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Jacquier, N., Yadav, A. K., Pillonel, T., Viollier, P. H., Cava, F. & Greub, G. (2019). A SpoIID Homolog Cleaves Glycan Strands at the Chlamydial Division Septum. mBio, 10(4), Article ID e01128-19.
Öppna denna publikation i ny flik eller fönster >>A SpoIID Homolog Cleaves Glycan Strands at the Chlamydial Division Septum
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2019 (Engelska)Ingår i: mBio, ISSN 2161-2129, E-ISSN 2150-7511, Vol. 10, nr 4, artikel-id e01128-19Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

Chlamydiales species are obligate intracellular bacteria lacking a classical peptidoglycan sacculus but relying on peptidoglycan synthesis for cytokinesis. While septal peptidoglycan biosynthesis seems to be regulated by MreB actin and its membrane anchor RodZ rather than FtsZ tubulin in Chlamydiales, the mechanism of peptidoglycan remodeling is poorly understood. An amidase conserved in Chlamydiales is able to cleave peptide stems in peptidoglycan, but it is not clear how peptidoglycan glycan strands are cleaved since no classical lytic transglycosylase is encoded in chlamydial genomes. However, a protein containing a SpoIID domain, known to possess transglycosylase activity in Bacillus subtilis, is conserved in Chiamydiales. We show here that the SpoIID homologue of the Chlamydia-related pathogen Waddlia chondrophila is a septal peptidoglycan-binding protein. Moreover, we demonstrate that SpoIID acts as a lytic transglycosylase on peptidoglycan and as a muramidase on denuded glycan strands in vitro. As SpoIID-like proteins are widespread in nonsporulating bacteria, SpoIID might commonly be a septal peptidoglycan remodeling protein in bacteria, including obligate intracellular pathogens, and thus might represent a promising drug target. IMPORTANCE Chlamydiales species are obligate intracellular bacteria and important human pathogens that have a minimal division machinery lacking the proteins that are essential for bacterial division in other species, such as FtsZ. Chlamydial division requires synthesis of peptidoglycan, which forms a ring at the division septum and is rapidly turned over. However, little is known of peptidoglycan degradation, because many peptidoglycan-degrading enzymes are not encoded by chlamydial genomes. Here we show that an homologue of SpoIID, a peptidoglycan-degrading enzyme involved in sporulation of bacteria such as Bacillus subtilis, is expressed in Chlamydiales, localizes at the division septum, and degrades peptidoglycan in vitro, indicating that SpoIID is not only involved in sporulation but also likely implicated in division of some bacteria.

Ort, förlag, år, upplaga, sidor
American Society for Microbiology (ASM), 2019
Nyckelord
Chlamydiales, Waddlia chondrophila, cell division, peptidoglycan, sporulation
Nationell ämneskategori
Mikrobiologi inom det medicinska området
Identifikatorer
urn:nbn:se:umu:diva-162887 (URN)10.1128/mBio.01128-19 (DOI)000481617000036 ()31311880 (PubMedID)
Tillgänglig från: 2019-09-04 Skapad: 2019-09-04 Senast uppdaterad: 2019-09-04Bibliografiskt granskad
Fleurie, A., Zoued, A., Alvarez, L., Hines, K. M., Cava, F., Xu, L., . . . Waldor, M. K. (2019). A Vibrio cholerae BolA-Like Protein Is Required for Proper Cell Shape and Cell Envelope Integrity. mBio, 10(4), Article ID e00790-19.
Öppna denna publikation i ny flik eller fönster >>A Vibrio cholerae BolA-Like Protein Is Required for Proper Cell Shape and Cell Envelope Integrity
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2019 (Engelska)Ingår i: mBio, ISSN 2161-2129, E-ISSN 2150-7511, Vol. 10, nr 4, artikel-id e00790-19Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

