pyocyanin

Pyocyanine
	IUPAC name 5-Methylphenazin-1-one
	Other names Pyocyanin; Pyrocyanine; 5-Methyl-1(5H)-phenazinone; Sanasin; Sanazin
Identifiers
CAS number	85-66-5
PubChem	6817
Jmol-3D images	Image 1
	SMILES CN1C2=CC=CC=C2N=C3C1=CC=CC3=O ;
Properties
Molecular formula	C13H10N2O
Molar mass	210.23 g mol−1
Appearance	Solid
	(verify) (what is: /?); Except where noted otherwise, data are given for materials in their standard state (at 25 °C, 100 kPa)
	Infobox references

ピオシアニン

関: pyocyanine

WordNet

a toxic blue crystalline antibiotic found in green pus

Wikipedia preview

出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2013/06/26 01:17:30」(JST)

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Pyocyanin (PCN^-) is one of the many toxins produced and secreted by the Gram negative bacterium Pseudomonas aeruginosa. Pyocyanin is a blue, secondary metabolite with the ability to oxidise and reduce other molecules^[2] and therefore can kill microbes competing against P. aeruginosa as well as mammalian cells of the lungs which P. aeruginosa has infected during cystic fibrosis. Since pyocyanin is a zwitterion at blood pH, it is easily able to cross the cell membrane. There are three different states in which pyocyanin can exist; oxidized, monovalently reduced or divalently reduced. Mitochondria play a huge role in the cycling of pyocyanin between its redox states. Due to its redox-active properties, pyocyanin generates reactive oxygen species.

Synthesis[edit]

In order for pyocyanin to be synthesised by P. aeruginosa, two specific genes must be functional. MvfR is a gene which produces a transcription factor which activates phnAB genes. These genes produce the molecule quinolone which then regulates operons 1 and 2 of phzRABCDEFG which are key to the synthesis of phenazine.^[3] The synthesis of pyocyanin is primarily controlled by the quorum sensing process. P.aeruginosa strains which are unable to synthesise PCN can still benefit from its effects if the strain has co- infected the lung with wild type strains which can produce pyocyanin.^[4] Biosynthesis can be impaired by disrupting the aro pathway which is responsible for the synthesis of chorismic acid from shikimate.^[5] Chorismic acid is the precursor of pyocyanin.

Shikimate → Chorismic acid → phenazine-1-carboxylic acid → 5-methylphenazine-1-carboxylic acid betaine → Pyocyanin^[6]

The complete virulence of P.aeruginosa can only be experienced when pyocyanin is produced.^[7]

Redox warfare[edit]

Pyocyanin inactivates catalase by reducing its gene’s transcription as well as directly targeting the enzyme itself. Glutathione, an important antioxidant is modulated by pyocyanin.^[8] In particular the pool of the reduced form is depleted while the oxidised form is promoted by hydrogen peroxide which is not dismutated by catalase. In the cystic fibrosis lung, intracellular pyocyanin converts molecular oxygen to the superoxide free radical by reducing NADPH to NADP⁺. This has a doubly negative effect on the lungs. Firstly, the NADPH used by pyocyanin depletes the available substrate for the reaction catalysed by the NADPH oxidase enzyme. Secondly, the superoxide radical generated can inhibit cytokines such as IL-4, IL-13 and IFN-γ which usually upregulate NADPH oxidase. When the lung is confronted with pyocyanin, an increased concentration of catalase and superoxide dismutase is seen in order to deal with the barrage of radicals being produced.^[9]

Targets[edit]

