{"id":545739,"date":"2026-03-19T01:33:10","date_gmt":"2026-03-19T01:33:10","guid":{"rendered":"https:\/\/www.newsbeep.com\/ca\/545739\/"},"modified":"2026-03-19T01:33:10","modified_gmt":"2026-03-19T01:33:10","slug":"periplasmic-crowding-and-peptidoglycan-hydrolase-activity-as-drivers-of-outer-membrane-vesiculation-in-acinetobacter-baumannii","status":"publish","type":"post","link":"https:\/\/www.newsbeep.com\/ca\/545739\/","title":{"rendered":"Periplasmic crowding and peptidoglycan hydrolase activity as drivers of outer membrane vesiculation in Acinetobacter baumannii"},"content":{"rendered":"

Schwechheimer, C. & Kuehn, M. J. Outer-membrane vesicles from Gram-negative bacteria: biogenesis and functions. Nat. Rev. Microbiol. 13, 605\u2013619 (2015).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Park, J. et al. A novel decoy strategy for polymyxin resistance in Acinetobacter baumannii. eLife 10, e66988 (2021).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Sartorio, M. G., Pardue, E. J., Feldman, M. F. & Haurat, M. F. Bacterial outer membrane vesicles: from discovery to applications. Annu. Rev. Microbiol. 75, 609\u2013630 (2021).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Li, C. et al. T6SS secretes an LPS-binding effector to recruit OMVs for exploitative competition and horizontal gene transfer. ISME J. 16, 500\u2013510 (2022).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Juodeikis, R. & Carding, S. R. Outer membrane vesicles: biogenesis, functions, and issues. Microbiol. Mol. Biol. Rev. 86, e0003222 (2022).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

McMillan, H. M. & Kuehn, M. J. The extracellular vesicle generation paradox: a bacterial point of view. EMBO J. 40, e108174 (2021).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Caruana, J. C. & Walper, S. A. Bacterial membrane vesicles as mediators of microbe-microbe and microbe-host community interactions. Front. Microbiol. 11, 432 (2020).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Clairfeuille, T. et al. Structure of the essential inner membrane lipopolysaccharide\u2013PbgA complex. Nature 584, 479\u2013483 (2020).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Shen, Z. et al. Outer membrane vesicles mediating horizontal transfer of the epidemic bla(OXA-232) carbapenemase gene among Enterobacterales. Emerg. Microbes Infect. 13, 2290840 (2024).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Zhao, X., Wei, Y., Bu, Y., Ren, X. & Dong, Z. Review on bacterial outer membrane vesicles: structure, vesicle formation, separation and biotechnological applications. Microb. Cell Fact. 24, 27 (2025).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Flannagan, R. S., Aubert, D., Kooi, C., Sokol, P. A. & Valvano, M. A. Burkholderia cenocepacia requires a periplasmic HtrA protease for growth under thermal and osmotic stress and for survival in vivo. Infect. Immun. 75, 1679\u20131689 (2007).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Fu, X. et al. DegP functions as a critical protease for bacterial acid resistance. FEBS J. 285, 3525\u20133538 (2018).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Leandro, M. R. et al. DegP protease is essential for tolerance to salt stress in the plant growth-promoting bacterium Gluconacetobacter diazotrophicus PAL5. Microbiol. Res. 243, 126654 (2021).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

\u0160ulskis, D., Thoma, J. & Burmann, B. M. Structural basis of DegP protease temperature-dependent activation. Sci. Adv. 7, eabj1816 (2021).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