BolA family proteins are conserved in Gram-negative bacteria and many eukaryotes. While diverse cellular phenotypes have been linked to this protein family, the molecular pathways through which these proteins mediate their effects are not well described. Here, we investigated the roles of BolA family proteins in Vibrio cholerae, the cholera pathogen. Like Escherichia coli, V. cholerae encodes two BolA proteins, BolA and IbaG. However, in marked contrast to E. coli, where bolA is linked to cell shape and ibaG is not, in V. cholerae, bolA mutants lack morphological defects, whereas ibaG proved critical for the generation and/or maintenance of the pathogen's morphology. Notably, the bizarre-shaped, multipolar, elongated, and wide cells that predominated in exponential-phase Delta ibaG V. cholerae cultures were not observed in stationary-phase cultures. The V. cholerae Delta ibaG mutant exhibited increased sensitivity to cell envelope stressors, including cell wall-acting antibiotics and bile, and was defective in intestinal colonization. Delta ibaG V. cholerae had reduced peptidoglycan and lipid II and altered outer membrane lipids, likely contributing to the mutant's morphological defects and sensitivity to envelope stressors. Transposon insertion sequencing analysis of ibaG's genetic interactions suggested that ibaG is involved in several processes involved in the generation and homeostasis of the cell envelope. Furthermore, copurification studies revealed that IbaG interacts with proteins containing iron-sulfur clusters or involved in their assembly. Collectively, our findings suggest that V. cholerae IbaG controls cell morphology and cell envelope integrity through its role in biogenesis or trafficking of iron-sulfur cluster proteins. IMPORTANCE BolA-like proteins are conserved across prokaryotes and eukaryotes. These proteins have been linked to a variety of phenotypes, but the pathways and mechanisms through which they act have not been extensively characterized. Here, we unraveled the role of the BolA-like protein IbaG in the cholera pathogen Vibrio cholerae. The absence of IbaG was associated with dramatic changes in cell morphology, sensitivity to envelope stressors, and intestinal colonization defects. IbaG was found to be required for biogenesis of several components of the V. cholerae cell envelope and to interact with numerous iron-sulfur cluster-containing proteins and factors involved in their assembly. Thus, our findings suggest that IbaG governs V. cholerae cell shape and cell envelope homeostasis through its effects on iron-sulfur proteins and associated pathways. The diversity of processes involving ironsulfur-containing proteins is likely a factor underlying the range of phenotypes associated with BolA family proteins.

Ort, förlag, år, upplaga, sidor
American Society for Microbiology (ASM), 2019
Nyckelord
BolA, IbaG, Vibrio cholerae, cell envelope, cell shape, iron-sulfur cluster
Nationell ämneskategori
Mikrobiologi inom det medicinska området
Identifikatorer
urn:nbn:se:umu:diva-162888 (URN)10.1128/mBio.00790-19 (DOI)000481617000011 ()31289173 (PubMedID)
Tillgänglig från: 2019-09-03 Skapad: 2019-09-03 Senast uppdaterad: 2019-09-03Bibliografiskt granskad
Howell, M., Aliashkevich, A., Sundararajan, K., Daniel, J. J., Lariviere, P. J., Goley, E. D., . . . Brown, P. J. B. (2019). Agrobacterium tumefaciens divisome proteins regulate the transition from polar growth to cell division. Molecular Microbiology, 111(4), 1074-1092
Öppna denna publikation i ny flik eller fönster >>Agrobacterium tumefaciens divisome proteins regulate the transition from polar growth to cell division
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2019 (Engelska)Ingår i: Molecular Microbiology, ISSN 0950-382X, E-ISSN 1365-2958, Vol. 111, nr 4, s. 1074-1092Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

The mechanisms that restrict peptidoglycan biosynthesis to the pole during elongation and re-direct peptidoglycan biosynthesis to mid-cell during cell division in polar-growing Alphaproteobacteria are largely unknown. Here, we explore the role of early division proteins of Agrobacterium tumefaciens including three FtsZ homologs, FtsA and FtsW in the transition from polar growth to mid-cell growth and ultimately cell division. Although two of the three FtsZ homologs localize to mid-cell, exhibit GTPase activity and form co-polymers, only one, FtsZ(AT), is required for cell division. We find that FtsZ(AT) is required not only for constriction and cell separation, but also for initiation of peptidoglycan synthesis at mid-cell and cessation of polar peptidoglycan biosynthesis. Depletion of FtsZ(AT) in A. tumefaciens causes a striking phenotype: cells are extensively branched and accumulate growth active poles through tip splitting events. When cell division is blocked at a later stage by depletion of FtsA or FtsW, polar growth is terminated and ectopic growth poles emerge from mid-cell. Overall, this work suggests that A. tumefaciens FtsZ makes distinct contributions to the regulation of polar growth and cell division.

