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TolB protein of Escherichia coli K‐12 interacts with the outer membrane peptidoglycan‐associated proteins Pal, Lpp and OmpA

k-12

Germon P.
GSID: w0Y0ioKFfvcJ
T Clavel, P Germon, A Vianney, R Portalier… - Molecular …, 1998 - Wiley Online Library

… coli K-12 consists of several proteins that form two complexes in the cell envelope. The TolQ, TolR and TolA proteins are located in the … coli K-12 strains used in this study were all derivatives of strain JC8056...

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Clavel, T., Germon, P., Vianney, A., Portalier, R., & Lazzaroni, J. C. (1998). TolB protein of Escherichia coli K‐12 interacts with the outer membrane peptidoglycan‐associated proteins Pal, Lpp and OmpA. Molecular microbiology, 29(1), 359-367.
Clavel, Thierry, et al. "TolB protein of Escherichia coli K‐12 interacts with the outer membrane peptidoglycan‐associated proteins Pal, Lpp and OmpA." Molecular microbiology 29.1 (1998): 359-367.
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Evolution of peptidoglycan biosynthesis under the selective pressure of antibiotics in Gram-positive bacteria

STEM and diversification

Mayer C.
GSID: KvSpWv36YjQJ
JL Mainardi, R Villet, TD Bugg, C Mayer… - FEMS microbiology …, 2008 - academic.oup.com

… for diversification of the fifth position of stem pentapeptides … Diversification of the side chain of the precursors, presumably … Diversification of the side chains has been accompanied by …

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Mainardi, J. L., Villet, R., Bugg, T. D., Mayer, C., & Arthur, M. (2008). Evolution of peptidoglycan biosynthesis under the selective pressure of antibiotics in Gram-positive bacteria. FEMS microbiology reviews, 32(2), 386-408.
Mainardi, Jean-Luc, et al. "Evolution of peptidoglycan biosynthesis under the selective pressure of antibiotics in Gram-positive bacteria." FEMS microbiology reviews 32.2 (2008): 386-408.
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Molecular Mechanisms and Clinical Impact of Acquired and Intrinsic Fosfomycin Resistance.

Antibiotics (Basel, Switzerland)

Castañeda-García A, Blázquez J, Rodríguez-Rojas A.
PMID: 27029300
Antibiotics (Basel). 2013 Apr 16;2(2):217-36. doi: 10.3390/antibiotics2020217.

Bacterial infections caused by antibiotic-resistant isolates have become a major health problem in recent years, since they are very difficult to treat, leading to an increase in morbidity and mortality. Fosfomycin is a broad-spectrum bactericidal antibiotic that inhibits cell...

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Castañeda-García A, Blázquez J, Rodríguez-Rojas A. Molecular Mechanisms and Clinical Impact of Acquired and Intrinsic Fosfomycin Resistance. Antibiotics (Basel). 2013;2(2):217-36doi: 10.3390/antibiotics2020217.
Castañeda-García, A., Blázquez, J., & Rodríguez-Rojas, A. (2013). Molecular Mechanisms and Clinical Impact of Acquired and Intrinsic Fosfomycin Resistance. Antibiotics (Basel, Switzerland), 2(2), 217-36. https://doi.org/10.3390/antibiotics2020217
Castañeda-García, Alfredo, et al. "Molecular Mechanisms and Clinical Impact of Acquired and Intrinsic Fosfomycin Resistance." Antibiotics (Basel, Switzerland) vol. 2,2 (2013): 217-36. doi: https://doi.org/10.3390/antibiotics2020217
Castañeda-García A, Blázquez J, Rodríguez-Rojas A. Molecular Mechanisms and Clinical Impact of Acquired and Intrinsic Fosfomycin Resistance. Antibiotics (Basel). 2013 Apr 16;2(2):217-36. doi: 10.3390/antibiotics2020217. PMID: 27029300; PMCID: PMC4790336.
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The endolysin from the Enterococcus faecalis bacteriophage VD13 and conditions stimulating its lytic activity.

FEMS microbiology letters

Swift SM, Rowley DT, Young C, Franks A, Hyman P, Donovan DM.
PMID: 27634307
FEMS Microbiol Lett. 2016 Oct 01;363(19). doi: 10.1093/femsle/fnw216.