Pyocyanin is able to target a wide range of cellular components and pathways. Pathways which are affected by pyocyanin include the electron transport chain, vesicular transport, and cell growth. An enhanced susceptibility to pyocyanin is seen in cells which have mutation in certain proteins or complexes. Mutations in genes affecting V-ATPase synthesis and assembly,^[10] vesicle transport machinery, protein sorting machinery all confer an increased sensitivity to pyocyanin which further enhances the effects on cystic fibrosis on the patient. Vacuolar- ATPase in yeast cells is a particularly potent target as it is the main non-mitochondrial producer of ATP but also has numerous other functions such as calcium homeostatic control, the facilitation of receptor-mediated endocytosis and the degradation of proteins. Therefore the inactivation of vacuolar-ATPase by hydrogen peroxide produced by pyocyanin has huge consequences for the lung. Additional to these effects, another target of pyocyanin is caspase 3-like proteases which can then go on to initiate apoptosis and necrosis. Mitochondrial electron carrier’s ubiquinone and nicotinic acid are also susceptible to pyocyanin.^[11] The cell cycle can be disturbed by the action of pyocyanin as well as hinder the proliferation of lymphocytes.^[12] This is done by the generation of reactive oxygen intermediates such as hydrogen peroxide and superoxide which cause oxidative stress by damaging DNA directly or alternatively targeting other constituents of the cell cycle such as DNA recombination and repair machinery. Pyocyanin contributes to the disproportion of protease and antiprotease activity by disabling α₁- protease inhibitor.

Cystic fibrosis[edit]

Many studies have concluded that pyocyanin has a derogatory effect in cystic fibrosis which enables P. aeruginosa to persist in the cystic fibrosis lung; it is often detected in the sputum from cystic fibrosis patients. Pyocyanin in vitro has the ability to interfere with functions such as ciliary beating and therefore cause epithelial dysfunction as the ciliary are needed to sweep mucus up the throat.^[13] Additionally, neutrophil apoptosis,^[14] immunoglobulin release from B-lymphocytes and interleukin release e.g. IL-8^[15] and CCL5 are all impaired by pyocyanin causing the immune system of the lung to be weakened. In vivo studies have shown that the growth of fungus is inhibited in the presence of pyocyanin.^[16] The fungicidal mechanism is the activation of NAD(P)H to induce a redox active cascade to produce reactive oxygen intermediates. This allows P. aeruginosa to have a competitive advantage as it may dominate over other microorganisms in the cystic fibrosis lung. The intracellular concentration of ATP is also diminished by pyocyanin causing further damage to CFTR which are already impaired in cystic fibrosis. CFTR channels rely on ATP for two main purposes. Firstly, the binding and hydrolysis of ATP has to occur at two nucleotide binding domains for the channel to move between its open and closed conformation.^[17] Secondly, phosphorylation of CFTR by Protein kinase A II should occur in order for the channel to be operational. PKA II is activated by cAMP which is produced from ATP. Both these processes are impaired when ATP is depleted by pyocyanin.

Defence against pyocyanin[edit]

C. elegans possess two specific ABC transporter called pgp-1 and pgp-2 which are effectively able to extrude intracellular pyocyanin in an energy dependent manner.^[18]

References[edit]