Ort, förlag, år, upplaga, sidor
Wiley-Blackwell Publishing Inc., 2019
Nationell ämneskategori
Mikrobiologi inom det medicinska området
Identifikatorer
urn:nbn:se:umu:diva-158586 (URN)10.1111/mmi.14212 (DOI)000464655800015 ()30693575 (PubMedID)
Tillgänglig från: 2019-05-27 Skapad: 2019-05-27 Senast uppdaterad: 2019-05-27Bibliografiskt granskad
Chauhan, D., Srivastava, P. A., Ritzl, B., Yennamalli, R. M., Cava, F. & Priyadarshini, R. (2019). Amino Acid-Dependent Alterations in Cell Wall and Cell Morphology of Deinococcus indicus DR1. Frontiers in Microbiology, 10, Article ID 1449.
Öppna denna publikation i ny flik eller fönster >>Amino Acid-Dependent Alterations in Cell Wall and Cell Morphology of Deinococcus indicus DR1
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2019 (Engelska)Ingår i: Frontiers in Microbiology, ISSN 1664-302X, E-ISSN 1664-302X, Vol. 10, artikel-id 1449Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

Deinococcus radiodurans exhibits growth medium-dependent morphological variation in cell shape, but there is no evidence whether this phenomenon is observed in other members of the Deinococcaceae family. In this study, we isolated a red-pigmented, aerobic, Deinococcus indicus strain DR1 from Dadri wetland, India. This D. indicus strain exhibited cell-morphology transition from rod-shaped cells to multi-cell chains in a growth-medium-dependent fashion. In response to addition of 1% casamino acids in the minimal growth medium, rod-shaped cells formed multi-cell chains. Addition of all 20 amino acids to the minimal medium was able to recapitulate the phenotype. Specifically, a combination of L-methionine, L-lysine, L-aspartate, and L-threonine caused morphological alterations. The transition from rod shape to multi-cell chains is due to delay in daughter cell separation after cell division. Minimal medium supplemented with L-ornithine alone was able to cause cell morphology changes. Furthermore, a comparative UPLC analysis of PG fragments isolated from D. indicus cells propagated in different growth media revealed alterations in the PG composition. An increase in the overall cross-linkage of PG was observed in muropeptides from nutrient-rich TSB and NB media versus PYE medium. Overall our study highlights that environmental conditions influence PG composition and cell morphology in D. indicus.

Ort, förlag, år, upplaga, sidor
Frontiers Media S.A., 2019
Nyckelord
Deinococcus indicus, morphological alterations, amino acids, cell wall, muropeptides
Nationell ämneskategori
Mikrobiologi Mikrobiologi inom det medicinska området
Identifikatorer
urn:nbn:se:umu:diva-161695 (URN)10.3389/fmicb.2019.01449 (DOI)000473576800001 ()
Forskningsfinansiär
Knut och Alice Wallenbergs StiftelseVetenskapsrådetKempestiftelserna
Tillgänglig från: 2019-08-05 Skapad: 2019-08-05 Senast uppdaterad: 2019-08-05Bibliografiskt granskad
Kumar, K. & Cava, F. (2019). Chromatographic analysis of peptidoglycan samples with the aid of a chemometric technique: introducing a novel analytical procedure to classify bacterial cell wall collection. Analytical Methods, 11(12), 1671-1679
Öppna denna publikation i ny flik eller fönster >>Chromatographic analysis of peptidoglycan samples with the aid of a chemometric technique: introducing a novel analytical procedure to classify bacterial cell wall collection
2019 (Engelska)Ingår i: Analytical Methods, ISSN 1759-9660, E-ISSN 1759-9679, Vol. 11, nr 12, s. 1671-1679Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

The technical development of liquid chromatography has provided the necessary sensitivity to characterise peptidoglycan samples. However, the analysis of large numbers of complex chromatographic data sets without the aid of a proper chemometric technique is a laborious task, carrying a high risk of losing important biochemical information. The present work describes the development of a simple analytical procedure using self-organising map (SOM) analysis to analyse the large number of complex chromatographic data sets from bacterial peptidoglycan samples. SOM analysis essentially maps the samples to a hexagonal sheet based on their compositional similarity, and thus provides an approach to classify the bacterial cell wall collection in an unsupervised manner. The utility of the proposed approach was successfully validated by analysing peptidoglycan samples belonging to the Alphaproteobacterium class. The classification results achieved with SOM analysis were found to correlate well with their relative similarity in peptidoglycan compositions. In summary, the SOM analysis-based analytical procedure is shown to be useful towards automatising the analyses of chromatographic data sets of peptidoglycan samples from bacterial collections.