McBroom, A. J., Johnson, A. P., Vemulapalli, S. & Kuehn, M. J. Outer membrane vesicle production by Escherichia coli is independent of membrane instability. J. Bacteriol. 188, 5385\u20135392 (2006).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Birkle, K. et al. An unprecedented tolerance to deletion of the periplasmic chaperones SurA, Skp, and DegP in the nosocomial pathogen Acinetobacter baumannii. J. Bacteriol. 204, e00054-22 (2022).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Kim, S. Y. et al. The sensor kinase BfmS controls production of outer membrane vesicles in Acinetobacter baumannii. BMC Microbiol. 19, 301 (2019).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Schwechheimer, C. & Kuehn, M. J. Synthetic effect between envelope stress and lack of outer membrane vesicle production in Escherichia coli. J. Bacteriol. 195, 4161\u20134173 (2013).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Sonntag, I., Schwarz, H., Hirota, Y. & Henning, U. Cell envelope and shape of Escherichia coli: multiple mutants missing the outer membrane lipoprotein and other major outer membrane proteins. J. Bacteriol. 136, 280\u2013285 (1978).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Takaki, K. et al. Multilamellar and multivesicular outer membrane vesicles produced by a Buttiauxella agrestis tolB mutant. App. Environ. Microbiol. 86, e01131\u201320 (2020).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

McBroom, A. J. & Kuehn, M. J. Release of outer membrane vesicles by Gram-negative bacteria is a novel envelope stress response. Mol. Microbiol. 63, 545\u2013558 (2007).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Bernadac, A., Gavioli, M., Lazzaroni, J. C., Raina, S. & Lloub\u00e8s, R. Escherichia coli tol-pal mutants form outer membrane vesicles. J. Bacteriol. 180, 4872\u20134878 (1998).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Betton, J. M., Boscus, D., Missiakas, D., Raina, S. & Hofnung, M. Probing the structural role of an alpha beta loop of maltose-binding protein by mutagenesis: heat-shock induction by loop variants of the maltose-binding protein that form periplasmic inclusion bodies. J. Mol. Biol. 262, 140\u2013150 (1996).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Matheli\u00e9-Guinlet, M., Asmar, A. T., Collet, J. F. & Dufr\u00eane, Y. F. Lipoprotein Lpp regulates the mechanical properties of the E. coli cell envelope. Nat. Commun. 11, 1789 (2020).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Rojas, E. R. et al. The outer membrane is an essential load-bearing element in Gram-negative bacteria. Nature 559, 617\u2013621 (2018).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Fenn, K. L. et al. Outer membrane protein assembly mediated by BAM-SurA complexes. Nat. Commun. 15, 7612 (2024).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Bryant, J. A. et al. Bam complex associated proteins in Escherichia coli are functionally linked to peptidoglycan biosynthesis, membrane fluidity and DNA replication. eLife 13, RP99955 (2024).<\/p>\n

Chamachi, N. et al. Chaperones Skp and SurA dynamically expand unfolded OmpX and synergistically disassemble oligomeric aggregates. PNAS 119, e2118919119 (2022).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Subrini, O. & Betton, J. M. Assemblies of DegP underlie its dual chaperone and protease function. FEMS Microbiol. Lett. 296, 143\u2013148 (2009).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Gilmore, M. C. & Cava, F. Peptidoglycan recycling mediated by an ABC transporter in the plant pathogen Agrobacterium tumefaciens. Nat. Commun. 13, 7927 (2022).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Simpson, B. W., Gilmore, M. C., McLean, A. B., Cava, F. & Trent, M. S. Escherichia coli utilizes multiple peptidoglycan recycling permeases with distinct strategies of recycling. PNAS 120, e2308940120 (2023).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Sverak, H. E. et al. Cryo-EM characterization of the anydromuropeptide permease AmpG central to bacterial fitness and \u03b2-lactam antibiotic resistance. Nat. Commun. 15, 9936 (2024).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Hayashi, J.-I., Hamada, N. & Kuramitsu, H. K. The autolysin of Porphyromonas gingivalis is involved in outer membrane vesicle release. FEMS Microbiol. Lett. 216, 217\u2013222 (2002).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Schwechheimer, C., Rodriguez, D. L. & Kuehn, M. J. NlpI-mediated modulation of outer membrane vesicle production through peptidoglycan dynamics in Escherichia coli. Microbiologyopen 4, 375\u2013389 (2015).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Egan, A. J. F., Errington, J. & Vollmer, W. Regulation of peptidoglycan synthesis and remodelling. Nat. Rev. Microbiol. 18, 446\u2013460 (2020).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Garde, S., Chodisetti, P. K. & Reddy, M. Peptidoglycan: structure, synthesis, and regulation. EcoSal Plus. 9, (2021).<\/p>\n

