scholarly journals Adaptive Evolution of Industrial Lactococcus lactis Under Cell Envelope Stress Provides Phenotypic Diversity

2018 ◽  
Vol 9 ◽  
Author(s):  
María Jesús López-González ◽  
Susana Escobedo ◽  
Ana Rodríguez ◽  
A. Rute Neves ◽  
Thomas Janzen ◽  
...  
Keyword(s):  
Lactococcus Lactis ◽  
Adaptive Evolution ◽  
Phenotypic Diversity ◽  
Cell Envelope ◽  
Envelope Stress

scholarly journals Use of Green Fluorescent Protein To Monitor Cell Envelope Stress in Lactococcus lactis

2009 ◽  
Vol 76 (3) ◽  
pp. 978-981 ◽  
Author(s):  
Ana Belén Campelo ◽  
Ana Rodríguez ◽  
Beatriz Martínez
Keyword(s):  
Green Fluorescent Protein ◽  
Lactococcus Lactis ◽  
Fluorescent Protein ◽  
Cell Envelope ◽  
Dot Blot ◽  
Reporter System ◽  
Fast Detection ◽  
Envelope Stress ◽  
Dot Blot Assay ◽  
Green Fluorescent

ABSTRACT A Lactococcus lactis reporter system suitable to detect cell envelope stress in high-throughput settings was developed by fusing the CesR-regulated promoter of llmg0169 to the gfpuv gene. A dot blot assay allowed fast detection of green fluorescent protein (GFP) fluorescence even at low production levels. Unexpectedly, this promoter was also induced by mitomycin C via CesR.

scholarly journals Efficient Overproduction of Membrane Proteins in Lactococcus lactis Requires the Cell Envelope Stress Sensor/Regulator Couple CesSR

PLoS ONE ◽  
2011 ◽  
Vol 6 (7) ◽  
pp. e21873 ◽  
Author(s):  
Joao P. C. Pinto ◽  
Oscar P. Kuipers ◽  
Ravi K. R. Marreddy ◽  
Bert Poolman ◽  
Jan Kok
Keyword(s):  
Membrane Proteins ◽  
Lactococcus Lactis ◽  
Cell Envelope ◽  
Stress Sensor ◽  
Envelope Stress

scholarly journals Combining Cell Envelope Stress Reporter Assays in a Screening Approach to Identify BAM Complex Inhibitors

2021 ◽  
Author(s):  
Maurice Steenhuis ◽  
Federico Corona ◽  
Corinne M. ten Hagen-Jongman ◽  
Waldemar Vollmer ◽  
Dominique Lambin ◽  
...  
Keyword(s):  
Cell Envelope ◽  
Bam Complex ◽  
Screening Approach ◽  
Envelope Stress ◽  
Reporter Assays

Varying influence of the autolysin, N-acetyl muramidase, and the cell envelope proteinase on the rate of autolysis of six commercial Lactococcus lactis cheese starter bacteria grown in milk

2000 ◽  
Vol 67 (4) ◽  
pp. 585-596 ◽  
Author(s):  
SELVARANI GOVINDASAMY-LUCEY ◽  
PRAMOD K. GOPAL ◽  
PATRICK A. SULLIVAN ◽  
CHRISTOPHER J. PILLIDGE
Keyword(s):  
Lactococcus Lactis ◽  
Cell Walls ◽  
Cell Envelope ◽  
Laboratory Strain ◽  
Proteolytic Cleavage ◽  
Zymogram Analysis ◽  
Sds Page ◽  
Derivatives Of ◽  
Free Strains

