Journal Articles
- Investigation of Bottleneck Enzyme Through Flux Balance Analysis to Improve Glycolic Acid Production in Escherichia coli
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Jungyeon Kim, Ye-Bin Kim, Ju-Young Kim, Min-Ju Seo, Soo-Jin Yeom, Bong Hyun Sung
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J. Microbiol. 2024;62(11):1023-1033. Published online October 28, 2024
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DOI: https://doi.org/10.1007/s12275-024-00175-4
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Abstract
- Amid rising environmental concerns, attempts have been made to produce glycolic acid (GA) using microbial processes with renewable carbon resources instead of using chemicals. The Dahms pathway for GA production uses xylose as a substrate and consists of relatively simple enzymatic steps. However, employing it leads to a decrease in cell growth and GA productivity. Systematically identifying and addressing metabolic bottlenecks in the Dahms pathway are essential for efficient glycolic acid (GA) production have not yet been performed. Through metabolic flux balance analysis, we found that insufficient aldehyde dehydrogenase (AldA) activity lowers GA production and negatively affects cell growth due to reduced energy production. Thus, we discovered a novel AldA isolated from Buttiauxella agrestis (BaAldA) demonstrated a 1.69-fold lower KM and a 1.49-fold higher turnover rate (kcat/KM) than AldA from Escherichia coli (EcAldA). GA production in E. coli harboring BaAldA was 1.59 times higher than in the original strain. Fed-batch fermentation of E. coli harboring BaAldA produced 22.70 g/L GA with a yield of 0.497 g/gxylose (98.2% of the theoretical maximum yield in the Dahms pathway), showing a higher final yield for GA than previously reported in E. coli. Our novel BaAldA enzyme shows great potential for the production of GA using microorganisms or enzymes. Furthermore, our approach to identifying metabolic bottlenecks using flux balance analysis could be utilized to enhance the microbial production of various desirable products in future studies.
- The putative polysaccharide synthase AfCps1 regulates Aspergillus fumigatus morphogenesis and conidia immune response in mouse bone marrow-derived macrophages
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Sha Wang , Anjie Yuan , Liping Zeng , Sikai Hou , Meng Wang , Lei Li , Zhendong Cai , Guowei Zhong
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J. Microbiol. 2021;59(1):64-75. Published online November 17, 2020
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DOI: https://doi.org/10.1007/s12275-021-0347-x
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4
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Abstract
- Aspergillus fumigatus is a well-known opportunistic pathogen
that causes invasive aspergillosis (IA) infections with high
mortality in immunosuppressed individuals. Morphogenesis,
including hyphal growth, conidiation, and cell wall biosynthesis
is crucial in A. fumigatus pathogenesis. Based on a previous
random insertional mutagenesis library, we identified
the putative polysaccharide synthase gene Afcps1 and its paralog
Afcps2. Homologs of the cps gene are commonly found
in the genomes of most fungal and some bacterial pathogens.
Afcps1/cpsA is important in sporulation, cell wall composition,
and virulence. However, the precise regulation patterns
of cell wall integrity by Afcps1/cpsA and further effects on the
immune response are poorly understood. Specifically, our
in-depth study revealed that Afcps1 affects cell-wall stability,
showing an increased resistance of ΔAfcps1 to the chitinmicrofibril
destabilizing compound calcofluor white (CFW)
and susceptibility of ΔAfcps1 to the β-(1,3)-glucan synthase
inhibitor echinocandin caspofungin (CS). Additionally, deletion
of Afcps2 had a normal sporulation phenotype but
caused hypersensitivity to Na+ stress, CFW, and Congo red
(CR). Specifically, quantitative analysis of cell wall composition
using high-performance anion exchange chromatography-
pulsed amperometric detector (HPAEC-PAD) analysis
revealed that depletion of Afcps1 reduced cell wall glucan
and chitin contents, which was consistent with the downregulation
of expression of the corresponding biosynthesis
genes. Moreover, an elevated immune response stimulated
by conidia of the ΔAfcps1 mutant in marrow-derived macrophages
(BMMs) during phagocytosis was observed. Thus,
our study provided new insights into the function of polysaccharide
synthase Cps1, which is necessary for the maintenance
of cell wall stability and the adaptation of conidia to
the immune response of macrophages in A. fumigatus.
