Umeå University's logo

umu.sePublications
Change search
Link to record
Permanent link

Direct link
Publications (10 of 150) Show all publications
Vaidya, S., Saha, D., Rode, D. K. H., Torrens, G., Hansen, M. F., Singh, P. K., . . . Drescher, K. (2025). Bacteria use exogenous peptidoglycan as a danger signal to trigger biofilm formation. Nature Microbiology, 10(1), 144-157
Open this publication in new window or tab >>Bacteria use exogenous peptidoglycan as a danger signal to trigger biofilm formation
Show others...
2025 (English)In: Nature Microbiology, E-ISSN 2058-5276, Vol. 10, no 1, p. 144-157Article in journal (Refereed) Published
Abstract [en]

For any organism, survival is enhanced by the ability to sense and respond to threats in advance. For bacteria, danger sensing among kin cells has been observed, but the presence or impacts of general danger signals are poorly understood. Here we show that different bacterial species use exogenous peptidoglycan fragments, which are released by nearby kin or non-kin cell lysis, as a general danger signal. Using microscopy and gene expression profiling of Vibrio cholerae, we find that even brief signal exposure results in a regulatory response that causes three-dimensional biofilm formation, which protects cells from a broad range of stresses, including bacteriophage predation. A diverse set of species (Pseudomonas aeruginosa, Acinetobacter baumannii, Staphylococcus aureus, Enterococcus faecalis) also respond to exogenous peptidoglycan by forming biofilms. As peptidoglycan from different Gram-negative and Gram-positive species triggered three-dimensional biofilm formation, we propose that this danger signal and danger response are conserved among bacteria.

Place, publisher, year, edition, pages
Springer Nature, 2025
National Category
Microbiology in the medical area
Identifiers
urn:nbn:se:umu:diva-234005 (URN)10.1038/s41564-024-01886-5 (DOI)001388924600001 ()39753671 (PubMedID)2-s2.0-85213967811 (Scopus ID)
Funder
EU, Horizon 2020, 716734Swedish Research CouncilKnut and Alice Wallenberg FoundationSwedish Cancer SocietyThe Kempe Foundations
Available from: 2025-01-14 Created: 2025-01-14 Last updated: 2025-01-14Bibliographically approved
Pulido-Sánchez, M., Leal-Morales, A., López-Sánchez, A., Cava, F. & Govantes, F. (2025). Spatial, temporal and numerical regulation of polar flagella assembly in Pseudomonas putida. Microbiological Research, 292, Article ID 128033.
Open this publication in new window or tab >>Spatial, temporal and numerical regulation of polar flagella assembly in Pseudomonas putida
Show others...
2025 (English)In: Microbiological Research, ISSN 0944-5013, E-ISSN 1618-0623, Vol. 292, article id 128033Article in journal (Refereed) Published
Abstract [en]

The Gram-negative bacterium Pseudomonas putida bears a tuft of flagella at a single cell pole. New flagella must be assembled de novo every cell cycle to secure motility of both daughter cells. Here we show that the coordinated action of FimV, FlhF and FleN sets the location, timing and number of flagella assembled. The polar landmark proteins FimV and FlhF are independently targeted to the nascent new pole during or shortly after cell division, but FimV stabilizes FlhF association with the cell poles. FlhF determines the polar position of the flagella by targeting early flagellar components to the cell pole and preventing their nucleation at non-polar sites. FlhF also promotes efficient flagellar assembly and indirectly stimulates Class III flagellar promoter activation by promoting secretion of the anti-FliA anti-σ factor FlgM. The MinD-like ATPase FleN partitions between the cell poles and the cytoplasm. Cytoplasmic FleN regulates flagellar number by preventing excessive accumulation of FlhF at the cell poles that may otherwise lead to hyperflagellation, likely by antagonizing FleQ-dependent transcriptional activation. FimV is essential to FleN polar location. FimV and FleN temporally regulate the onset of flagellar assembly by preventing premature polar targeting of FlhF and the ensuing premature targeting of additional flagellar components. Our results shed new light on the mechanisms that ensure the timely assembly of the appropriate number of flagella at the correct polar location in polarly flagellated bacteria.