Bacteriophages produce endolysins (peptidoglycan hydrolases) to lyse the host cell from within and release nascent bacteriophage particles. Recombinant endolysins can lyse Gram-positive bacteria when added exogenously. As a potential alternative antimicrobial, we cloned and expressed the enterococcal VD13 bacteriophage...

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Swift SM, Rowley DT, Young C, et al. The endolysin from the Enterococcus faecalis bacteriophage VD13 and conditions stimulating its lytic activity. FEMS Microbiol Lett. 2016;363(19)doi: 10.1093/femsle/fnw216.
Swift, S. M., Rowley, D. T., Young, C., Franks, A., Hyman, P., & Donovan, D. M. (2016). The endolysin from the Enterococcus faecalis bacteriophage VD13 and conditions stimulating its lytic activity. FEMS microbiology letters, 363(19), . https://doi.org/10.1093/femsle/fnw216
Swift, Steven M, et al. "The endolysin from the Enterococcus faecalis bacteriophage VD13 and conditions stimulating its lytic activity." FEMS microbiology letters vol. 363,19 (2016). doi: https://doi.org/10.1093/femsle/fnw216
Swift SM, Rowley DT, Young C, Franks A, Hyman P, Donovan DM. The endolysin from the Enterococcus faecalis bacteriophage VD13 and conditions stimulating its lytic activity. FEMS Microbiol Lett. 2016 Oct 01;363(19). doi: 10.1093/femsle/fnw216. PMID: 27634307.
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The Peptidoglycan Pattern of Staphylococcus carnosus TM300-Detailed Analysis and Variations Due to Genetic and Metabolic Influences.

Antibiotics (Basel, Switzerland)

Deibert J, Kühner D, Stahl M, Koeksoy E, Bertsche U.
PMID: 27669322
Antibiotics (Basel). 2016 Sep 23;5(4). doi: 10.3390/antibiotics5040033.

The Gram-positive bacterium Staphylococcus carnosus (S. carnosus) TM300 is an apathogenic staphylococcal species commonly used in meat starter cultures. As with all Gram-positive bacteria, its cytoplasmic membrane is surrounded by a thick peptidoglycan (PGN) or murein sacculus consisting of...

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Deibert J, Kühner D, Stahl M, et al. The Peptidoglycan Pattern of Staphylococcus carnosus TM300-Detailed Analysis and Variations Due to Genetic and Metabolic Influences. Antibiotics (Basel). 2016;5(4)doi: 10.3390/antibiotics5040033.
Deibert, J., Kühner, D., Stahl, M., Koeksoy, E., & Bertsche, U. (2016). The Peptidoglycan Pattern of Staphylococcus carnosus TM300-Detailed Analysis and Variations Due to Genetic and Metabolic Influences. Antibiotics (Basel, Switzerland), 5(4), . https://doi.org/10.3390/antibiotics5040033
Deibert, Julia, et al. "The Peptidoglycan Pattern of Staphylococcus carnosus TM300-Detailed Analysis and Variations Due to Genetic and Metabolic Influences." Antibiotics (Basel, Switzerland) vol. 5,4 (2016). doi: https://doi.org/10.3390/antibiotics5040033
Deibert J, Kühner D, Stahl M, Koeksoy E, Bertsche U. The Peptidoglycan Pattern of Staphylococcus carnosus TM300-Detailed Analysis and Variations Due to Genetic and Metabolic Influences. Antibiotics (Basel). 2016 Sep 23;5(4). doi: 10.3390/antibiotics5040033. PMID: 27669322; PMCID: PMC5187514.
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Highly Variable Streptococcus oralis Strains Are Common among Viridans Streptococci Isolated from Primates.

mSphere

Denapaite D, Rieger M, Köndgen S, Brückner R, Ochigava I, Kappeler P, Mätz-Rensing K, Leendertz F, Hakenbeck R.
PMID: 27303717
mSphere. 2016 Mar 09;1(2). doi: 10.1128/mSphere.00041-15. eCollection 2016.

