Altered Envelope Structure and Nanomechanical Properties of a C-Terminal Protease A-Deficient Rhizobium leguminosarum

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dc.contributor.authorJun, Dong
dc.contributor.authorIdem, Ubong
dc.contributor.authorDahms, Tanya E. S.
dc.date.accessioned2023-05-15T19:22:34Z
dc.date.available2023-05-15T19:22:34Z
dc.date.issued2020-09-16
dc.description© 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).en_US
dc.description.abstract1) Background: Many factors can impact bacterial mechanical properties, which play an important role in survival and adaptation. This study characterizes the ultrastructural phenotype, elastic and viscoelastic properties of Rhizobium leguminosarum bv. viciae 3841 and the C-terminal protease A (ctpA) null mutant strain predicted to have a compromised cell envelope; (2) Methods: To probe the cell envelope, we used transmission electron microscopy (TEM), high performance liquid chromatography (HPLC), mass spectrometry (MS), atomic force microscopy (AFM) force spectroscopy, and time-dependent AFM creep deformation; (3) Results: TEM images show a compromised and often detached outer membrane for the ctpA mutant. Muropeptide characterization by HPLC and MS showed an increase in peptidoglycan dimeric peptide (GlcNAc-MurNAc-Ala-Glu-meso-DAP-Ala-meso-DAP-Glu-Ala-MurNAc-GlcNAc) for the ctpA mutant, indicative of increased crosslinking. The ctpA mutant had significantly larger spring constants than wild type under all hydrated conditions, attributable to more highly crosslinked peptidoglycan. Time-dependent AFM creep deformation for both the wild type and ctpA mutant was indicative of a viscoelastic cell envelope, with best fit to the four-element Burgers model and generating values for viscoelastic parameters k1, k2, η1, and η2; (4) Conclusions: The viscoelastic response of the ctpA mutant is consistent with both its compromised outer membrane (TEM) and fortified peptidoglycan layer (HPLC/MS).en_US
dc.description.authorstatusFacultyen_US
dc.description.peerreviewyesen_US
dc.description.sponsorshipThis research was funded by a Natural Sciences and Engineering Research Council (NSERC) Discovery Grant (228206-2012) and Canada Foundation for Innovation Leaders Opportunity Fund to T.E.S.D. U.I. was supported by a NSERC undergraduate student research assistantship and D.J. was partially supported by the Faculty of Graduate Studies and Research, University of Regina. The APC was funded by the University of Regina. This publication was paid for, in part, by the University of Regina President's Publication Fund.en_US
dc.identifier.citationJun D., Idem U., Dahms T. E. S.* (2020) Altered Envelope Structure and Nanomechanical Properties of a C-Terminal Protease A-Deficient Rhizobium leguminosarum. Microorganisms 8(9):1421. doi: 10.3390/microorganisms8091421en_US
dc.identifier.doihttps://doi.org/10.3390/microorganisms8091421
dc.identifier.urihttps://hdl.handle.net/10294/15920
dc.language.isoenen_US
dc.publisherMultidisciplinary Digital Publishing Instituteen_US
dc.rightsAttribution 4.0 International*
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/*
dc.subjectatomic force microscopyen_US
dc.subjectcell envelopeen_US
dc.subjectC-terminal proteaseen_US
dc.subjectforce spectroscopyen_US
dc.subjectRhizobium leguminosarumen_US
dc.subjectviscoelasticityen_US
dc.titleAltered Envelope Structure and Nanomechanical Properties of a C-Terminal Protease A-Deficient Rhizobium leguminosarumen_US
dc.typeArticleen_US
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