Place, publisher, year, edition, pages
Elsevier, 2025
Keywords
FimV, Flagella, FleN, FlhF, Polar landmark proteins, Pseudomonas
National Category
Microbiology
Identifiers
urn:nbn:se:umu:diva-233380 (URN)10.1016/j.micres.2024.128033 (DOI)2-s2.0-85212559942 (Scopus ID)
Available from: 2025-01-09 Created: 2025-01-09 Last updated: 2025-01-09Bibliographically approved
Sen, B. C., Mavi, P. S., Irazoki, O., Datta, S., Kaiser, S., Cava, F. & Flärdh, K. (2024). A dispensable SepIVA orthologue in Streptomyces venezuelae is associated with polar growth and not cell division. BMC Microbiology, 24(1), Article ID 481.
Open this publication in new window or tab >>A dispensable SepIVA orthologue in Streptomyces venezuelae is associated with polar growth and not cell division
Show others...
2024 (English)In: BMC Microbiology, E-ISSN 1471-2180, Vol. 24, no 1, article id 481Article in journal (Refereed) Published
Abstract [en]

Background: SepIVA has been reported to be an essential septation factor in Mycolicibacterium smegmatis and Mycobacterium tuberculosis. It is a coiled-coil protein with similarity to DivIVA, a protein necessary for polar growth in members of the phylum Actinomycetota. Orthologues of SepIVA are broadly distributed among actinomycetes, including in Streptomyces spp.

Results: To clarify the role of SepIVA and its potential involvement in cell division in streptomycetes, we generated sepIVA deletion mutants in Streptomyces venezuelae and found that sepIVA is dispensable for growth, cell division and sporulation. Further, mNeonGreen-SepIVA fusion protein did not localize at division septa, and we found no evidence of involvement of SepIVA in cell division. Instead, mNeonGreen-SepIVA was accumulated at the tips of growing vegetative hyphae in ways reminiscent of the apical localization of polarisome components like DivIVA. Bacterial two-hybrid system analyses revealed an interaction between SepIVA and DivIVA. The results indicate that SepIVA is associated with polar growth. However, no phenotypic effects of sepIVA deletion could be detected, and no evidence was observed of redundancy with the other DivIVA-like coiled-coil proteins Scy and FilP that are also associated with apical growth in streptomycetes.

Conclusions: We conclude that S. venezuelae SepIVA, in contrast to the situation in mycobacteria, is dispensable for growth and viability. The results suggest that it is associated with polar growth rather than septum formation.

Place, publisher, year, edition, pages
BioMed Central (BMC), 2024
Keywords
Cell division, Cell wall synthesis, FtsZ, Polar growth, Streptomyces
National Category
Microbiology
Identifiers
urn:nbn:se:umu:diva-232277 (URN)10.1186/s12866-024-03625-6 (DOI)2-s2.0-85209567520 (Scopus ID)
Funder
Sven och Lilly Lawskis fond för naturvetenskaplig forskningCarl Tryggers foundation Swedish Research Council, 2015-05452Swedish Research Council, 2019-04643Swedish Research Council, 2018-02823Swedish Research Council, 2018-05882Knut and Alice Wallenberg FoundationThe Kempe Foundations, SMK2062
Available from: 2024-11-28 Created: 2024-11-28 Last updated: 2024-11-28Bibliographically approved
Espaillat, A., Alvarez, L., Torrens, G., ter Beek, J., Miguel-Ruano, V., Irazoki, O., . . . Cava, F. (2024). A distinctive family of L,D-transpeptidases catalyzing L-Ala-mDAP crosslinks in Alpha- and Betaproteobacteria. Nature Communications, 15(1), Article ID 1343.
Open this publication in new window or tab >>A distinctive family of L,D-transpeptidases catalyzing L-Ala-mDAP crosslinks in Alpha- and Betaproteobacteria
Show others...
2024 (English)In: Nature Communications, E-ISSN 2041-1723, Vol. 15, no 1, article id 1343Article in journal (Refereed) Published
Abstract [en]