^ Pyocyanin at Sigma-Aldrich
^ Hassan H & Fridovich I (1980). "Mechanism of the antibiotic action pyocyanine.". Journal of Bacteriology 141 (1): 156–163. PMC 293551. PMID 6243619.
^ Mavrodi D, Bonsall, R, Delaney, S, Soule, M, Phillips G & Thomashow, L. S. (2001). "Function analysis of genes for biosynthesis of pyocyanin and phenazine -1-carboxamide from Pseudomonas aeruginosa PAO1". Journal of Bacteriology 183 (21): 6454–6465. doi:10.1128/JB.183.21.6454-6465.2001.
^ Lau E, Ran H, Kong F, Hassett D, Mavrodi D. (2004). "Pseudomonas aeruginosa Pyocyanin Is Critical for Lung Infection in Mice". Infection and Immunity 72 (7): 4275–4278. doi:10.1128/IAI.72.7.4275-4278.2004.
^ Denning G, Iyer S,Reszka K, O'Malley Y,Rasmussen G & Britigan B (2003). "Phenazine-1-carboxylic acid, a secondary metabolite of Pseudomonas aeruginosa, alters expression of immunomodulatory proteins by human airway epithelial cells". American Journal of Physiology 285: 584–L592. doi:10.1152/ajplung.00086.2003.
^ Lau G, Hassett D, Ran H & Kong F (2004). "The role of pyocyanin in Pseudomonas aeruginosa infection". Trends in Molecular Medicine 10 (12): 1–666. doi:10.1016/j.molmed.2004.10.002. PMID 15567330.
^ Britigin B, Railsback A, Cox D. (1999). "The Pseudomonas aeruginosa secretory product pyocyanin inactivates α1 protease inhibitor: implications for the pathogenesis of cystic fibrosis lung disease". Infection and Immunity 67: 1207–1212.
^ Muller M (2002). "Pyocyanin inducesoxidative stress in human endothelialcells and modulates the glutathione redox cycle". Free Radical Biology and Medicine 33 (11): 1527–1533. doi:10.1016/S0891-5849(02)01087-0.
^ Huimin R, Hassett D & Lau G (2003). "Human targets of Pseudomonas aeruginosa pyocyanin". PNAS 100 (24): 14315–14320. doi:10.1073/pnas.2332354100. PMC 283589. PMID 14605211.
^ Ho M, Hirata R, Umemota N, Ohya Y, Takatsuki A, Stevens T & Anraku Y. (1993). "VMA13 encodes a 54-kDa vacuolar H(+)ATPase subunit required for activity but not assembly of the enzyme complex in Saccharomyces cerevisiae". The Journal of Biological Chemistry 268 (24): 18286–18292. PMID 8349704.
^ Hassett D, Woodruff W, Wozniak D, Vasil M, Cohen S & Ohman D (1993). "Cloning and characterization of the Pseudomonas aeruginosa soda and sodB genes encoding manganese- and iron cofactored SOD: demonstration of increased Mn SOD dismutase activity in alginate-producing bacteria". Journal of Bacteriology 1 (23): 1–666. PMC 206923. PMID 8244935.
^ Sorensen R &Klinger J (1987). "Biological effects of Pseudomonas aeruginosa phenazine pigments". Journal of antibiotic Chemotherapy 39: 113–124. PMID 3118778.
^ Kanthakumar K, Taylor G, Tsang K, Cundell D, Rutman A, Smith S, Jeffery P, Cole P & Wilson R (1993). "Mechanism of action of Pseudomona aeruginosa pyocyanin on human ciliary beat in vitro". Infection and Immunity 61: 2848–2853.
^ Usher L, Lawson R, Gaery I, Taylor C, Bingle C, Taylor G, Whyte M. (2002). "Induction of neutrophil apoptosis by the Pseudomonas aeruginosa exotoxin pyocyanin: a potential mechanism of persistant infection". The Journal of Immunology 4: 1861–1868.
^ Denning G, Wollenweber L, Railsback M, Cox C, Stoll L & Britigan B (1998). "Pseudomonas pyocyanin increases interleukin-8 expression by human airway epithelial cells". Infection and Immunity 66 (12): 5777–5784. PMC 108730. PMID 9826354.
^ Kerr J, Taylor G, Rutman A, Hoiby N, Cole P, Wilson R (1998). "Pseudomonas aeruginosa pyocyanin and 1-hydroxyphenazine inhbit fungal growth". Journal of Clinical Pathology 52 (5): 385–387. doi:10.1136/jcp.52.5.385.
^ Ostedgaard S, Baldursson O, Vermeer D, Welsh M, Robertson A (2001). "Regulation of the cystic fibrosis transmembrane conductance regulator ClK channel by its R domain". Journal of Biological Chemistry 276 (11): 7689–7692. doi:10.1074/jbc.R100001200.
^ Mahajan-Miklos S, Tan M, Rahme L, Ausubel F (1999). "Molecular mechanisms of bacterial virulence elucidated using a Pseudomonas aeruginosa-Caenorhabditis elegans pathogenesis model". The Cell 96 (1): 47–56. doi:10.1016/S0092-8674(00)80958-7. PMID 9989496.

External links[edit]

Pyocyanin profile

UpToDate Contents

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English Journal

ERK1/2 activation modulates pyocyanin-induced toxicity in A549 respiratory epithelial cells.

