Flotillin homologue is involved in the swimming behavior of Escherichia coli

Padilla‐Vaca, Felipe; Vargas-Maya, Naurú Idalia; Elizarrarás-Vargas, Narciso Ulises; Rangel-Serrano, Ángeles; Cardoso-Reyes, Luis Rafael; Razo-Soria, Tannia; Membrillo-Hernández, Jorge; Franco, Bernardo

doi:10.1007/s00203-019-01670-8

Cited by 13 publications

(14 citation statements)

References 48 publications

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“…Therefore, the cortical and cell-wall cytoskeleton may result in a more uniform dynamic coverage of the cells by FMMs, which could facilitate the efficient capture of FMM client proteins to promote their oligomerization. The efficient oligomerization of these complexes in general and their partitioning in particular might play an important role in bacterial processes like cell division, peptidoglycan synthesis, protein secretion, motility or signal transduction, which have been associated with the integrity of FMMs in previous studies 27,31,71,101 .…”

Section: Discussionmentioning

confidence: 95%

The Bacterial Cytoskeleton Spatially Confines Functional Membrane Microdomains

Machta

et al. 2020

Preprint

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22Cell membranes laterally segregate into microdomains enriched in certain lipids and scaffold 23 proteins. Membrane microdomains modulate protein-protein interactions and are essential for cell 24 polarity, signaling and membrane trafficking. How cells organize their membrane microdomains, and 25 the physiological importance of these microdomains, is unknown. In eukaryotes, the cortical actin 26 cytoskeleton is proposed to act like a fence, constraining the dynamics of membrane microdomains. 27Like their eukaryotic counterparts, bacterial cells have functional membrane microdomains (FMMs) 28 that act as platforms for the efficient oligomerization of protein complexes. In this work, we used the 29 model organism Bacillus subtilis to demonstrate that FMM organization and movement depend 30 primarily on the interaction of FMM scaffold proteins with the domains' protein cargo, rather than with 31 domain lipids. Additionally, the MreB actin-like cytoskeletal network that underlies the bacterial 32 membrane was found to frame areas of the membrane in which FMM mobility is concentrated. 33Variations in membrane fluidity did not affect FMM mobility whereas alterations in cell wall organization 34 affected FMM mobility substantially. Interference with MreB organization alleviates FMM spatial 35 confinement whereas, by contrast, inhibition of cell wall synthesis strengthens FMM confinement. The 36 restriction of FMM lateral mobility by the submembranous actin-like cytoskeleton or the extracellular 37 wall cytoskeleton appears to be a conserved mechanism in prokaryotic and eukaryotic cells for 38 localizing functional protein complexes in specific membrane regions, thus contributing to the 39 organization of cellular processes. 40 41 42 43 48 actually heterogeneous fluids, with different membrane lipid species laterally segregating into sub-49 micrometer domains, driven by their physico-chemical properties 2-4 . This heterogeneous organization 50 of membrane lipids leads to a heterogeneous distribution of the embedded membrane proteins, which 51 appears essential for their functionality 5 . Membrane microdomains are widely present, mobile 52 structures that vary in size from transient protein clusters measured in nm 6 to large micron-sized stable 53 domains such as desmosomes 7 . These domains harbor proteins specialized in membrane trafficking, 54 cell-cell adhesion, and signal transduction, and they provide targets for viral entry 8 . 56It is now appreciated that membrane proteins can significantly impact membrane organization, in 57 particular stabilizing membrane domains. For instance, the scaffold activity of the flotillin proteins FLO1 58 and FLO2 plays an important role in stabilizing some eukaryotic membrane rafts ("lipid rafts") 9-11 ; it 59 would seem that this raft organization occurs in part through the capture and stabilization of specific 60 lipids by flotillins 12,13 . In addition, the activity of the flotillin scaffold contributes to the recruitment of 61 other raft-associated proteins, thus facilitatin...