The bacterial cell-wall peptidoglycan is made of glycan strands crosslinked by short peptide stems. Crosslinks are catalyzed by DD-transpeptidases (4,3-crosslinks) and LD-transpeptidases (3,3-crosslinks). However, recent research on non-model species has revealed novel crosslink types, suggesting the existence of uncharacterized enzymes. Here, we identify an LD-transpeptidase, LDTGo, that generates 1,3-crosslinks in the acetic-acid bacterium Gluconobacter oxydans. LDTGo-like proteins are found in Alpha- and Betaproteobacteria lacking LD3,3-transpeptidases. In contrast with the strict specificity of typical LD- and DD-transpeptidases, LDTGo can use non-terminal amino acid moieties for crosslinking. A high-resolution crystal structure of LDTGo reveals unique features when compared to LD3,3-transpeptidases, including a proline-rich region that appears to limit substrate access, and a cavity accommodating both glycan chain and peptide stem from donor muropeptides. Finally, we show that DD-crosslink turnover is involved in supplying the necessary substrate for LD1,3-transpeptidation. This phenomenon underscores the interplay between distinct crosslinking mechanisms in maintaining cell wall integrity in G. oxydans.

Place, publisher, year, edition, pages
Springer Nature, 2024
National Category
Biochemistry and Molecular Biology
Identifiers
urn:nbn:se:umu:diva-221654 (URN)10.1038/s41467-024-45620-5 (DOI)38351082 (PubMedID)2-s2.0-85185130975 (Scopus ID)
Funder
Swedish Research Council, 2018- 02823Swedish Research Council, 2018-05882The Kempe Foundations, SMK2062Knut and Alice Wallenberg FoundationSwedish Research Council, 2018-07152Swedish Research Council, 2016-03599Swedish Research Council Formas, 2019- 02496The Kempe Foundations, SMK-1762The Kempe Foundations, SMK-1869
Available from: 2024-03-04 Created: 2024-03-04 Last updated: 2024-07-12Bibliographically approved
Gilmore, M. C., Yadav, A. K., Espaillat, A., Gust, A. A., Williams, M. A., Brown, P. J. .. & Cava, F. (2024). A peptidoglycan N-deacetylase specific for anhydroMurNAc chain termini in Agrobacterium tumefaciens. Journal of Biological Chemistry, 300(2), Article ID 105611.
Open this publication in new window or tab >>A peptidoglycan N-deacetylase specific for anhydroMurNAc chain termini in Agrobacterium tumefaciens
Show others...
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
Keywords
Agrobacterium tumefaciens, anhydromuropeptide, deacetylase, lytic transglycosylase, peptidoglycan
National Category
Microbiology Microbiology in the medical area
Identifiers
urn:nbn:se:umu:diva-220439 (URN)10.1016/j.jbc.2023.105611 (DOI)38159848 (PubMedID)2-s2.0-85183154845 (Scopus ID)
Funder
Swedish Research CouncilKnut and Alice Wallenberg FoundationThe Kempe Foundations
Available from: 2024-02-07 Created: 2024-02-07 Last updated: 2024-03-20Bibliographically approved
Gyger, J., Torrens, G., Cava, F., Bernhardt, T. G. & Fumeaux, C. (2024). A potential space-making role in cell wall biogenesis for SltB1and DacB revealed by a beta-lactamase induction phenotype in Pseudomonas aeruginosa. mBio, 15(7), Article ID e0141924.
Open this publication in new window or tab >>A potential space-making role in cell wall biogenesis for SltB1and DacB revealed by a beta-lactamase induction phenotype in Pseudomonas aeruginosa
Show others...
2024 (English)In: mBio, ISSN 2161-2129, E-ISSN 2150-7511, Vol. 15, no 7, article id e0141924Article in journal (Refereed) Published
Abstract [en]