Viridans streptococci were obtained from primates (great apes, rhesus monkeys, and ring-tailed lemurs) held in captivity, as well as from free-living animals (chimpanzees and lemurs) for whom contact with humans is highly restricted. Isolates represented a variety of viridans...

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Denapaite D, Rieger M, Köndgen S, et al. Highly Variable Streptococcus oralis Strains Are Common among Viridans Streptococci Isolated from Primates. mSphere. 2016;1(2)doi: 10.1128/mSphere.00041-15.
Denapaite, D., Rieger, M., Köndgen, S., Brückner, R., Ochigava, I., Kappeler, P., Mätz-Rensing, K., Leendertz, F., & Hakenbeck, R. (2016). Highly Variable Streptococcus oralis Strains Are Common among Viridans Streptococci Isolated from Primates. mSphere, 1(2), . https://doi.org/10.1128/mSphere.00041-15
Denapaite, Dalia, et al. "Highly Variable Streptococcus oralis Strains Are Common among Viridans Streptococci Isolated from Primates." mSphere vol. 1,2 (2016). doi: https://doi.org/10.1128/mSphere.00041-15
Denapaite D, Rieger M, Köndgen S, Brückner R, Ochigava I, Kappeler P, Mätz-Rensing K, Leendertz F, Hakenbeck R. Highly Variable Streptococcus oralis Strains Are Common among Viridans Streptococci Isolated from Primates. mSphere. 2016 Mar 09;1(2). doi: 10.1128/mSphere.00041-15. eCollection 2016. PMID: 27303717; PMCID: PMC4863584.
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Analysis of five complete genome sequences for members of the class Peribacteria in the recently recognized Peregrinibacteria bacterial phylum.

PeerJ

Anantharaman K, Brown CT, Burstein D, Castelle CJ, Probst AJ, Thomas BC, Williams KH, Banfield JF.
PMID: 26844018
PeerJ. 2016 Jan 28;4:e1607. doi: 10.7717/peerj.1607. eCollection 2016.

Five closely related populations of bacteria from the Candidate Phylum (CP) Peregrinibacteria, part of the bacterial Candidate Phyla Radiation (CPR), were sampled from filtered groundwater obtained from an aquifer adjacent to the Colorado River near the town of Rifle,...

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Anantharaman K, Brown CT, Burstein D, et al. Analysis of five complete genome sequences for members of the class Peribacteria in the recently recognized Peregrinibacteria bacterial phylum. PeerJ. 2016;4:e1607doi: 10.7717/peerj.1607.
Anantharaman, K., Brown, C. T., Burstein, D., Castelle, C. J., Probst, A. J., Thomas, B. C., Williams, K. H., & Banfield, J. F. (2016). Analysis of five complete genome sequences for members of the class Peribacteria in the recently recognized Peregrinibacteria bacterial phylum. PeerJ, 4e1607. https://doi.org/10.7717/peerj.1607
Anantharaman, Karthik, et al. "Analysis of five complete genome sequences for members of the class Peribacteria in the recently recognized Peregrinibacteria bacterial phylum." PeerJ vol. 4 (2016): e1607. doi: https://doi.org/10.7717/peerj.1607
Anantharaman K, Brown CT, Burstein D, Castelle CJ, Probst AJ, Thomas BC, Williams KH, Banfield JF. Analysis of five complete genome sequences for members of the class Peribacteria in the recently recognized Peregrinibacteria bacterial phylum. PeerJ. 2016 Jan 28;4:e1607. doi: 10.7717/peerj.1607. eCollection 2016. PMID: 26844018; PMCID: PMC4736985.
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Cell Wall-active Bacteriocins and Their Applications Beyond Antibiotic Activity.

Probiotics and antimicrobial proteins

Roces C, Rodríguez A, Martínez B.
PMID: 26782186
Probiotics Antimicrob Proteins. 2012 Dec;4(4):259-72. doi: 10.1007/s12602-012-9116-9.

Microorganisms synthesize several compounds with antimicrobial activity in order to compete or defend themselves against others and ensure their survival. In this line, the cell wall is a major protective barrier whose integrity is essential for many vital bacterial...

