SwePub
Sök i LIBRIS databas

  Utökad sökning

id:"swepub:oai:DiVA.org:umu-209548"
 

Sökning: id:"swepub:oai:DiVA.org:umu-209548" > Peptidoglycan deace...

  • Boamah, DavidDepartment of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, United States (författare)

Peptidoglycan deacetylation controls type IV secretion and the intracellular survival of the bacterial pathogen Legionella pneumophila

  • Artikel/kapitelEngelska2023

Förlag, utgivningsår, omfång ...

  • Proceedings of the National Academy of Sciences (PNAS),2023
  • electronicrdacarrier

Nummerbeteckningar

  • LIBRIS-ID:oai:DiVA.org:umu-209548
  • https://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-209548URI
  • https://doi.org/10.1073/pnas.2119658120DOI

Kompletterande språkuppgifter

  • Språk:engelska
  • Sammanfattning på:engelska

Ingår i deldatabas

Klassifikation

  • Ämneskategori:ref swepub-contenttype
  • Ämneskategori:art swepub-publicationtype

Anmärkningar

  • Peptidoglycan is a critical component of the bacteria cell envelope. Remodeling of the peptidoglycan is required for numerous essential cellular processes and has been linked to bacterial pathogenesis. Peptidoglycan deacetylases that remove the acetyl group of the N-acetylglucosamine (NAG) subunit protect bacterial pathogens from immune recognition and digestive enzymes secreted at the site of infection. However, the full extent of this modification on bacterial physiology and pathogenesis is not known. Here, we identify a polysaccharide deacetylase of the intracellular bacterial pathogen Legionella pneumophila and define a two-tiered role for this enzyme in Legionella pathogenesis. First, NAG deacetylation is important for the proper localization and function of the Type IVb secretion system, linking peptidoglycan editing to the modulation of host cellular processes through the action of secreted virulence factors. As a consequence, the Legionella vacuole mis-traffics along the endocytic pathway to the lysosome, preventing the formation of a replication permissive compartment. Second, within the lysosome, the inability to deacetylate the peptidoglycan renders the bacteria more sensitive to lysozyme-mediated degradation, resulting in increased bacterial death. Thus, the ability to deacetylate NAG is important for bacteria to persist within host cells and in turn, Legionella virulence. Collectively, these results expand the function of peptidoglycan deacetylases in bacteria, linking peptidoglycan editing, Type IV secretion, and the intracellular fate of a bacterial pathogen.

Ämnesord och genrebeteckningar

Biuppslag (personer, institutioner, konferenser, titlar ...)

  • Gilmore, Michael C.Umeå universitet,Molekylär Infektionsmedicin, Sverige (MIMS),Umeå Centre for Microbial Research (UCMR),Institutionen för molekylärbiologi (Medicinska fakulteten)(Swepub:umu)migi0012 (författare)
  • Bourget, SarahDepartment of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, United States (författare)
  • Ghosh, AnushkaDepartment of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, United States (författare)
  • Hossain, Mohammad J.Department of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, United States (författare)
  • Vogel, Joseph P.Department of Molecular Microbiology, Washington University School of Medicine, St. Louis, United States (författare)
  • Cava, FelipeUmeå universitet,Molekylär Infektionsmedicin, Sverige (MIMS),Umeå Centre for Microbial Research (UCMR),Institutionen för molekylärbiologi (Medicinska fakulteten)(Swepub:umu)feca0003 (författare)
  • O'Connor, Tamara J.Department of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, United States (författare)
  • Department of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, United StatesMolekylär Infektionsmedicin, Sverige (MIMS) (creator_code:org_t)

Sammanhörande titlar

  • Ingår i:Proceedings of the National Academy of Sciences of the United States of America: Proceedings of the National Academy of Sciences (PNAS)120:230027-84241091-6490

Internetlänk

Hitta via bibliotek

Till lärosätets databas

Kungliga biblioteket hanterar dina personuppgifter i enlighet med EU:s dataskyddsförordning (2018), GDPR. Läs mer om hur det funkar här.
Så här hanterar KB dina uppgifter vid användning av denna tjänst.

 
pil uppåt Stäng

Kopiera och spara länken för att återkomma till aktuell vy