Forbes A1, Davey AK1, Perkins AV2, Grant GD1, McFarland AJ1, McDermott CM3, Anoopkumar-Dukie S4.Author information 1Griffith Health Institute, Griffith University, Queensland, Australia; School of Pharmacy, Griffith University, Queensland, Australia.2Griffith Health Institute, Griffith University, Queensland, Australia; School of Medical Science, Griffith University, Queensland, Australia.3Faculty of Health Sciences and Medicine, Bond University, Robina, Queensland, Australia.4Griffith Health Institute, Griffith University, Queensland, Australia; School of Pharmacy, Griffith University, Queensland, Australia. Electronic address: s.dukie@griffith.edu.au.AbstractPyocyanin (PCN), a virulence factor produced by Pseudomonas aeruginosa, has many damaging effects on mammalian cells. Several lines of evidence suggest that this damage is primarily mediated by its ability to generate oxidative stress. However mechanisms underlying PCN-induced oxidative injury remain unclear. Although oxidative stress and subsequent MAPK signaling has been shown to modulate cell death in other models, its role in PCN-induced cytotoxicity remains unknown. Therefore the aim of this study was to investigate the role of redox-sensitive MAPK in PCN-induced toxicity in A549 cells. Here we show that PCN (50μM) rapidly increased ERK1/2 phosphorylation after 5min. Pre-treatment of A549 cells with the MEK1/2 inhibitor U0126 (10μM) decreased PCN-induced ERK1/2 phosphorylation and protected cells against apoptosis and cell injury suggesting a role for ERK signalling. In contrast, JNK and p38 MAPK phosphorylation remained unchanged following exposure to PCN and pretreatment with either the JNK or p38 MAPK inhibitors (10μM SP600125 and 10μM SB203580, respectively) did not afford protection against PCN toxicity. This would suggest that PCN-induced cytotoxicity appears to occur independently of JNK and p38 MAPK signaling pathways. Finally, although we confirm that oxidative stress contributes to PCN-induced toxicity, our data suggest the contribution of oxidative stress is independent of ERK1/2 signaling. These findings may provide insight for novel targeted therapies to reduce PCN-mediated lung injury in patients with chronic P. aeruginosa respiratory infections.
Chemico-biological interactions.Chem Biol Interact.2014 Feb 5;208:58-63. doi: 10.1016/j.cbi.2013.11.016. Epub 2013 Dec 5.
Pyocyanin (PCN), a virulence factor produced by Pseudomonas aeruginosa, has many damaging effects on mammalian cells. Several lines of evidence suggest that this damage is primarily mediated by its ability to generate oxidative stress. However mechanisms underlying PCN-induced oxidative injury remai
PMID 24316274

Phenazine antibiotic inspired discovery of potent bromophenazine antibacterial agents against Staphylococcus aureus and Staphylococcus epidermidis.

Borrero NV, Bai F, Perez C, Duong BQ, Rocca JR, Jin S, Huigens Iii RW.Author information University of Florida, Gainesville, Florida 32610, USA. rhuigens@cop.ufl.edu.AbstractNearly all clinically used antibiotics have been (1) discovered from microorganisms (2) using phenotype screens to identify inhibitors of bacterial growth. The effectiveness of these antibiotics is attributed to their endogenous roles as bacterial warfare agents against competing microorganisms. Unfortunately, every class of clinically used antibiotic has been met with drug resistant bacteria. In fact, the emergence of resistant bacterial infections coupled to the dismal pipeline of new antibacterial agents has resulted in a global health care crisis. There is an urgent need for innovative antibacterial strategies and treatment options to effectively combat drug resistant bacterial pathogens. Here, we describe the implementation of a Pseudomonas competition strategy, using redox-active phenazines, to identify novel antibacterial leads against Staphylococcus aureus and Staphylococcus epidermidis. In this report, we describe the chemical synthesis and evaluation of a diverse 27-membered phenazine library. Using this microbial warfare inspired approach, we have identified several bromophenazines with potent antibacterial activities against S. aureus and S. epidermidis. The most potent bromophenazine analogue from this focused library demonstrated a minimum inhibitory concentration (MIC) of 0.78-1.56 μM, or 0.31-0.62 μg mL(-1), against S. aureus and S. epidermidis and proved to be 32- to 64-fold more potent than the phenazine antibiotic pyocyanin in head-to-head MIC experiments. In addition to the discovery of potent antibacterial agents against S. aureus and S. epidermidis, we also report a detailed structure-activity relationship for this class of bromophenazine small molecules.
Organic & biomolecular chemistry.Org Biomol Chem.2014 Jan 14;12(6):881-6. doi: 10.1039/c3ob42416b.
Nearly all clinically used antibiotics have been (1) discovered from microorganisms (2) using phenotype screens to identify inhibitors of bacterial growth. The effectiveness of these antibiotics is attributed to their endogenous roles as bacterial warfare agents against competing microorganisms. Unf
PMID 24389824

