projects
Results
Organizations

Quick search

  • Projects supported by TA ČR
  • Excellent projects
  • Projects with the highest public support
  • Current projects

Smart search

  • That is how I find a specific +word
  • That is how I leave the -word out of the results
  • “That is how I can find the whole phrase”

A human secretome library screen reveals a role for Peptidoglycan Recognition Protein 1 in Lyme borreliosis.

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60460709%3A41340%2F20%3A85190" target="_blank" >RIV/60460709:41340/20:85190 - isvavai.cz</a>

  • Result on the web

    <a href="https://journals.plos.org/plospathogens/article?id=10.1371/journal.ppat.1009030" target="_blank" >https://journals.plos.org/plospathogens/article?id=10.1371/journal.ppat.1009030</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1371/journal.ppat.1009030" target="_blank" >10.1371/journal.ppat.1009030</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    A human secretome library screen reveals a role for Peptidoglycan Recognition Protein 1 in Lyme borreliosis.

  • Original language description

    Lyme disease, the most common vector borne illness in North America, is caused by the spirochete Borrelia burgdorferi. Infection begins in the skin following a tick bite and can spread to the hearts, joints, nervous system, and other organs. Diverse host responses influence the level of B. burgdorferi infection in mice and humans. Using a systems biology approach, we examined potential molecular interactions between human extracellular and secreted proteins and B. burgdorferi. A yeast display library expressing 1031 human extracellular proteins was probed against 36 isolates of B. burgdorferi sensu lato. We found that human Peptidoglycan Recognition Protein 1 (PGLYRP1) interacted with the vast majority of B. burgdorferi isolates. In subsequent experiments, we demonstrated that recombinant PGLYRP1 interacts with purified B. burgdorferi peptidoglycan and exhibits borreliacidal activity, suggesting that vertebrate hosts may use PGLYRP1 to identify B. burgdorferi. We examined B. burgdorferi infection in

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10606 - Microbiology

Result continuities

  • Project

  • Continuities

    S - Specificky vyzkum na vysokych skolach

Others

  • Publication year

    2020

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    PLoS Pathogens

  • ISSN

    1553-7366

  • e-ISSN

    1553-7374

  • Volume of the periodical

    16

  • Issue of the periodical within the volume

    11

  • Country of publishing house

    CZ - CZECH REPUBLIC

  • Number of pages

    21

  • Pages from-to

    1-21

  • UT code for WoS article

    000592436400001

  • EID of the result in the Scopus database

    2-s2.0-85096083410