Dik, D. A., Marous, D. R., Fisher, J. F. & Mobashery, S. Lytic transglycosylases: concinnity in concision of the bacterial cell wall. Crit. Rev. Biochem. Mol. Biol. 52, 503\u2013542 (2017).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Kaul, M., Meher, S. K., Nallamotu, K. C. & Reddy, M. Glycan strand cleavage by a lytic transglycosylase, MltD contributes to the expansion of peptidoglycan in Escherichia coli. PLoS Genet. 20, e1011161 (2024).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Hoang, Y. et al. An experimental framework to assess biomolecular condensates in bacteria. Nat. Commun. 15, 3222 (2024).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Ma, B., Reynolds, C. M. & Raetz, C. R. H. Periplasmic orientation of nascent lipid A in the inner membrane of an Escherichia coli LptA mutant. Proc. Natl. Acad. Sci. USA. 105, 13823\u201313828 (2008).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Mor\u00e1n-Barrio, J. et al. The lipoprotein biosynthesis pathway: key to OXA-mediated carbapenem resistance in Acinetobacter baumannii. Antimicrob. Agents Chemother. 69, e0109925 (2025).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Huang, K. et al. Deletion of a previously uncharacterized lipoprotein lirL confers resistance to an inhibitor of type II signal peptidase in Acinetobacter baumannii. Proc. Natl. Acad. Sci. USA. 119, e2123117119 (2022).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Martorana, A. M. et al. Degradation of components of the Lpt transenvelope machinery reveals LPS-dependent Lpt complex stability in Escherichia coli. Front. Mol. Biosci. 8, 758228 (2021).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Son, Y. et al. Unexpected vulnerability of Enterococcus faecium to polymyxin B under anaerobic condition. Gut Microbes 16, 2438465 (2024).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Yang, J., Yun, S. & Park, W. Blue Light Sensing BlsA-mediated modulation of meropenem resistance and biofilm formation in Acinetobacter baumannii. mSystems 8, e00897-22 (2023).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Manioglu, S. et al. Antibiotic polymyxin arranges lipopolysaccharide into crystalline structures to solidify the bacterial membrane. Nat. Commun. 13, 6195 (2022).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Marotta, J., May, K. L., Bae, C. Y. & Grabowicz, M. Molecular insights into Escherichia coli Cpx envelope stress response activation by the sensor lipoprotein NlpE. Mol. Microbiol. 119, 586\u2013598 (2023).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Roch, M. et al. Thermosensitive PBP2a requires extracellular folding factors PrsA and HtrA1 for Staphylococcus aureus MRSA \u03b2-lactam resistance. Commun. Biol. 2, 417 (2019).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Penwell, W. F. et al. Molecular mechanisms of sulbactam antibacterial activity and resistance determinants in Acinetobacter baumannii. AAC 59, 1680\u20131689 (2015).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Kocaoglu, O. & Carlson, E. E. Profiling of \u03b2-lactam selectivity for penicillin-binding proteins in Escherichia coli Strain DC2. AAC 59, 2785\u20132790 (2015).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Cr\u00e9pin, S. et al. The lytic transglycosylase MltB connects membrane homeostasis and in vivo fitness of Acinetobacter baumannii. Mol. Microbiol. 109, 745\u2013762 (2018).<\/p>\n

Le, N. H. et al. Peptidoglycan editing provides immunity to Acinetobacter baumannii during bacterial warfare. Sci. Adv. 6, eabb5614 (2020).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Raustad, N. et al. A phosphorylation signal activates genome-wide transcriptional control by BfmR, the global regulator of Acinetobacter resistance and virulence. Nucleic Acids Res. 53, gkaf063 (2025).<\/p>\n