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Section: Discussionmentioning

confidence: 95%

The Bacterial Cytoskeleton Spatially Confines Functional Membrane Microdomains

Machta

et al. 2020

Preprint

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“…This assumption is supported by several previous reports. In a recent study, two Salmonella flagellar mutants were reported to be defective in the early stage of biofilm formation in microtiter plates in the crystal violet biofilm assay [41]. Another study on Salmonella showed that flagella were not required for the production of RDAR biofilms on CR-agar plates, whereas absence of flagella did influence biofilm formation on air-liquid, surfaceliquid or cell-cell-liquid interfaces [42].…”

Section: Discussionmentioning

confidence: 99%

“…The YqiK protein is suggested to be implicated in stress sensing in E.coli. A yqiK-deficient mutant strain showed enhanced swimming behavior, implying that this gene downregulates motility [41]. Regarding the other candidate, sugE, a deletion of this gene in Klebsiella pneumonia provided a 1.5-fold enhanced ability to produce biofilm, suggesting a biofilm repressing function of the gene [42].…”

Section: Discussionmentioning

confidence: 99%

The Effect of Antimicrobial Resistance Plasmids Carrying blaCMY-2 on Biofilm Formation by Escherichia coli from the Broiler Production Chain

Nesse

Ramstad

et al. 2021

Microorganisms

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Extended-spectrum cephalosporin-resistant Escherichia coli (ESCR E. coli) with plasmids carrying the blaCMY-2 resistance gene have been isolated from the Norwegian broiler production chain through the Norwegian monitoring program for antimicrobial resistance in animals, food and feed, NORM-VET. The aim of the present study was to investigate the biofilm forming abilities of these strains, and in particular to see whether these might be influenced by the carriage of blaCMY-2 plasmids. The ESCR E. coli from the broiler production chain displayed relatively low biofilm forming abilities in the crystal violet biofilm assay as compared to quinolone-resistant E. coli (QREC) from the same population (mean ± SD = 0.686 ± 0.686 vs. 1.439 ± 0.933, respectively). Acquisition of two different blaCMY-2 plasmids by QREC strains reduced their biofilm production in microtiter plates, but not their biofilm production on Congo Red agar plates. Furthermore, motility was reduced, but not planktonic growth. We hypothesize that genes carried by these plasmids may have caused the observed reduction in biofilm formation, possibly mediated through changes in flagellar expression or function. Furthermore, this may help explain the different biofilm forming abilities observed between ESCR E. coli and QREC. The results also indicate that the risk of biofilm reservoirs of antimicrobial resistant E. coli on in the broiler production is lower for ESCR E. coli than for QREC.

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“…The BceAB system appears to act in disassembly of bacitracin complexes to confer resistance (Kobras et al, 2020). In addition, BceAB interacts with the BceRS TCS to allow sensing of bacitracin (Ohki et al, 2003;Dintner et al, 2014;Fritz et al, 2015;Koh et al, 2020). The BceRS-AB system provides a first line of defense against bacitracin, with higher levels of antibiotic activating the protective responses mediated by the LiaRS and σ ECF regulons (Radeck et al, 2016).…”

Section: Antibiotic Specific Detoxification Modulesmentioning

confidence: 99%

“…In S. aureus , FloA colocalizes with staphyloxanthin in FMMs ( Garcia-Fernandez et al, 2017 ; Foster, 2019 ). In other systems, flotillins and FMMs are associated with flagellar function and chemotaxis ( Padilla-Vaca et al, 2019 ; Takekawa et al, 2019 ), type VII secretion ( Mielich-Suss et al, 2017 ), signaling ( Wagner et al, 2017 ), and interaction with the host during infection ( Hutton et al, 2017 ). Ongoing efforts strive to track the mobility, oligomerization state, and interaction partners of flotillins in living cells.…”

Section: Cell Envelope Stress Responses That Function Through Membrane Proteinsmentioning

confidence: 99%

Mini Review: Bacterial Membrane Composition and Its Modulation in Response to Stress

Willdigg

Helmann

2021

Front. Mol. Biosci.

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Antibiotics and other agents that perturb the synthesis or integrity of the bacterial cell envelope trigger compensatory stress responses. Focusing on Bacillus subtilis as a model system, this mini-review summarizes current views of membrane structure and insights into how cell envelope stress responses remodel and protect the membrane. Altering the composition and properties of the membrane and its associated proteome can protect cells against detergents, antimicrobial peptides, and pore-forming compounds while also, indirectly, contributing to resistance against compounds that affect cell wall synthesis. Many of these regulatory responses are broadly conserved, even where the details of regulation may differ, and can be important in the emergence of antibiotic resistance in clinical settings.

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Flotillin homologue is involved in the swimming behavior of Escherichia coli

Cited by 13 publications

References 48 publications

The Bacterial Cytoskeleton Spatially Confines Functional Membrane Microdomains

The Bacterial Cytoskeleton Spatially Confines Functional Membrane Microdomains

The Effect of Antimicrobial Resistance Plasmids Carrying blaCMY-2 on Biofilm Formation by Escherichia coli from the Broiler Production Chain

Mini Review: Bacterial Membrane Composition and Its Modulation in Response to Stress

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