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Citations
Citations to this article as recorded by

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Study on the metabolic changes and regulatory mechanism of
Aspergillus flavus
conidia germination
Sifan Jia, Chong Li, Yu An, Desheng Qi, Erik F. Y. Hom
Microbiology Spectrum.2024;[Epub] CrossRef - Chitin Biosynthesis in Aspergillus Species
Veronica S. Brauer, André M. Pessoni, Mateus S. Freitas, Marinaldo P. Cavalcanti-Neto, Laure N. A. Ries, Fausto Almeida
Journal of Fungi.2023; 9(1): 89. CrossRef - Evidencing New Roles for the Glycosyl-Transferase Cps1 in the Phytopathogenic Fungus Botrytis cinerea
Matthieu Blandenet, Isabelle R. Gonçalves, Christine Rascle, Jean-William Dupuy, François-Xavier Gillet, Nathalie Poussereau, Mathias Choquer, Christophe Bruel
Journal of Fungi.2022; 8(9): 899. CrossRef
Review
- REVIEW] Recent paradigm shift in the assembly of bacterial tripartite efflux pumps and the type I secretion system
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Inseong Jo , Jin-Sik Kim , Yongbin Xu , Jaekyung Hyun , Kangseok Lee , Nam-Chul Ha
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J. Microbiol. 2019;57(3):185-194. Published online February 26, 2019
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DOI: https://doi.org/10.1007/s12275-019-8520-1
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9
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Abstract
- Tripartite efflux pumps and the type I secretion system of
Gram-negative bacteria are large protein complexes that span
the entire cell envelope. These complexes expel antibiotics and
other toxic substances or transport protein toxins from bacterial
cells. Elucidating the binary and ternary complex structures
at an atomic resolution are crucial to understanding the
assembly and working mechanism. Recent advances in cryoelectron
microscopy along with the construction of chimeric
proteins drastically shifted the assembly models. In this review,
we describe the current assembly models from a historical
perspective and emphasize the common assembly mechanism
for the assembly of diverse tripartite pumps and type
I secretion systems.
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Citations
Citations to this article as recorded by

- Molecular mechanisms of antibiotic resistance revisited
Elizabeth M. Darby, Eleftheria Trampari, Pauline Siasat, Maria Solsona Gaya, Ilyas Alav, Mark A. Webber, Jessica M. A. Blair
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Vinaya Kumar Golla, Claudio Piselli, Ulrich Kleinekathöfer, Roland Benz
The Journal of Physical Chemistry B.2022; 126(7): 1388. CrossRef - Adaptation of the periplasm to maintain spatial constraints essential for cell envelope processes and cell viability
Eric Mandela, Christopher J Stubenrauch, David Ryoo, Hyea Hwang, Eli J Cohen, Von L Torres, Pankaj Deo, Chaille T Webb, Cheng Huang, Ralf B Schittenhelm, Morgan Beeby, JC Gumbart, Trevor Lithgow, Iain D Hay
eLife.2022;[Epub] CrossRef - Structure, Assembly, and Function of Tripartite Efflux and Type 1 Secretion Systems in Gram-Negative Bacteria
Ilyas Alav, Jessica Kobylka, Miriam S. Kuth, Klaas M. Pos, Martin Picard, Jessica M. A. Blair, Vassiliy N. Bavro
Chemical Reviews.2021; 121(9): 5479. CrossRef - Biotechnological applications of type 1 secretion systems
Zohreh Pourhassan N., Sander H.J. Smits, Jung Hoon Ahn, Lutz Schmitt
Biotechnology Advances.2021; 53: 107864. CrossRef - Protein-Protein Interactions in the Cytoplasmic Membrane of Escherichia coli: Influence of the Overexpression of Diverse Transporter-Encoding Genes on the Activities of PTS Sugar Uptake Systems
Mohammad Aboulwafa, Zhongge Zhang, Milton H. Saier Jr.