The autolysin, N-acetyl muramidase (AcmA), of six commercial Lactococcus lactis subsp. cremoris starter strains and eight Lc. lactis subsp. cremoris derivatives or plasmid-free strains was shown by renaturing SDS-PAGE (zymogram analysis) to be degraded by the cell envelope proteinase (lactocepin; EC 3.4.21.96) after growth of strains in milk at 30 °C for 72 h. Degradation of AcmA was less in starter strains and derivatives producing lactocepin I/III (intermediate specificity) than in strains producing lactocepin I. This supports previous observations on AcmA degradation in derivatives of the laboratory strain Lc. lactis subsp. cremoris MG1363 (Buist et al. Journal of Bacteriology180 5947–5953 1998). In contrast to the MG1363 derivatives, however, the extent of autolysis in milk of the commercial Lc. lactis subsp. cremoris starter strains in this study did not always correlate with lactocepin specificity and AcmA degradation. The distribution of autolysins within the cell envelope of Lc. lactis subsp. cremoris starter strains and derivatives harvested during growth in milk was compared by zymogram analysis. AcmA was found associated with cell membranes as well as cell walls and some cleavage of AcmA occurred independently of lactocepin activity. An AcmA product intermediate in size between precursor (46 kDa) and mature (41 kDa) forms of AcmA was clearly visible on zymograms, even in the absence of lactocepin I activity. These results show that autolysis of commercial Lc. lactis subsp. cremoris starter strains is not primarily determined by AcmA activity in relation to lactocepin specificity and that proteolytic cleavage of AcmA in vivo is not fully defined.

scholarly journals Glycopeptide resistance: Links with inorganic phosphate metabolism and cell envelope stress

2017 ◽  
Vol 133 ◽  
pp. 74-85 ◽  
Author(s):  
Fernando Santos-Beneit ◽  
María Ordóñez-Robles ◽  
Juan F. Martín
Keyword(s):  
Inorganic Phosphate ◽  
Cell Envelope ◽  
Phosphate Metabolism ◽  
Glycopeptide Resistance ◽  
Envelope Stress

scholarly journals Phyletic distribution and diversification of the Phage Shock Protein stress response system in bacteria and archaea

2021 ◽  
Author(s):  
Philipp F. Popp ◽  
Vadim M. Gumerov ◽  
Ekaterina P. Andrianova ◽  
Lisa Bewersdorf ◽  
Thorsten Mascher ◽  
...  
Keyword(s):  
Stress Response ◽  
Large Scale ◽  
Cell Envelope ◽  
Model Organisms ◽  
Microbial World ◽  
Natural Classification ◽  
Response System ◽  
Core Proteins ◽  
Envelope Stress

AbstractThe bacterial cell envelope is an essential structure that protects the cell from environmental threats, while simultaneously serving as communication interface and diffusion barrier. Therefore, maintaining cell envelope integrity is of vital importance for all microorganisms. Not surprisingly, evolution has shaped conserved protection networks that connect stress perception, transmembrane signal transduction and mediation of cellular responses upon cell envelope stress. The phage shock protein (PSP) stress response is one of such conserved protection networks. Most of the knowledge about the Psp response comes from studies in the Gram-negative model bacterium, Escherichia coli where the Psp system consists of several well-defined protein components. Homologous systems were identified in representatives of Proteobacteria, Actinobacteria, and Firmicutes; however, the Psp system distribution in the microbial world remains largely unknown. By carrying out a large-scale, unbiased comparative genomics analysis, we found components of the Psp system in many bacterial and archaeal phyla and demonstrated that the PSP system deviates dramatically from the proteobacterial prototype. Two of its core proteins, PspA and PspC, have been integrated in various (often phylum-specifically) conserved protein networks during evolution. Based on protein sequence and gene neighborhood analyses of pspA and pspC homologs, we built a natural classification system of PSP networks in bacteria and archaea. We performed a comprehensive in vivo protein interaction screen for the PSP network newly identified in the Gram-positive model organism Bacillus subtilis and found a strong interconnected PSP response system, illustrating the validity of our approach. Our study highlights the diversity of PSP organization and function across many bacterial and archaeal phyla and will serve as foundation for future studies of this envelope stress response beyond model organisms.

scholarly journals Swarmer cell development of the bacteriumProteus mirabilisrequires the conserved ECA biosynthesis gene,rffG