Enhancement of bioelectricity generation by manipulation of the electron shuttles synthesis pathway in microbial fuel cells.

Yong XY1, Shi DY2, Chen YL2, Jiao F2, Lin X2, Zhou J3, Wang SY3, Yong YC4, Sun YM5, Ouyang PK3, Zheng T6.Author information 1College of Biotechnology and Pharmaceutical Engineering, Nanjing University of Technology, Nanjing 210095, China; Bioenergy Research Institute, Nanjing University of Technology, Nanjing 210095, China. Electronic address: yongxiaoyu@njut.edu.cn.2College of Biotechnology and Pharmaceutical Engineering, Nanjing University of Technology, Nanjing 210095, China.3College of Biotechnology and Pharmaceutical Engineering, Nanjing University of Technology, Nanjing 210095, China; Bioenergy Research Institute, Nanjing University of Technology, Nanjing 210095, China.4Biofuels Institute, School of the Environment, Jiangsu University, Zhenjiang 212013, China.5Guangzhou Institute of Energy Conversion, Key Laboratory of Renewable Energy, Chinese Academy of Sciences, Guangzhou 510640, China.6College of Biotechnology and Pharmaceutical Engineering, Nanjing University of Technology, Nanjing 210095, China; Bioenergy Research Institute, Nanjing University of Technology, Nanjing 210095, China. Electronic address: hellozheng@gmail.com.AbstractMicrobial fuel cells (MFCs) are promising for generating bioenergy and treating organic waste simultaneously. However, low extracellular electron transfer (EET) efficiency between electrogens and anodes remains one of the major bottlenecks in practical applications of MFCs. In this paper, pyocyanin (PYO) synthesis pathway was manipulated to improve the EET efficiency in Pseudomonas aeruginosa-inoculated MFCs. By overexpression of phzM (methyltransferase encoding gene), the maximum power density of P. aeruginosa-phzM-inoculated MFC was enhanced to 166.68μW/cm(2), which was four folds of the original strain. In addition, the phzM overexpression strain exhibited an increase of 1.6 folds in PYO production and about a onefold decrease in the total internal resistance than the original strain, which should underlie the enhancement of the EET efficiency and the electricity power output (EPT). On the basis of these results, the manipulation of electron shuttles synthesis pathways could be an efficient approach to improve the EPT of MFCs.
Bioresource technology.Bioresour Technol.2014 Jan;152:220-4. doi: 10.1016/j.biortech.2013.10.086. Epub 2013 Nov 5.
Microbial fuel cells (MFCs) are promising for generating bioenergy and treating organic waste simultaneously. However, low extracellular electron transfer (EET) efficiency between electrogens and anodes remains one of the major bottlenecks in practical applications of MFCs. In this paper, pyocyanin
PMID 24292201

Japanese Journal

Roles of Pseudomonas aeruginosa Autoinducers and their Degradation Products, Tetramic acids, in Bacterial Survival and Behavior in Ecological Niches