Nationell ämneskategori
Mikrobiologi
Identifikatorer
urn:nbn:se:umu:diva-158380 (URN)10.1039/c8ay02501k (DOI)000463892500011 ()
Tillgänglig från: 2019-04-29 Skapad: 2019-04-29 Senast uppdaterad: 2019-04-29Bibliografiskt granskad
Bernardo-Garcia, N., Sánchez-Murcia, P. A., Espaillat, A., Martínez-Caballero, S., Cava, F., Hermoso, J. A. & Gago, F. (2019). Cold-induced aldimine bond cleavage by Tris in Bacillus subtilis alanine racemase. Organic and biomolecular chemistry, 17(17), 4350-4358
Öppna denna publikation i ny flik eller fönster >>Cold-induced aldimine bond cleavage by Tris in Bacillus subtilis alanine racemase
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2019 (Engelska)Ingår i: Organic and biomolecular chemistry, ISSN 1477-0520, E-ISSN 1477-0539, Vol. 17, nr 17, s. 4350-4358Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

Pyridoxal 5'-phosphate (PLP) is a versatile cofactor involved in a large variety of enzymatic processes. Most of PLP-catalysed reactions, such as those of alanine racemases (AlaRs), present a common resting state in which the PLP is covalently bound to an active-site lysine to form an internal aldimine. The crystal structure of BsAlaR grown in the presence of Tris lacks this covalent linkage and the PLP cofactor appears deformylated. However, loss of activity in a Tris buffer only occurred after the solution was frozen prior to carrying out the enzymatic assay. This evidence strongly suggests that Tris can access the active site at subzero temperatures and behave as an alternate racemase substrate leading to mechanism-based enzyme inactivation, a hypothesis that is supported by additional X-ray structures and theoretical results from QM/ MM calculations. Taken together, our findings highlight a possibly underappreciated role for a common buffer component widely used in biochemical and biophysical experiments.

Ort, förlag, år, upplaga, sidor
Royal Society of Chemistry, 2019
Nationell ämneskategori
Organisk kemi Cell- och molekylärbiologi
Identifikatorer
urn:nbn:se:umu:diva-159052 (URN)10.1039/c9ob00223e (DOI)000465953500024 ()30977502 (PubMedID)
Tillgänglig från: 2019-05-21 Skapad: 2019-05-21 Senast uppdaterad: 2019-05-21Bibliografiskt granskad
Murphy, S. G., Alvarez, L., Adams, M. C., Liu, S., Chappie, J. S., Cava, F. & Dorr, T. (2019). Endopeptidase Regulation as a Novel Function of the Zur-Dependent Zinc Starvation Response. mBio, 10(1), Article ID e02620-18.
Öppna denna publikation i ny flik eller fönster >>Endopeptidase Regulation as a Novel Function of the Zur-Dependent Zinc Starvation Response
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2019 (Engelska)Ingår i: mBio, ISSN 2161-2129, E-ISSN 2150-7511, Vol. 10, nr 1, artikel-id e02620-18Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