Pseudomonas aeruginosa encodes the beta-lactamase AmpC, which promotes resistance to beta-lactam antibiotics. Expression of ampC is induced by anhydro-muropeptides (AMPs) released from the peptidoglycan (PG) cell wall upon beta-lactam treatment. AmpC can also be induced via genetic inactivation of PG biogenesis factors such as the endopeptidase DacB that cleaves PG crosslinks. Mutants in dacB occur in beta-lactam-resistant clinical isolates of P. aeruginosa, but it has remained unclear why DacB inactivation promotes ampC induction. Similarly, the inactivation of lytic transglycosylase (LT) enzymes such as SltB1 that cut PG glycans has also been associated with ampC induction and beta-lactam resistance. Given that LT enzymes are capable of producing AMP products that serve as ampC inducers, this latter observation has been especially difficult to explain. Here, we show that ampC induction in sltB1 or dacB mutants requires another LT enzyme called MltG. In Escherichia coli, MltG has been implicated in the degradation of nascent PG strands produced upon beta-lactam treatment. Accordingly, in P. aeruginosa sltB1 and dacB mutants, we detected the MltG-dependent production of pentapeptide-containing AMP products that are signatures of nascent PG degradation. Our results therefore support a model in which SltB1 and DacB use their PG-cleaving activity to open space in the PG matrix for the insertion of new material. Thus, their inactivation mimics low-level beta-lactam treatment by reducing the efficiency of new PG insertion into the wall, causing the degradation of some nascent PG material by MltG to produce the ampC-inducing signal.

IMPORTANCE: Inducible beta-lactamases like the ampC system of Pseudomonas aeruginosa are a common determinant of beta-lactam resistance among gram-negative bacteria. The regulation of ampC is elegantly tuned to detect defects in cell wall synthesis caused by beta-lactam drugs. Studies of mutations causing ampC induction in the absence of drug therefore promise to reveal new insights into the process of cell wall biogenesis in addition to aiding our understanding of how resistance to beta-lactam antibiotics arises in the clinic. In this study, the ampC induction phenotype for mutants lacking a glycan-cleaving enzyme or an enzyme that cuts cell wall crosslinks was used to uncover a potential role for these enzymes in making space in the wall matrix for the insertion of new material during cell growth.

Place, publisher, year, edition, pages
American Society for Microbiology, 2024
Keywords
beta-lactamases, lytic transglycosylase, penicillin resistance, peptidoglycan
National Category
Microbiology in the medical area
Identifiers
urn:nbn:se:umu:diva-228076 (URN)10.1128/mbio.01419-24 (DOI)001255064300001 ()38920394 (PubMedID)2-s2.0-85199125682 (Scopus ID)
Funder
NIH (National Institutes of Health), R01AI083365NIH (National Institutes of Health), U19AI158028
Available from: 2024-07-30 Created: 2024-07-30 Last updated: 2024-07-30Bibliographically approved
Gilmore, M. C. & Cava, F. (2024). Bacterial peptidoglycan recycling. Trends in Microbiology
Open this publication in new window or tab >>Bacterial peptidoglycan recycling
2024 (English)In: Trends in Microbiology, ISSN 0966-842X, E-ISSN 1878-4380Article, review/survey (Refereed) Epub ahead of print
Abstract [en]

During growth and division, the bacterial cell wall is remodeled, resulting in the liberation of peptidoglycan (PG) fragments which are typically reinternalized and recycled. Recycling of PG has been studied in a few model species, but its importance and diversity are not yet well understood. Here, we review how bacteria transport and recycle the components of their PG, highlighting updates and new findings.

Place, publisher, year, edition, pages
Elsevier, 2024
Keywords
bacterial cell wall, GlcNAc, MurNAc, muropeptide, peptidoglycan recycling
National Category
Microbiology in the medical area Microbiology
Identifiers
urn:nbn:se:umu:diva-232802 (URN)10.1016/j.tim.2024.11.004 (DOI)2-s2.0-85210751421 (Scopus ID)
Funder
Swedish Research CouncilUmeå UniversityKnut and Alice Wallenberg FoundationThe Kempe Foundations
Available from: 2024-12-10 Created: 2024-12-10 Last updated: 2025-01-10
Delerue, T., Updegrove, T. B., Chareyre, S., Anantharaman, V., Gilmore, M. C., Jenkins, L. M., . . . Ramamurthi, K. S. (2024). Bacterial spore surface nanoenvironment requires a AAA+ ATPase to promote MurG function. Proceedings of the National Academy of Sciences of the United States of America, 121(43), Article ID e2414737121.
Open this publication in new window or tab >>Bacterial spore surface nanoenvironment requires a AAA+ ATPase to promote MurG function
Show others...
2024 (English)In: Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, E-ISSN 1091-6490, Vol. 121, no 43, article id e2414737121Article in journal (Refereed) Published
Abstract [en]