Rao, S. et al. Characterizing membrane association and periplasmic transfer of bacterial lipoproteins through molecular dynamics simulations. Structure 28, 475\u2013487.e3 (2020).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Micelli, C. et al. A conserved zinc-binding site in Acinetobacter baumannii PBP2 required for elongasome-directed bacterial cell shape. PNAS 120, e2215237120 (2023).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

May, K. L., Lehman, K. M., Mitchell, A. M. & Grabowicz, M. A stress response monitoring lipoprotein trafficking to the outer membrane. mBio 10, e00618-19 (2019).<\/p>\n

Gottesman, S. Proteases and their targets in Escherichia coli. Annu. Rev. Genet. 30, 465\u2013506 (1996).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Soltes, G. R., Martin, N. R., Park, E., Sutterlin, H. A. & Silhavy, T. J. Distinctive roles for periplasmic proteases in the maintenance of essential outer membrane protein assembly. J. Bacteriol. 199, 10 (2017).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Birkle, K. et al. An unprecedented tolerance to deletion of the periplasmic chaperones SurA, Skp, and DegP in the nosocomial pathogen Acinetobacter baumannii. J. Bacteriol. 204, e00054\u20132 (2022).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Spiess, C., Beil, A. & Ehrmann, M. A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein. Cell 97, 339\u2013347 (1999).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Krojer, T., Garrido-Franco, M., Huber, R., Ehrmann, M. & Clausen, T. Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine. Nature 416, 455\u2013459 (2022).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Fantappi\u00e8, L., Irene, C., De Santis, M., Armini, A. & Gagliardi, A. Some Gram-negative lipoproteins keep their surface topology when transplanted from one species to another and deliver foreign polypeptides to the bacterial surface. Mol Cell Proteomics 16, 1348\u20131364 (2017).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Raivio, T. L., Leblanc, S. K. & Price, N. L. The Escherichia coli Cpx envelope stress response regulates genes of diverse function that impact antibiotic resistance and membrane integrity. J. Bacteriol. 195, 2755\u20132767 (2014).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Cian, M. B., Giordano, N. P., Mettlach, J. A., Minor, K. E. & Dalebroux, Z. D. Separation of the cell envelope for Gram-negative bacteria into inner and outer membrane fractions with technical adjustments for Acinetobacter baumannii. J. Vis. Exp. 10, 10.3791-60517 (2020).<\/p>\n

Cho, T. H. S., Wang, J. & Raivio, T. L. NlpE is an OmpA-associated outer membrane sensor of the Cpx envelope stress response. J. Bacteriol. 205, e00407-22 (2023).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Lin, M. F., Lin, Y. Y. & Lan, C. Y. The role of the two-component system BaeSR in disposing chemicals through regulating transporter systems in Acinetobacter baumannii. PLoS ONE 10, e0132843 (2015).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Palethorpe, S. et al. Acinetobacter baumannii Regulates its stress responses via the BfmRS two-component regulatory system. J. Bacteriol. 204, e0049421 (2022).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Laloux, G. & Collet, J. F. Major Tom to ground control: how lipoproteins communicate extracytoplasmic stress to the decision center of the cell. J. Bacteriol. 199, 3 (2017).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Delhaye, A., Collet, J. F. & Laloux, G. Fine-tuning of the Cpx envelope stress response is required for cell wall homeostasis in Escherichia coli. mBio 7, 1128 (2016).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Price, N. L. & Raivio, T. L. Characterization of the Cpx regulon in Escherichia coli strain MC4100. J. Bacteriol. 191, 1798\u20131815 (2009).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Raivio, T. L., Leblanc, S. K. & Price, N. L. The Escherichia coli Cpx envelope stress response regulates genes of diverse function that impact antibiotic resistance and membrane integrity. J. Bacteriol. 195, 2755\u20132767 (2013).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Scheurwater, E., Reid, C. W. & Clarke, A. J. Lytic transglycosylases: bacterial space-making autolysins. Int. J. Biochem. Cell Biol. 40, 586\u2013591 (2007).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Avila-Cobian, L. F., De Benedetti, S., Kim, C., Feltzer, R. & Champion, M. M. In vitro studies of the protein-interaction network of cell-wall lytic transglycosylase RlpA of Pseudomonas aeruginosa. Commun. Biol. 5, 1314 (2022).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Lee, M. et al. Reactions of all Escherichia coli lytic transglycosylases with bacterial cell wall. J. Am. Chem. Soc. 135, 3311\u20133314 (2013).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Weaver, A. I. et al. Lytic transglycosylases RlpA and MltC assist in Vibrio cholerae daughter cell separation. Mol. Microbiol. 112, 1100\u20131115 (2019).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Alvarez, L. et al. Control of bacterial cell wall autolysins by peptidoglycan crosslinking mode. Nat. Commun. 15, 7937 (2024).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Yunck, R., Cho, H. & Bernhardt, T. G. Identification of MltG as a potential terminase for peptidoglycan polymerization in bacteria. Mol. Microbiol. 99, 700\u2013718 (2016).<\/p>\n