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Roces C, Rodríguez A, Martínez B. Cell Wall-active Bacteriocins and Their Applications Beyond Antibiotic Activity. Probiotics Antimicrob Proteins. 2012;4(4):259-72doi: 10.1007/s12602-012-9116-9.
Roces, C., Rodríguez, A., & Martínez, B. (2012). Cell Wall-active Bacteriocins and Their Applications Beyond Antibiotic Activity. Probiotics and antimicrobial proteins, 4(4), 259-72. https://doi.org/10.1007/s12602-012-9116-9
Roces, Clara, et al. "Cell Wall-active Bacteriocins and Their Applications Beyond Antibiotic Activity." Probiotics and antimicrobial proteins vol. 4,4 (2012): 259-72. doi: https://doi.org/10.1007/s12602-012-9116-9
Roces C, Rodríguez A, Martínez B. Cell Wall-active Bacteriocins and Their Applications Beyond Antibiotic Activity. Probiotics Antimicrob Proteins. 2012 Dec;4(4):259-72. doi: 10.1007/s12602-012-9116-9. PMID: 26782186.
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The Mechanism Underlying the Antibacterial Activity of Shikonin against Methicillin-Resistant Staphylococcus aureus.

Evidence-based complementary and alternative medicine : eCAM

Lee YS, Lee DY, Kim YB, Lee SW, Cha SW, Park HW, Kim GS, Kwon DY, Lee MH, Han SH.
PMID: 26265924
Evid Based Complement Alternat Med. 2015;2015:520578. doi: 10.1155/2015/520578. Epub 2015 Jul 21.

Shikonin (SKN), a highly liposoluble naphthoquinone pigment isolated from the roots of Lithospermum erythrorhizon, is known to exert antibacterial, wound-healing, anti-inflammatory, antithrombotic, and antitumor effects. The aim of this study was to examine SKN antibacterial activity against methicillin-resistant Staphylococcus...

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Lee YS, Lee DY, Kim YB, et al. The Mechanism Underlying the Antibacterial Activity of Shikonin against Methicillin-Resistant Staphylococcus aureus. Evid Based Complement Alternat Med. 2015;2015:520578doi: 10.1155/2015/520578.
Lee, Y. S., Lee, D. Y., Kim, Y. B., Lee, S. W., Cha, S. W., Park, H. W., Kim, G. S., Kwon, D. Y., Lee, M. H., & Han, S. H. (2015). The Mechanism Underlying the Antibacterial Activity of Shikonin against Methicillin-Resistant Staphylococcus aureus. Evidence-based complementary and alternative medicine : eCAM, 2015520578. https://doi.org/10.1155/2015/520578
Lee, Young-Seob, et al. "The Mechanism Underlying the Antibacterial Activity of Shikonin against Methicillin-Resistant Staphylococcus aureus." Evidence-based complementary and alternative medicine : eCAM vol. 2015 (2015): 520578. doi: https://doi.org/10.1155/2015/520578
Lee YS, Lee DY, Kim YB, Lee SW, Cha SW, Park HW, Kim GS, Kwon DY, Lee MH, Han SH. The Mechanism Underlying the Antibacterial Activity of Shikonin against Methicillin-Resistant Staphylococcus aureus. Evid Based Complement Alternat Med. 2015;2015:520578. doi: 10.1155/2015/520578. Epub 2015 Jul 21. PMID: 26265924; PMCID: PMC4523682.
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EzrA: a spectrin-like scaffold in the bacterial cell division machinery.

Microbial cell (Graz, Austria)

Cleverley R, Lewis R.
PMID: 28357277
Microb Cell. 2015 Jan 15;2(2):59-61. doi: 10.15698/mic2015.02.187.

Much progress has been made in identifying the components of the divisome, the assembly of proteins that undertakes the vital process of cell division in bacteria. However, how the highly interdependent processes on either side of the membrane are...

