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A peptidoglycan N-deacetylase specific for anhydroMurNAc chain termini in 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). Academy of Scientific and Innovative Research (AcSIR), Uttar Pradesh, Ghaziabad, India; Regulatory Toxicology Group, CSIR-Indian Institute of Toxicology Research (CSIR-IITR), Uttar Pradesh, Lucknow, India.
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).
Department of Plant Biochemistry, Center of Plant Molecular Biology (ZMBP), Eberhard-Karls-University of Tübingen, Tübingen, Germany.
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2024 (English)In: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 300, no 2, article id 105611Article in journal (Refereed) Published
Abstract [en]

During growth, bacteria remodel and recycle their peptidoglycan (PG). A key family of PG-degrading enzymes is the lytic transglycosylases, which produce anhydromuropeptides, a modification that caps the PG chains and contributes to bacterial virulence. Previously, it was reported that the polar-growing Gram-negative plant pathogen Agrobacterium tumefaciens lacks anhydromuropeptides. Here, we report the identification of an enzyme, MdaA (MurNAc deacetylase A), which specifically removes the acetyl group from anhydromuropeptide chain termini in A. tumefaciens, resolving this apparent anomaly. A. tumefaciens lacking MdaA accumulates canonical anhydromuropeptides, whereas MdaA was able to deacetylate anhydro-N-acetyl muramic acid in purified sacculi that lack this modification. As for other PG deacetylases, MdaA belongs to the CE4 family of carbohydrate esterases but harbors an unusual Cys residue in its active site. MdaA is conserved in other polar-growing bacteria, suggesting a possible link between PG chain terminus deacetylation and polar growth.

Place, publisher, year, edition, pages
Elsevier, 2024. Vol. 300, no 2, article id 105611
Keywords [en]
Agrobacterium tumefaciens, anhydromuropeptide, deacetylase, lytic transglycosylase, peptidoglycan
National Category
Microbiology Microbiology in the medical area
Identifiers
URN: urn:nbn:se:umu:diva-220439DOI: 10.1016/j.jbc.2023.105611PubMedID: 38159848Scopus ID: 2-s2.0-85183154845OAI: oai:DiVA.org:umu-220439DiVA, id: diva2:1835850
Funder
Swedish Research CouncilKnut and Alice Wallenberg FoundationThe Kempe FoundationsAvailable from: 2024-02-07 Created: 2024-02-07 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)
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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.Yadav, Akhilesh K.Espaillat, AkbarCava, Felipe

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Gilmore, Michael C.Yadav, Akhilesh K.Espaillat, AkbarCava, 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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