Sassine, J., Pazos, M., Breukink, E. & Vollmer, W. Lytic transglycosylase MltG cleaves in nascent peptidoglycan and produces short glycan strands. Cell Surf. 7, 100053 (2021).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

White, C. L. & Gober, J. W. MreB: pilot or passenger of cell wall synthesis? Trends Microbiol. 20, 74\u201379 (2012).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Yun, S. et al. Experimental evolution under different nutritional conditions changes the genomic architecture and virulence of Acinetobacter baumannii. Commun. Biol. 7, 1274 (2024).<\/p>\n

Yang, J., Son, Y., Kang, M. & Park, W. AamA-mediated epigenetic control of genome-wide gene expression and phenotypic traits in Acinetobacter baumannii ATCC 17978. Microbial Genomics 9, 001093 (2023).<\/p>\n

Wang, Y. et al. A highly efficient CRISPR-Cas9-based genome engineering platform in Acinetobacter baumannii to understand the H2O2-sensing mechanism of OxyR. Cell Chem. Biol. 26, 1732\u20131742.e5 (2019).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Park, Y. et al. Alleviation of H2O2 toxicity by extracellular catalases in the phycosphere of Microcystis aeruginosa. Harmful Algae 137, 102680 (2024).<\/p>\n

Choi, J. et al. Efficient hepatic differentiation and regeneration potential under xeno-free conditions using mass-producible amnion-derived mesenchymal stem cells. Stem Cell Res. Ther. 12, 569 (2021).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Cian, M. B., Giordano, N. P., Mettlach, J. A., Minor, K. E. & Dalebroux, Z. D. Separation of the cell envelope for Gram-negative bacteria into inner and outer membrane fractions with technical adjustments for Acinetobacter baumannii. J. Vis. Exp. 10, 10 (2020).<\/p>\n

Damke, P. P. et al. Identification of the periplasmic DNA receptor for natural transformation of Helicobacter pylori. Nat. Commun. 10, 5357 (2019).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Simpson, B. W. et al. Acinetobacter baumannii can survive with an outer membrane lacking lipooligosaccharide due to structural support from elongasome peptidoglycan synseparatemutantsthesis. mBio 12, e03099-21 (2021).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Vroom, M. M. et al. Modeled microgravity alters lipopolysaccharide and outer membrane vesicle production of the beneficial symbiont Vibrio fischeri. npj Microgravity 7, 8 (2021).<\/p>\n


\n Google Scholar<\/a>\u00a0\n <\/p>\n

Matano, C. et al. Corynebacterium glutamicum possesses \u03b2-N-acetylglucosaminidase. BMC Microbiol. 16, 177 (2016).<\/p>\n


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