Microbial Physiology.2020; 30(1-6): 36. CrossRef - Perspectives towards antibiotic resistance: from molecules to population
Joon-Hee Lee
Journal of Microbiology.2019; 57(3): 181. CrossRef
Journal Article
- Contribution of EmrAB efflux pumps to colistin resistance in Acinetobacter baumannii
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Ming-Feng Lin , Yun-You Lin , Chung-Yu Lan
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J. Microbiol. 2017;55(2):130-136. Published online January 26, 2017
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DOI: https://doi.org/10.1007/s12275-017-6408-5
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Abstract
- Efflux pumps play an important role in antimicrobial resistance
for Acinetobacter baumannii. However, the function of
the Emr pump system and the relationship between Emr and
drug resistance has not been characterized in A. baumannii.
In this study, four possible groups of emr-like genes were
found by searching a genome database. Among them, A1S_
1772 (emrB) and A1S_1773 (emrA) were demonstrated to be
co-transcribed as a single operon. Moreover, during osmotic
stress, A1S_1772 showed the largest change in gene expression
compared to the other emrB-like genes, and deletion of
A1S_1772 (AB ΔemrB) significantly slowed cell growth in
20% sucrose. Using a phenotypic microarray analysis, the AB
ΔemrB mutant was more susceptible to colistin and nafcillin,
paromomycin, spiramycin, and D,L-serine hydroxmate than
the wild type. The spot assay, time kill assay and minimal
inhibition concentration determination also indicated that
the wild type could tolerate colistin better than the AB ΔemrB
mutant. Finally, the increased expression levels of all emrBlike
genes, including A1S_0775, A1S_0909, A1S_1772, and
A1S_1799, in colistin resistance-induced A. baumannii further
supported the possible involvement of the emrB genes
in A. baumannii colistin resistance. Together, the Emr pump
systems in A. baumannii contribute to adaptation to osmotic
stress and resistance to colistin.
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Research Support, Non-U.S. Gov't
- Mutational inactivation of OprD in carbapenem-resistant Pseudomonas aeruginosa isolates from Korean hospitals
-
Chi Hyun Kim , Hee Young Kang , Bo Ra Kim , Hyejin Jeon , Yoo Chul Lee , Sang Hwa Lee , Je Chul Lee
-
J. Microbiol. 2016;54(1):44-49. Published online January 5, 2016
-
DOI: https://doi.org/10.1007/s12275-016-5562-5
-
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43
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0
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20
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Abstract
- This study investigated the mechanisms underlying the carbapenem
resistance of bloodstream isolates of Pseudomonas
aeruginosa obtained from two Korean hospitals. Of the 79
P. aeruginosa isolates, 22 and 21 were resistant to imipenem
and meropenem, respectively. The 22 imipenem-resistant
P. aeruginosa isolates were classified into 7 sequence types
(STs) and 13 pulsotypes. Twelve imipenem-resistant isolates
from one hospital were found to belong to the international
clone ST111. Two imipenem-resistant P. aeruginosa ST235
isolates carried the blaIMP-6 gene, but the remaining 20 isolates
did not produce carbapenemases. Mutations in the oprD
gene and a related decrease in gene expression were found
in 21 and 5 isolates, respectively. However, all imipenemresistant
P. aeruginosa isolates showed no significant expression
of OprD in the outer membrane as compared with that
of carbapenem-susceptible PAO1 strain. Overexpression of
genes associated with efflux pumps, including mexB, mexD,
mexF, and mexY, was not found in any imipenem-resistant
isolate. One imipenem-resistant P. aeruginosa isolate overexpressed
the ampC gene. Our results show that the low permeability
of drugs due to the mutational inactivation of OprD
is primarily responsible for carbapenem resistance in bloodstream
isolates of P. aeruginosa from Korean hospitals.