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Cleverley R, Lewis R. EzrA: a spectrin-like scaffold in the bacterial cell division machinery. Microb Cell. 2015;2(2):59-61doi: 10.15698/mic2015.02.187.
Cleverley, R., & Lewis, R. (2015). EzrA: a spectrin-like scaffold in the bacterial cell division machinery. Microbial cell (Graz, Austria), 2(2), 59-61. https://doi.org/10.15698/mic2015.02.187
Cleverley, Robert, and Lewis, Richard. "EzrA: a spectrin-like scaffold in the bacterial cell division machinery." Microbial cell (Graz, Austria) vol. 2,2 (2015): 59-61. doi: https://doi.org/10.15698/mic2015.02.187
Cleverley R, Lewis R. EzrA: a spectrin-like scaffold in the bacterial cell division machinery. Microb Cell. 2015 Jan 15;2(2):59-61. doi: 10.15698/mic2015.02.187. PMID: 28357277; PMCID: PMC5354558.
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Use of Toll-like receptor assays for the detection of bacterial contaminations in icodextrin batches released for peritoneal dialysis.

Toxicology reports

Hacine-Gherbi H, Denys A, Carpentier M, Heysen A, Duflot P, Lanos P, Allain F.
PMID: 29152461
Toxicol Rep. 2017 Oct 23;4:566-573. doi: 10.1016/j.toxrep.2017.10.004. eCollection 2017.

Icodextrin is a starch derivative used for preparing solutions of peritoneal dialysis. Unfortunately, peptidoglycans (PGN) and lipopolysaccharides (LPS) have been reported to contaminate certain icodextrin batches and to contribute to the development of sterile peritonitis. The decision of selecting...

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Hacine-Gherbi H, Denys A, Carpentier M, et al. Use of Toll-like receptor assays for the detection of bacterial contaminations in icodextrin batches released for peritoneal dialysis. Toxicol Rep. 2017;4:566-573doi: 10.1016/j.toxrep.2017.10.004.
Hacine-Gherbi, H., Denys, A., Carpentier, M., Heysen, A., Duflot, P., Lanos, P., & Allain, F. (2017). Use of Toll-like receptor assays for the detection of bacterial contaminations in icodextrin batches released for peritoneal dialysis. Toxicology reports, 4566-573. https://doi.org/10.1016/j.toxrep.2017.10.004
Hacine-Gherbi, Hêla, et al. "Use of Toll-like receptor assays for the detection of bacterial contaminations in icodextrin batches released for peritoneal dialysis." Toxicology reports vol. 4 (2017): 566-573. doi: https://doi.org/10.1016/j.toxrep.2017.10.004
Hacine-Gherbi H, Denys A, Carpentier M, Heysen A, Duflot P, Lanos P, Allain F. Use of Toll-like receptor assays for the detection of bacterial contaminations in icodextrin batches released for peritoneal dialysis. Toxicol Rep. 2017 Oct 23;4:566-573. doi: 10.1016/j.toxrep.2017.10.004. eCollection 2017. PMID: 29152461; PMCID: PMC5671617.
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NOD2 and inflammation: current insights.

Journal of inflammation research

Negroni A, Pierdomenico M, Cucchiara S, Stronati L.
PMID: 29483781
J Inflamm Res. 2018 Feb 12;11:49-60. doi: 10.2147/JIR.S137606. eCollection 2018.

The nucleotide-binding oligomerization domain (NOD) protein, NOD2, belonging to the intracellular NOD-like receptor family, detects conserved motifs in bacterial peptidoglycan and promotes their clearance through activation of a proinflammatory transcriptional program and other innate immune pathways, including autophagy and...

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Negroni A, Pierdomenico M, Cucchiara S, et al. NOD2 and inflammation: current insights. J Inflamm Res. 2018;11:49-60doi: 10.2147/JIR.S137606.
Negroni, A., Pierdomenico, M., Cucchiara, S., & Stronati, L. (2018). NOD2 and inflammation: current insights. Journal of inflammation research, 1149-60. https://doi.org/10.2147/JIR.S137606
Negroni, Anna, et al. "NOD2 and inflammation: current insights." Journal of inflammation research vol. 11 (2018): 49-60. doi: https://doi.org/10.2147/JIR.S137606
Negroni A, Pierdomenico M, Cucchiara S, Stronati L. NOD2 and inflammation: current insights. J Inflamm Res. 2018 Feb 12;11:49-60. doi: 10.2147/JIR.S137606. eCollection 2018. PMID: 29483781; PMCID: PMC5813767.
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