Bacillus subtilis spores are produced inside the cytosol of a mother cell. Spore surface assembly requires the SpoVK protein in the mother cell, but its function is unknown. Here, we report that SpoVK is a sporulation-specific, forespore-localized putative chaperone from a distinct higher-order clade of AAA+ ATPases that promotes the peptidoglycan glycosyltransferase activity of MurG during sporulation, even though MurG does not normally require activation during vegetative growth. MurG redeploys to the forespore surface during sporulation, where we show that the local pH is reduced and propose that this change in cytosolic nanoenvironment abrogates MurG function. Further, we show that SpoVK participates in a developmental checkpoint in which improper spore surface assembly mis-localizes SpoVK, which leads to sporulation arrest. The AAA+ ATPase clade containing SpoVK includes specialized chaperones involved in secretion, cell envelope biosynthesis, and carbohydrate metabolism, suggesting that such fine-tuning might be a widespread feature of different subcellular nanoenvironments.

Place, publisher, year, edition, pages
Proceedings of the National Academy of Sciences (PNAS), 2024
Keywords
ClpXP, HSP90, SpoIVA, spores, SpoVID
National Category
Microbiology
Identifiers
urn:nbn:se:umu:diva-231125 (URN)10.1073/pnas.2414737121 (DOI)39405354 (PubMedID)2-s2.0-85206528128 (Scopus ID)
Funder
Swedish Research CouncilKnut and Alice Wallenberg FoundationThe Kempe Foundations
Available from: 2024-11-01 Created: 2024-11-01 Last updated: 2024-11-01Bibliographically approved
Sun, W.-S., Torrens, G., ter Beek, J., Cava, F. & Berntsson, R.-A. P. A. (2024). Breaking barriers: pCF10 type 4 secretion system relies on a self-regulating muramidase to modulate the cell wall. mBio, 15(8), Article ID e00488-24.
Open this publication in new window or tab >>Breaking barriers: pCF10 type 4 secretion system relies on a self-regulating muramidase to modulate the cell wall
Show others...
2024 (English)In: mBio, ISSN 2161-2129, E-ISSN 2150-7511, Vol. 15, no 8, article id e00488-24Article in journal (Refereed) Published
Abstract [en]

Conjugative type 4 secretion systems (T4SSs) are the main driver for the spread of antibiotic resistance genes and virulence factors in bacteria. To deliver the DNA substrate to recipient cells, it must cross the cell envelopes of both donor and recipient bacteria. In the T4SS from the enterococcal conjugative plasmid pCF10, PrgK is known to be the active cell wall degrading enzyme. It has three predicted extracellular hydrolase domains: metallo-peptidase (LytM), soluble lytic transglycosylase (SLT), and cysteine, histidine-dependent amidohydrolases/peptidases (CHAP). Here, we report the structure of the LytM domain and show that its active site is degenerate and lacks the active site metal. Furthermore, we show that only the predicted SLT domain is functional in vitro and that it unexpectedly has a muramidase instead of a lytic transglycosylase activity. While we did not observe any peptidoglycan hydrolytic activity for the LytM or CHAP domain, we found that these domains downregulated the SLT muramidase activity. The CHAP domain was also found to be involved in PrgK dimer formation. Furthermore, we show that PrgK interacts with PrgL, which likely targets PrgK to the rest of the T4SS. The presented data provides important information for understanding the function of Gram-positive T4SSs.