-
Citations
Citations to this article as recorded by

Reviews
- MINIREVIEW] Multidrug efflux pumps in Staphylococcus aureus and their clinical implications
-
Soojin Jang
-
J. Microbiol. 2016;54(1):1-8. Published online January 5, 2016
-
DOI: https://doi.org/10.1007/s12275-016-5159-z
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-
46
View
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0
Download
-
78
Crossref
-
Abstract
- Antibiotic resistance is rapidly spreading among bacteria
such as Staphylococcus aureus, an opportunistic bacterial
pathogen that causes a variety of diseases in humans. For
the last two decades, bacterial multidrug efflux pumps have
drawn attention due to their potential association with clinical
multidrug resistance. Numerous researchers have demonstrated
efflux-mediated resistance in vitro and in vivo
and found novel multidrug transporters using advanced
genomic information about bacteria. This article aims to
provide a concise summary of multidrug efflux pumps and
their important clinical implications, focusing on recent
findings concerning S. aureus efflux pumps.
-
Citations
Citations to this article as recorded by

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Durairaj Thiyagarajan, Gopal Das, Aiyagari Ramesh
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Serajus Salaheen, Mengfei Peng, Jungsoo Joo, Hironori Teramoto, Debabrata Biswas
Frontiers in Microbiology.2017;[Epub] CrossRef - Multidrug Efflux Pumps at the Crossroad between Antibiotic Resistance and Bacterial Virulence
Manuel Alcalde-Rico, Sara Hernando-Amado, Paula Blanco, José L. Martínez
Frontiers in Microbiology.2016;[Epub] CrossRef
- MINIREVIEW] Molecular architecture of the bacterial tripartite multidrug efflux pump focusing on the adaptor bridging model
-
Saemee Song , Jin-Sik Kim , Kangseok Lee , Nam-Chul Ha
-
J. Microbiol. 2015;53(6):355-364. Published online May 30, 2015
-
DOI: https://doi.org/10.1007/s12275-015-5248-4
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47
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Abstract
- Gram-negative bacteria expel a wide range of toxic substances
through tripartite drug efflux pumps consisting of an inner
membrane transporter, an outer membrane channel protein,
and a periplasmic adaptor protein. These pumps form tripartite
assemblies which can span the entire cell envelope,
including the inner and outer membranes. There have been
controversial findings regarding the assembly of the individual
components in tripartite drug efflux pumps. Recent
structural and functional studies have advanced our understanding
of the assembly and working mechanisms of the
pumps. Here, we re-evaluate the assembly models based on
recent structural and functional studies. In particular, this
study focuses on the ‘adaptor bridging model’, highlighting
the intermeshing cogwheel-like interactions between the tip
regions of the outer membrane channel protein and the periplasmic
adaptor protein in the hexameric assembly.
