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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%2F60077344%3A_____%2F20%3A00537471" target="_blank" >RIV/60077344:_____/20:00537471 - 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 mice lacking PGLYRP1 and observed an increased spirochete burden in the heart and joints, along with splenomegaly. Mice lacking PGLYRP1 also showed signs of immune dysregulation, including lower serum IgG levels and higher levels of IFN gamma, CXCL9, and CXCL10.Taken together, our findings suggest that PGLYRP1 plays a role in the host's response to B. burgdorferi and further demonstrate the utility of expansive yeast display screening in capturing biologically relevant interactions between spirochetes and their hosts.

  • 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

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

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

    1553-7374

  • e-ISSN

  • Volume of the periodical

    16

  • Issue of the periodical within the volume

    11

  • Country of publishing house

    US - UNITED STATES

  • Number of pages

    21

  • Pages from-to

    e1009030

  • UT code for WoS article

    000592436400001

  • EID of the result in the Scopus database

    2-s2.0-85096083410