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Peptidoglycan recycling mediated by an ABC transporter in the plant pathogen Agrobacterium tumefaciens
Umeå University, Faculty of Medicine, Molecular Infection Medicine Sweden (MIMS). Umeå University, Faculty of Medicine, Umeå Centre for Microbial Research (UCMR). Umeå University, Faculty of Medicine, Department of Molecular Biology (Faculty of Medicine).ORCID iD: 0000-0002-6848-5134
Umeå University, Faculty of Medicine, Molecular Infection Medicine Sweden (MIMS). Umeå University, Faculty of Medicine, Umeå Centre for Microbial Research (UCMR). Umeå University, Faculty of Medicine, Department of Molecular Biology (Faculty of Medicine).ORCID iD: 0000-0001-5995-718x
2022 (English)In: Nature Communications, E-ISSN 2041-1723, Vol. 13, no 1, article id 7927Article in journal (Refereed) Published
Abstract [en]

During growth and division, the bacterial cell wall peptidoglycan (PG) is remodelled, resulting in the liberation of PG muropeptides which are typically reinternalized and recycled. Bacteria belonging to the Rhizobiales and Rhodobacterales orders of the Alphaproteobacteria lack the muropeptide transporter AmpG, despite having other key PG recycling enzymes. Here, we show that an alternative transporter, YejBEF-YepA, takes over this role in the Rhizobiales phytopathogen Agrobacterium tumefaciens. Muropeptide import by YejBEF-YepA governs expression of the β-lactamase AmpC in A. tumefaciens, contributing to β-lactam resistance. However, we show that the absence of YejBEF-YepA causes severe cell wall defects that go far beyond lowered AmpC activity. Thus, contrary to previously established Gram-negative models, PG recycling is vital for cell wall integrity in A. tumefaciens. YepA is widespread in the Rhizobiales and Rhodobacterales, suggesting that YejBEF-YepA-mediated PG recycling could represent an important but overlooked aspect of cell wall biology in these bacteria.

Place, publisher, year, edition, pages
Nature Publishing Group, 2022. Vol. 13, no 1, article id 7927
National Category
Microbiology in the medical area
Identifiers
URN: urn:nbn:se:umu:diva-202244DOI: 10.1038/s41467-022-35607-5ISI: 000971044000010PubMedID: 36566216Scopus ID: 2-s2.0-85144637346OAI: oai:DiVA.org:umu-202244DiVA, id: diva2:1724848
Funder
Swedish Research CouncilKnut and Alice Wallenberg FoundationThe Kempe FoundationsAvailable from: 2023-01-09 Created: 2023-01-09 Last updated: 2024-03-20Bibliographically approved
In thesis
1. Studies on cell wall recycling and modification in Gram-negative bacteria
Open this publication in new window or tab >>Studies on cell wall recycling and modification in Gram-negative bacteria
2024 (English)Doctoral thesis, comprehensive summary (Other academic)
Alternative title[sv]
Studier om cellväggsåtervinning och modifiering i gramnegativa bakterier
Abstract [en]

The bacterial cell wall is made from peptidoglycan (PG), a heteropolymer which forms a bag-like exoskeleton that envelopes the cell. PG is constantly remodelled during growth and division, and in response to environmental stimuli. Decades of study of this process have focused largely on a select few model organisms, leaving its diversity poorly understood. In this thesis, I present studies on different aspects of PG recycling and modification in several Gram-negative models, with a particular focus on the plant pathogen Agrobacterium tumefaciens, a model of the Hyphomicrobiales group of the Alphaproteobacteria which includes several species of medical and environmental interest. It is shown that A. tumefaciens encodes a novel PG transporter, which is vital for cell wall integrity and resistance to β- lactam antibiotics, and widely conserved in the Hyphomicrobiales and Rhodobacterales orders. Growth defects caused by the loss of the transporter are suppressed by mutations in a novel glycopolymer, which is hypothesized to play a role in sequestering metal ions and thereby lowering periplasmic oxidative stress. Next, in collaboration, it is shown that PG recycling in the best studied model, Escherichia coli, is more complicated than previously thought. Rather than depending mostly on the MFS-family transporter AmpG, E. coli uses an ABC transporter, MppA-OppBCDF or AmpG depending on the growth phase and conditions. Finally, two studies on modification of PG by deacetylation are presented. First, A. tumefaciens is shown to encode a novel anhydroMurNAc deacetylase, which specifically deacetylates the PG chain termini. Then, it is shown that the causative agent of Legionnaires’ disease, Legionella pneumophila, depends on deacetylation of its PG during infection for defence against host lysozyme and correct polar placement of its type IV secretion system. 

Place, publisher, year, edition, pages
Umeå: Umeå University, 2024. p. 53
Series
Umeå University medical dissertations, ISSN 0346-6612 ; 2300
Keywords
Peptidoglycan recycling, bacterial cell wall, antibiotics, Agrobacterium tumefaciens, Escherichia coli, Legionella pneumophila
National Category
Microbiology
Research subject
Microbiology; Biochemistry
Identifiers
urn:nbn:se:umu:diva-222530 (URN)978-91-8070-295-9 (ISBN)978-91-8070-296-6 (ISBN)
Public defence
2024-04-19, Major Groove, Building 6L, Norrlands Universitetssjukhus, Umeå, 09:00 (English)
Opponent
Supervisors
Note

Number in series missing in publication. 

Available from: 2024-03-28 Created: 2024-03-20 Last updated: 2024-03-21Bibliographically approved

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Gilmore, Michael C.Cava, Felipe

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Molecular Infection Medicine Sweden (MIMS)Umeå Centre for Microbial Research (UCMR)Department of Molecular Biology (Faculty of Medicine)
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