-
Citations
Citations to this article as recorded by

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Jingwei Weng, Wenning Wang
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Reinke T. Müller, Timothy Travers, Hi-jea Cha, Joshua L. Phillips, S. Gnanakaran, Klaas M. Pos
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PLOS ONE.2016; 11(5): e0155846. CrossRef
Research Support, Non-U.S. Gov'ts
- Effect of carbonyl cyanide 3-chlorophenylhydrazone (CCCP) on killing Acinetobacter baumannii by colistin
-
Young Kyoung Park , Kwan Soo Ko
-
J. Microbiol. 2015;53(1):53-59. Published online January 4, 2015
-
DOI: https://doi.org/10.1007/s12275-015-4498-5
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49
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Abstract
- We investigated the effect of cyanide 3-chlorophenylhydrazone
(CCCP) and other efflux pump inhibitors (EPIs) on the
colistin susceptibility in Acinetobacter baumannii. While minimum
inhibitory concentrations (MICs) of colistin in all
colistin-resistant strains decreased significantly with 25 μM
of CCCP and 2,4-dinitrophenol (DNP), phenyl-arginine-β-
naphthylamide (PAβN), and reserpine did not decrease the
colistin MICs. However, CCCP and DNP as well as PAβN
and reserpine did not have a significant effect on the MICs of
the other agents. Efflux pump gene expressions in colistinresistant
strains were not increased compared with those in
colistin-susceptible strains. When only 5X MIC of colistin (5
mg/L) was provided to a colistin-susceptible A. baumannii
strain, the bacterial cell number was reduced by 9 h after exposure
to colistin, but regrowth was observed. When CCCP
was added to colistin, bacterial cells were completely killed
after 24 to 48 h of incubation, which was not due to the toxicity
of CCCP itself. Colistin resistance in A. baumannii may
not be due to efflux pumps. Our present study suggests that
bacterial cells with reduced metabolic activity by CCCP are
more susceptible to colistin in A. baumannii. It may show
the possibility that combined therapy with colistin and other
antimicrobial agents could effective against A. baumannii
infections.
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- Analysis of cepA Encoding an Efflux Pump-like Protein in Corynebacterium glutamicum
-
Soo-Yeon Sim , Eun-Ji Hong , Younhee Kim , Heung-Shick Lee
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J. Microbiol. 2014;52(4):278-283. Published online February 17, 2014
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DOI: https://doi.org/10.1007/s12275-014-3461-1
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Abstract
- A gene encoding a homolog of purine efflux proteins of Escherichia coli and Bacillus subtilis was identified in the genome of Corynebacterium glutamicum and designated as cepA. The gene encoded a putative protein product, containing
12 transmembrane helixes, which is a typical feature of integral membrane transport proteins. To elucidate the function of the gene, we constructed a cepA deletion mutant (ΔcepA) and a cepA-overexpressing strain and analyzed their physiological characteristics. The cepA gene could be deleted with no critical effect on cell growth. However, the cell yield of a ΔcepA strain was decreased by 10% as compared to that of a strain carrying a cepA-overexpression plasmid (P180-cepA). Further analysis identified increased resistance of the P180-cepA strain to the purine analogues 6-mercaptopurine and 6-mercaptoguanine, but not to 2-aminopurine and purine nucleoside analogues. Moreover, this strain showed increased resistance to the antibiotics nalidixic acid and ampicillin. Collectively, these data suggest that cepA is a novel multidrug resistance gene and probably functions in the efflux of toxic substances from the inside of cells to the environment, thus allowing cells to reach a higher cell yield.
-
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- AutoBioTech─A Versatile Biofoundry for Automated Strain Engineering
Tobias Michael Rosch, Julia Tenhaef, Tim Stoltmann, Till Redeker, Dominic Kösters, Niels Hollmann, Karin Krumbach, Wolfgang Wiechert, Michael Bott, Susana Matamouros, Jan Marienhagen, Stephan Noack
ACS Synthetic Biology.2024; 13(7): 2227. CrossRef
- Interaction between the α-Barrel Tip of Vibrio vulnificus TolC Homologs and AcrA Implies the Adapter Bridging Model
-
Seunghwa Lee , Saemee Song , Minho Lee , Soonhye Hwang , Ji-Sun Kim , Nam-Chul Ha , Kangseok Lee
-
J. Microbiol. 2014;52(2):148-153. Published online February 1, 2014
-
DOI: https://doi.org/10.1007/s12275-014-3578-2
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45
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10
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Abstract
- The AcrAB-TolC multidrug efflux pump confers resistance to Escherichia coli against many antibiotics and toxic compounds. The TolC protein is an outer membrane factor that participates in the formation of type I secretion systems. The genome of Vibrio vulnificus encodes two proteins homologous to the E. coli TolC, designated TolCV1 and TolCV2. Here, we show that both TolCV1 and TolCV2 partially complement the E. coli TolC function and physically interact with the membrane fusion protein AcrA, a component of the E. coli AcrAB-TolC efflux pump. Using site-directed mutational analyses and an in vivo cross-linking assay, we demonstrated that the α-barrel tip region of TolC homologs plays a critical role in the formation of functional AcrAB-TolC efflux pumps. Our findings suggest the adapter bridging model as a general assembly mechanism for tripartite drug efflux pumps in Gram-negative bacteria.