2017 ◽  
Author(s):  
Kristin Little ◽  
Murray J. Tipping ◽  
Karine A. Gibbs
Keyword(s):  
Cell Morphology ◽  
Stress Responses ◽  
Cell Elongation ◽  
Cell Envelope ◽  
Membrane Composition ◽  
Swarmer Cell ◽  
Enterobacterial Common Antigen ◽  
Envelope Stress ◽  
Open Question ◽  
Additional Role

AbstractIndividual cells of the bacteriumProteus mirabiliscan elongate up to 40-fold on surfaces before engaging in a cooperative surface-based motility termed swarming. How cells regulate this dramatic morphological remodeling remains an open question. In this paper, we move forward the understanding of this regulation by demonstrating thatP. mirabilisrequires the generffGfor swarmer cell elongation and subsequent swarm motility. TherffGgene encodes a protein homologous to the dTDP-glucose 4,6 dehydratase protein ofEscherichia coli, which contributes to Enterobacterial Common Antigen biosynthesis. Here we characterize therffGgene inP. mirabilis, demonstrating that it is required for the production of large lipopolysaccharide-linked moieties necessary for wild-type cell envelope integrity. We show that absence of therffGgene induces several stress-responsive pathways including those controlled by the transcriptional regulators RpoS, CaiF, and RcsB. We further show that inrffG-deficient cells, suppression of the Rcs phosphorelay, via loss of RcsB, is sufficient to induce cell elongation and swarm motility. However, loss of RcsB does not rescue cell envelope integrity defects and instead results in abnormally shaped cells, including cells producing more than two poles. We conclude that a RcsB-mediated response acts to suppress emergence of shape defects in cell envelope-compromised cells, suggesting an additional role for RcsB in maintaining cell morphology under stress conditions. We further propose that the composition of the cell envelope acts as a checkpoint before cells initiate swarmer cell elongation and motility.Importance statementP. mirabilisswarm motility has been implicated in pathogenesis. We have found that cells deploy multiple uncharacterized strategies to handle cell envelope stress beyond the Rcs phosphorelay when attempting to engage in swarm motility. While RcsB is known to directly inhibit the master transcriptional regulator for swarming, we have shown an additional role for RcsB in protecting cell morphology. These data support a growing appreciation that the Rcs phosphorelay is a multi-functional regulator of cell morphology in addition to its role in microbial stress responses. These data also strengthen the paradigm that outer membrane composition is a crucial checkpoint for modulating entry into swarm motility. Furthermore, therffG-dependent moieties provide a novel, attractive target for potential antimicrobials.

scholarly journals The Rcs System in Enterobacteriaceae: Envelope Stress Responses and Virulence Regulation

2021 ◽  
Vol 12 ◽  
Author(s):  
Jiao Meng ◽  
Glenn Young ◽  
Jingyu Chen
Keyword(s):  
Stress Response ◽  
Stress Responses ◽  
Bacterial Infections ◽  
Pathogenic Bacteria ◽  
Cell Envelope ◽  
Regulatory System ◽  
Virulence Regulation ◽  
Bacterial Interaction ◽  
Envelope Stress

The bacterial cell envelope is a protective barrier at the frontline of bacterial interaction with the environment, and its integrity is regulated by various stress response systems. The Rcs (regulator of capsule synthesis) system, a non-orthodox two-component regulatory system (TCS) found in many members of the Enterobacteriaceae family, is one of the envelope stress response pathways. The Rcs system can sense envelope damage or defects and regulate the transcriptome to counteract stress, which is particularly important for the survival and virulence of pathogenic bacteria. In this review, we summarize the roles of the Rcs system in envelope stress responses (ESRs) and virulence regulation. We discuss the environmental and intrinsic sources of envelope stress that cause activation of the Rcs system with an emphasis on the role of RcsF in detection of envelope stress and signal transduction. Finally, the different regulation mechanisms governing the Rcs system’s control of virulence in several common pathogens are introduced. This review highlights the important role of the Rcs system in the environmental adaptation of bacteria and provides a theoretical basis for the development of new strategies for control, prevention, and treatment of bacterial infections.

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