The cell wall is a strong, yet flexible, meshwork of peptidoglycan (PG) that gives a bacterium structural integrity. To accommodate a growing cell, the wall is remodeled by both PG synthesis and degradation. Vibrio cholerae encodes a group of three nearly identical zinc-dependent endopeptidases (EPs) that are predicted to hydrolyze PG to facilitate cell growth. Two of these (ShyA and ShyC) are conditionally essential housekeeping EPs, while the third (ShyB) is not expressed under standard laboratory conditions. To investigate the role of ShyB, we conducted a transposon screen to identify mutations that activate shyB transcription. We found that shyB is induced as part of the Zur-mediated zinc starvation response, a mode of regulation not previously reported for cell wall lytic enzymes. In vivo, ShyB alone was sufficient to sustain cell growth in low-zinc environments. In vitro, ShyB retained its D, D-endopeptidase activity against purified sacculi in the presence of the metal chelator EDTA at concentrations that inhibit ShyA and ShyC. This insensitivity to metal chelation is likely what enables ShyB to substitute for other EPs during zinc starvation. Our survey of transcriptomic data from diverse bacteria identified other candidate Zur-regulated EPs, suggesting that this adaptation to zinc starvation is employed by other Gram-negative bacteria. IMPORTANCE Bacteria encode a variety of adaptations that enable them to survive during zinc starvation, a condition which is encountered both in natural environments and inside the human host. In Vibrio cholerae, the causative agent of the diarrheal disease cholera, we have identified a novel member of this zinc starvation response, a cell wall hydrolase that retains function and is conditionally essential for cell growth in low-zinc environments. Other Gram-negative bacteria contain homologs that appear to be under similar regulatory control. These findings are significant because they represent, to our knowledge, the first evidence that zinc homeostasis influences cell wall turnover. Anti-infective therapies commonly target the bacterial cell wall; therefore, an improved understanding of how the cell wall adapts to host-induced zinc starvation could lead to new antibiotic development. Such therapeutic interventions are required to combat the rising threat of drug-resistant infections.

Ort, förlag, år, upplaga, sidor
AMER SOC MICROBIOLOGY, 2019
Nyckelord
Gram-negative, Vibrio cholerae, cell wall, hydrolase, metalloproteins, peptidoglycan, zinc starvation
Nationell ämneskategori
Mikrobiologi inom det medicinska området
Identifikatorer
urn:nbn:se:umu:diva-157540 (URN)10.1128/mBio.02620-18 (DOI)000460314300056 ()30782657 (PubMedID)
Tillgänglig från: 2019-04-01 Skapad: 2019-04-01 Senast uppdaterad: 2019-04-01Bibliografiskt granskad
Hsu, Y.-P., Hall, E., Booher, G., Murphy, B., Radkov, A. D., Yablonowski, J., . . . VanNieuwenhze, M. S. (2019). Fluorogenic D-amino acids enable real-time monitoring of peptidoglycan biosynthesis and high-throughput transpeptidation assays. Nature Chemistry, 11(4), 335-341
Öppna denna publikation i ny flik eller fönster >>Fluorogenic D-amino acids enable real-time monitoring of peptidoglycan biosynthesis and high-throughput transpeptidation assays
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2019 (Engelska)Ingår i: Nature Chemistry, ISSN 1755-4330, E-ISSN 1755-4349, Vol. 11, nr 4, s. 335-341Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

Peptidoglycan is an essential cell wall component that maintains the morphology and viability of nearly all bacteria. Its biosynthesis requires periplasmic transpeptidation reactions, which construct peptide crosslinkages between polysaccharide chains to endow mechanical strength. However, tracking the transpeptidation reaction in vivo and in vitro is challenging, mainly due to the lack of efficient, biocompatible probes. Here, we report the design, synthesis and application of rotor-fluorogenic D-amino acids (RfDAAs), enabling real-time, continuous tracking of transpeptidation reactions. These probes allow peptidoglycan biosynthesis to be monitored in real time by visualizing transpeptidase reactions in live cells, as well as real-time activity assays of D,D- and L,D-transpeptidases and sortases in vitro. The unique ability of RfDAAs to become fluorescent when incorporated into peptidoglycan provides a powerful new tool to study peptidoglycan biosynthesis with high temporal resolution and prospectively enable high-throughput screening for inhibitors of peptidoglycan biosynthesis.

Ort, förlag, år, upplaga, sidor
Nature Publishing Group, 2019
Nationell ämneskategori
Mikrobiologi inom det medicinska området
Identifikatorer
urn:nbn:se:umu:diva-157944 (URN)10.1038/s41557-019-0217-x (DOI)000462046600011 ()30804500 (PubMedID)
Tillgänglig från: 2019-04-18 Skapad: 2019-04-18 Senast uppdaterad: 2019-04-18Bibliografiskt granskad
Joers, A., Vind, K., Hernandez, S. B., Maruste, R., Pereira, M., Brauer, A., . . . Tenson, T. (2019). Muropeptides Stimulate Growth Resumption from Stationary Phase in Escherichia coli. Scientific Reports, 9, Article ID 18043.
Öppna denna publikation i ny flik eller fönster >>Muropeptides Stimulate Growth Resumption from Stationary Phase in Escherichia coli
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2019 (Engelska)Ingår i: Scientific Reports, ISSN 2045-2322, E-ISSN 2045-2322, Vol. 9, artikel-id 18043Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