-
Citations
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- Progress of Antimicrobial Mechanisms of Stilbenoids
Xiancai Li, Yongqing Li, Binghong Xiong, Shengxiang Qiu
Pharmaceutics.2024; 16(5): 663. CrossRef - Membrane Efflux Pumps of Pathogenic Vibrio Species: Role in Antimicrobial Resistance and Virulence
Jerusha Stephen, Manjusha Lekshmi, Parvathi Ammini, Sanath H. Kumar, Manuel F. Varela
Microorganisms.2022; 10(2): 382. CrossRef - TolCV1 Has Multifaceted Roles During Vibrio vulnificus Infection
Yue Gong, Rui Hong Guo, Joon Haeng Rhee, Young Ran Kim
Frontiers in Cellular and Infection Microbiology.2021;[Epub] CrossRef - Recent paradigm shift in the assembly of bacterial tripartite efflux pumps and the type I secretion system
Inseong Jo, Jin-Sik Kim, Yongbin Xu, Jaekyung Hyun, Kangseok Lee, Nam-Chul Ha
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Seunghwa Lee, Ji-Hyun Yeom, Sojin Seo, Minho Lee, Sarang Kim, Jeehyeon Bae, Kangseok Lee, Jihwan Hwang
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Saemee Song, Jin-Sik Kim, Kangseok Lee, Nam-Chul Ha
Journal of Microbiology.2015; 53(6): 355. CrossRef - Interaction Mediated by the Putative Tip Regions of MdsA and MdsC in the Formation of a Salmonella-Specific Tripartite Efflux Pump
Saemee Song, Soonhye Hwang, Seunghwa Lee, Nam-Chul Ha, Kangseok Lee, Eric Cascales
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Seunghwa Lee, Saemee Song, Kangseok Lee
Current Microbiology.2014; 68(6): 729. CrossRef
- The PseEF Efflux System Is a Virulence Factor of Pseudomonas syringae pv. syringae
-
Hyosun Cho , Hyojeung Kang
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J. Microbiol. 2012;50(1):79-90. Published online February 27, 2012
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DOI: https://doi.org/10.1007/s12275-012-1353-9
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Abstract
- An ATP-binding cassette (ABC) transporter, called the PseEF
efflux system, was identified at the left border of the syr-syp
genomic island of Pseudomonas syringae pv. syringae strain
B301D. The PseEF efflux system was located within a 3.3-kb
operon that encodes a periplasmic membrane fusion protein
(PseE), and an ABC-type cytoplasmic membrane protein
(PseF). The PseEF efflux system exhibited amino acid homology
to a putative ABC efflux system (MacAB) of E. coli
W3104 with identities of 47.2% (i.e., PseE to MacA) and
57.6% (i.e., PseF to MacB). A nonpolar mutation within the
pseF gene was generated by nptII insertional mutagenesis.