IMPORTANCE: Antibiotic resistance is a large threat to human health and is getting more prevalent. One of the major contributors to the spread of antibiotic resistance among different bacteria is type 4 secretion systems (T4SS). However, mainly T4SSs from Gram-negative bacteria have been studied in detail. T4SSs from Gram-positive bacteria, which stand for more than half of all hospital-acquired infections, are much less understood. The significance of our research is in identifying the function and regulation of a cell wall hydrolase, a key component of the pCF10 T4SS from Enterococcus faecalis. This system is one of the best-studied Gram-positive T4SSs, and this added knowledge aids in our understanding of horizontal gene transfer in E. faecalis as well as other medically relevant Gram-positive bacteria. Antibiotic resistance is a large threat to human health and is getting more prevalent. One of the major contributors to the spread of antibiotic resistance among different bacteria is type 4 secretion systems (T4SS). However, mainly T4SSs from Gram-negative bacteria have been studied in detail. T4SSs from Gram-positive bacteria, which stand for more than half of all hospital-acquired infections, are much less understood. The significance of our research is in identifying the function and regulation of a cell wall hydrolase, a key component of the pCF10 T4SS from Enterococcus faecalis. This system is one of the best-studied Gram-positive T4SSs, and this added knowledge aids in our understanding of horizontal gene transfer in E. faecalis as well as other medically relevant Gram-positive bacteria.

Place, publisher, year, edition, pages
American Society for Microbiology, 2024
Keywords
Type 4 Secretion System, cell wall, Gram-positive bacteria, pCF10, integrated structural biology
National Category
Microbiology in the medical area
Identifiers
urn:nbn:se:umu:diva-228675 (URN)10.1128/mbio.00488-24 (DOI)001257304300001 ()38940556 (PubMedID)2-s2.0-85201326237 (Scopus ID)
Funder
Swedish Research Council, 2016-03599Swedish Research Council, 2023-02423Swedish Research Council, 2018-02823Swedish Research Council, 2018-05882The Kempe Foundations, SMK-1762The Kempe Foundations, SMK-1869The Kempe Foundations, SMK-2062Knut and Alice Wallenberg FoundationSwedish Research Council, 2018-07152Vinnova, 2018-04969Swedish Research Council Formas, 2019-02496European Commission
Available from: 2024-08-21 Created: 2024-08-21 Last updated: 2025-01-10Bibliographically approved
Alvarez, L., Hernandez, S. B., Torrens, G., Weaver, A. I., Dörr, T. & Cava, F. (2024). Control of bacterial cell wall autolysins by peptidoglycan crosslinking mode. Nature Communications, 15(1), Article ID 7937.
Open this publication in new window or tab >>Control of bacterial cell wall autolysins by peptidoglycan crosslinking mode
Show others...
2024 (English)In: Nature Communications, E-ISSN 2041-1723, Vol. 15, no 1, article id 7937Article in journal (Refereed) Published
Abstract [en]

To withstand their internal turgor pressure and external threats, most bacteria have a protective peptidoglycan (PG) cell wall. The growth of this PG polymer relies on autolysins, enzymes that create space within the structure. Despite extensive research, the regulatory mechanisms governing these PG-degrading enzymes remain poorly understood. Here, we unveil a novel and widespread control mechanism of lytic transglycosylases (LTs), a type of autolysin responsible for breaking down PG glycan chains. Specifically, we show that LD-crosslinks within the PG sacculus act as an inhibitor of LT activity. Moreover, we demonstrate that this regulation controls the release of immunogenic PG fragments and provides resistance against predatory LTs of both bacterial and viral origin. Our findings address a critical gap in understanding the physiological role of the LD-crosslinking mode in PG homeostasis, highlighting how bacteria can enhance their resilience against environmental threats, including phage attacks, through a single structural PG modification.

Place, publisher, year, edition, pages
Springer Nature, 2024
National Category
Microbiology in the medical area Microbiology
Identifiers
urn:nbn:se:umu:diva-229655 (URN)10.1038/s41467-024-52325-2 (DOI)2-s2.0-85203548709 (Scopus ID)
Funder
Swedish Research CouncilKnut and Alice Wallenberg FoundationUmeå UniversityNIH (National Institutes of Health), R01GM130971
Available from: 2024-09-16 Created: 2024-09-16 Last updated: 2024-09-16Bibliographically approved
Projects
Peptidoglycan diversity and plasticity in bacteria [2013-02440_VR]; Umeå UniversityDismantling lipid rafts in Staphylococcus aureus to inhibit MRSA antibiotic resistance [2018-05882_VR]; Umeå UniversityWhat governs cell wall homeostasis in Bacteria? [2018-02823_VR]; Umeå University
Organisations
Identifiers
ORCID iD: ORCID iD iconorcid.org/0000-0001-5995-718x

Search in DiVA

Show all publications