When nutrients run out, bacteria enter a dormant metabolic state. This low or undetectable metabolic activity helps bacteria to preserve their scant reserves for the future needs, yet it also diminishes their ability to scan the environment for new growth-promoting substrates. However, neighboring microbial growth is a reliable indicator of a favorable environment and can thus serve as a cue for exiting dormancy. Here we report that for Escherichia coli and Pseudomonas aeruginosa this cue is provided by the basic peptidoglycan unit (i.e. muropeptide). We show that several forms of muropeptides from a variety of bacterial species can stimulate growth resumption of dormant cells and the sugar-peptide bond is crucial for this activity. These results, together with previous research that identifies muropeptides as a germination signal for bacterial spores, and their detection by mammalian immune cells, show that muropeptides are a universal cue for bacterial growth.

Ort, förlag, år, upplaga, sidor
Nature Publishing Group, 2019
Nationell ämneskategori
Mikrobiologi
Identifikatorer
urn:nbn:se:umu:diva-166826 (URN)10.1038/s41598-019-54646-5 (DOI)000500701400001 ()31792329 (PubMedID)
Forskningsfinansiär
Knut och Alice Wallenbergs StiftelseVetenskapsrådetKempestiftelserna
Tillgänglig från: 2020-01-03 Skapad: 2020-01-03 Senast uppdaterad: 2020-01-03Bibliografiskt granskad
Irazoki, O., Hernandez, S. B. & Cava, F. (2019). Peptidoglycan Muropeptides: Release, Perception, and Functions as Signaling Molecules. Frontiers in Microbiology, 10, Article ID 500.
Öppna denna publikation i ny flik eller fönster >>Peptidoglycan Muropeptides: Release, Perception, and Functions as Signaling Molecules
2019 (Engelska)Ingår i: Frontiers in Microbiology, ISSN 1664-302X, E-ISSN 1664-302X, Vol. 10, artikel-id 500Artikel, forskningsöversikt (Refereegranskat) Published
Abstract [en]

Peptidoglycan (PG) is an essential molecule for the survival of bacteria, and thus, its biosynthesis and remodeling have always been in the spotlight when it comes to the development of antibiotics. The peptidoglycan polymer provides a protective function in bacteria, but at the same time is continuously subjected to editing activities that in some cases lead to the release of peptidoglycan fragments (i.e., muropeptides) to the environment. Several soluble muropeptides have been reported to work as signaling molecules. In this review, we summarize the mechanisms involved in muropeptide release (PG breakdown and PG recycling) and describe the known PG-receptor proteins responsible for PG sensing. Furthermore, we overview the role of muropeptides as signaling molecules, focusing on the microbial responses and their functions in the host beyond their immunostimulatory activity.

Ort, förlag, år, upplaga, sidor
Frontiers Media S.A., 2019
Nyckelord
peptidoglycan, PG cleaving enzymes, PG recycling, PG receptors, signaling functions, bacterial interactions
Nationell ämneskategori
Mikrobiologi
Identifikatorer
urn:nbn:se:umu:diva-158090 (URN)10.3389/fmicb.2019.00500 (DOI)000462687700001 ()
Forskningsfinansiär
VetenskapsrådetKnut och Alice Wallenbergs StiftelseKempestiftelserna
Tillgänglig från: 2019-04-15 Skapad: 2019-04-15 Senast uppdaterad: 2019-04-15Bibliografiskt granskad
Projekt
Peptidoglykan mångfald och plasticitet hos bakterier [2013-02440_VR]; Umeå universitetDemontering av membranmikrodomäner i Staphylococcus aureus för att tämja antibiotikaresistens hos MRSA [2018-05882_VR]; Umeå universitetVad reglerar cellväggens homeostas hos bakterier? [2018-02823_VR]; Umeå universitet
Organisationer
Identifikatorer
ORCID-id: ORCID iD iconorcid.org/0000-0001-5995-718x

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