The resultant mutant strain showed significant reduction in
secretion of syringomycin (74%) and syringopeptin (71%),
as compared to parental strain B301D. Quantitative real-time
RT-PCR was used to determine transcript levels of the syringomycin
(syrB1) and syringopeptin (sypA) synthetase
genes in strain B301D-HK7 (a pseF mutant). Expression of
the sypA gene by mutant strain B301D-HK7 was approximately
6.9% as compared to that of parental strain B301D,
while the syrB1 gene expression by mutant strain B301D-HK7
was nearly 14.6%. In addition, mutant strain B301D-HK7
was less virulent by approximately 67% than parental strain
B301D in immature cherry fruits. Mutant strain B301D-HK7
was not reduced in resistance to any antibiotics used in this
study as compared to parental strain B301D. Expression
(transcript levels) of the pseF gene was induced approximately
six times by strain B301D grown on syringomycin
minimum medium (SRM) supplemented with the plant signal
molecules arbutin and D-fructose (SRMAF), as compared to
that of strain B301D grown on SRM (in the absence of plant
signal molecules). In addition, during infection of bean
plants by P. syringae pv. syringae strain B728a, expression
of the pseF gene increased at 3 days after inoculation (dai).
More than 180-fold induction was observed in transcript
levels of the pseF gene by parental strain B728a as compared
to strain B728a-SL7 (a salA mutant). Thus, the PseEF
efflux system, an ABC-type efflux system, has an important
role in secretion of syringomycin and syringopeptin, and is
required for full virulence in P. syringae pv. syringae.
- Functional Definition of LuxS, an Autoinducer-2 (AI-2) Synthase and Its Role in Full Virulence of Streptococcus suis Serotype 2
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Min Cao , Youjun Feng , Changjun Wang , Feng Zheng , Ming Li , Hui Liao , Yinghua Mao , Xiuzhen Pan , Jing Wang , Dan Hu , Fuquan Hu , Jiaqi Tang
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J. Microbiol. 2011;49(6):1000-1011. Published online December 28, 2011
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DOI: https://doi.org/10.1007/s12275-011-1523-1
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Abstract
- Quorum sensing is a widespread chemical communication in response to fluctuation of bacterial population density, and has been implicated into bacterial biofilm formation and regulation of expression of virulence factors. The luxS gene product, S-ribosylhomocysteinase, catalizes the last committed step in biosynthetic pathway of autoinducer 2 (AI-2), a signaling molecule for inter-species quorum sensing. We found a luxS homologue in 05ZYH33, an epidemic strain of Streptococcus suis serotype 2 (SS2) in China. A luxS null mutant (ΔluxS) of 05ZYH33 strain was obtained using an approach of homologous recombination. LuxS was determined to be required for AI-2 production in 05ZYH33 strain of S. suis 2. Inactivation of luxS gene led to a wide range of phenotypic changes including thinner capsular walls, increased tolerance to H2O2, reduced adherence capacity to epithelial cells, etc. In particular, loss of LuxS impaired dramatically its full virulence of SS2 in experimental model of piglets, and functional complementation restored it nearly to the level of parent strain. Genome-wide transcriptome analyses suggested that some known virulence factors such as CPS are down-regulated in the ΔluxS mutant, which might in part explain virulence attenuation by luxS deletion. Similarly, 29 of 71 genes with different expression level were proposed to be targets candidate regulated by LuxS/AI-2-dependent quorum sensing.
- Periplasmic Domain of CusA in an Escherichia coli Cu+/Ag+ Transporter Has Metal Binding Sites
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Bo-Young Yun , Yongbin Xu , Shunfu Piao , Nahee Kim , Jeong-Hyun Yoon , Hyun-Soo Cho , Kangseok Lee , Nam-Chul Ha
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J. Microbiol. 2010;48(6):829-835. Published online January 9, 2011
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DOI: https://doi.org/10.1007/s12275-010-0339-8
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6
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Abstract
- The resistance nodulation division (RND)-type efflux systems are utilized in Gram-negative bacteria to export a variety of substrates. The CusCFBA system is the Cu+ and Ag+ efflux system in Escherichia coli, conferring resistance to lethal concentrations of Cu+ and Ag+. The periplasmic component, CusB, which is
essential for the assembly of the protein complex, has Cu+ or Ag+ binding sites. The twelve-span membrane protein CusA is a homotrimeric transporter, and has a relatively large periplasmic domain. Here, we constructed the periplasmic domain of CusA by joining two DNA segments and then successfully expressed and purified the protein. Isothermal titration calorimetry experiments revealed Ag+ binding sites with Kds of 10-6-10-5 M. Our findings suggest that the metal binding in the periplasmic domain of CusA might play an important role in the function of the efflux pump.
- Identification of Vibrio natriegens uvrA and uvrB Genes and Analysis of Gene Regulation Using Transcriptional Reporter Plasmids
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Keryn L. Simons , Susan M. Thomas , Peter A. Anderson
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J. Microbiol. 2010;48(5):644-656. Published online November 3, 2010
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DOI: https://doi.org/10.1007/s12275-010-9370-z
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6
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Abstract
- Nucleotide excision repair (NER) rectifies a variety of chemically and structurally distinct DNA lesions. The current model of NER is based upon the enteric bacterium Escherichia coli and there is scarce information about how other bacterial species respond to, and correct, DNA damage. Here we report the isolation and functional analysis of the uvrA and uvrB genes from Vibrio natriegens, a naturally occurring marine bacterium. Genetic studies were completed to assess the repair capabilities of V. natriegens uvrA and uvrB in E. coli uvrA and uvrB mutants. In addition to the genetic studies, transcriptional fusions between the luciferase gene and the 5′ regulatory regions of uvrA and uvrB gene of V. natriegens and E. coli were constructed. Luminescent measurements from E. coli transformed with these constructs showed that whilst the response to UV irradiation of either E. coli or V. natriegens uvrA regulatory sequences was similar, both the rate and induction of luminescence detected from the uvrB regulatory regions differed.
Journal Article
- Molecular Characteristics and Resistant Mechanisms of Imipenem-Resistant Acinetobacter baumannii Isolates in Shenyang, China
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Jing Ping Zhang , Wan Zhu , Su Fei Tian , Yun Zhuo Chu , Bai Yi Chen
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J. Microbiol. 2010;48(5):689-694. Published online November 3, 2010
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DOI: https://doi.org/10.1007/s12275-010-0137-3
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Abstract
- The investigation was carried out to elucidate the molecular characteristics and resistant mechanisms of imipenem-resistant Acinetobacter baumannii. Thirty-seven isolates were collected from January 2007 to December 2007. The homology of the isolates was analyzed by both pulsed field gel electrophoresis (PFGE) and multilocus sequence typing (MLST). The genes of β-lactamases, adeB, and class 1 integron were polymerase chain reaction amplified. Genotype analysis of the 37 A. baumannii isolates by PFGE revealed the circulation of four PFGE types (A-D) ; the A- and B-type accounted for 48.6% and 40.5%, respectively. MLST showed the existence of three allelic profiles. The agar dilution method was carried out to determine the MIC of imipenem, in the absence or presence of carbonyl cyanide m-chlorophenylhydrazone (CCCP, 10 μg/ml). The MICs of the strains to imipenem were between 16 μg/ml and 128 μg/ml. When CCCP was added, a MIC decrease of at least four-fold was observed in 20 isolates, which belonged to the A- or C-type. AdeB and blaPER-1 genes were each detected in 35 isolates, blaOXA-23 gene in 34 isolates and blaOXA-58-like gene in 24 isolates. All isolates harbored blaOXA-51-like genes. No isolates carried the blaIMP-1 gene. Integron was detected in 25 isolates, which mediated the resistance to aminoglycosides and rifampin. The epidemiologic data suggested that the increasing infection of A. baumannii in our hospital was mainly caused by the inter-hospital spread of two epidemic clones. The AdeABC efflux system may be the important factor that leads to the high level of imipenem-resistance in PFGE A-type.