HOSONO HONDA NATSUE,KIMURA SOICHIRO,TATEDA KAZUHIRO,HORIKAWA MANABU,UEDA CHIHIRO,ISHII YOSHIKAZU,ISHIGURO MASAJI,MIYAIRI SHINICHI,YAMAGUCHI KEIZO
Microbes and environments 26(2), 160-164, 2011-06-01
… Exogenous tetramic acid did not induce significant changes in the formation of biofilm or production of exoproducts such as pyocyanin and elastase. …
NAID 10029122954

Improvement in pHERD vectors to express recombinant proteins tagged with hexahistidine at either the NH- or COOH- terminal in Pseudomonas aeruginosa

Iiyama Kazuhiro,Lee Jae Man,Kusakabe Takahiro [他]
Journal of insect biotechnology and sericology 80(2), 57-61, 2011-06
NAID 40019149658

Related Pictures

[1] Pyocyanin at Sigma-Aldrich

[2] Hassan H & Fridovich I (1980). "Mechanism of the antibiotic action pyocyanine.". Journal of Bacteriology 141 (1): 156–163. PMC 293551. PMID 6243619.

[3] Mavrodi D, Bonsall, R, Delaney, S, Soule, M, Phillips G & Thomashow, L. S. (2001). "Function analysis of genes for biosynthesis of pyocyanin and phenazine -1-carboxamide from Pseudomonas aeruginosa PAO1". Journal of Bacteriology 183 (21): 6454–6465. doi:10.1128/JB.183.21.6454-6465.2001.

[4] Lau E, Ran H, Kong F, Hassett D, Mavrodi D. (2004). "Pseudomonas aeruginosa Pyocyanin Is Critical for Lung Infection in Mice". Infection and Immunity 72 (7): 4275–4278. doi:10.1128/IAI.72.7.4275-4278.2004.

[5] Denning G, Iyer S,Reszka K, O'Malley Y,Rasmussen G & Britigan B (2003). "Phenazine-1-carboxylic acid, a secondary metabolite of Pseudomonas aeruginosa, alters expression of immunomodulatory proteins by human airway epithelial cells". American Journal of Physiology 285: 584–L592. doi:10.1152/ajplung.00086.2003.

[6] Lau G, Hassett D, Ran H & Kong F (2004). "The role of pyocyanin in Pseudomonas aeruginosa infection". Trends in Molecular Medicine 10 (12): 1–666. doi:10.1016/j.molmed.2004.10.002. PMID 15567330.

[7] Britigin B, Railsback A, Cox D. (1999). "The Pseudomonas aeruginosa secretory product pyocyanin inactivates α1 protease inhibitor: implications for the pathogenesis of cystic fibrosis lung disease". Infection and Immunity 67: 1207–1212.

[8] Muller M (2002). "Pyocyanin inducesoxidative stress in human endothelialcells and modulates the glutathione redox cycle". Free Radical Biology and Medicine 33 (11): 1527–1533. doi:10.1016/S0891-5849(02)01087-0.

[9] Huimin R, Hassett D & Lau G (2003). "Human targets of Pseudomonas aeruginosa pyocyanin". PNAS 100 (24): 14315–14320. doi:10.1073/pnas.2332354100. PMC 283589. PMID 14605211.

[10] Ho M, Hirata R, Umemota N, Ohya Y, Takatsuki A, Stevens T & Anraku Y. (1993). "VMA13 encodes a 54-kDa vacuolar H(+)ATPase subunit required for activity but not assembly of the enzyme complex in Saccharomyces cerevisiae". The Journal of Biological Chemistry 268 (24): 18286–18292. PMID 8349704.

[11] Hassett D, Woodruff W, Wozniak D, Vasil M, Cohen S & Ohman D (1993). "Cloning and characterization of the Pseudomonas aeruginosa soda and sodB genes encoding manganese- and iron cofactored SOD: demonstration of increased Mn SOD dismutase activity in alginate-producing bacteria". Journal of Bacteriology 1 (23): 1–666. PMC 206923. PMID 8244935.

[12] Sorensen R &Klinger J (1987). "Biological effects of Pseudomonas aeruginosa phenazine pigments". Journal of antibiotic Chemotherapy 39: 113–124. PMID 3118778.

[13] Kanthakumar K, Taylor G, Tsang K, Cundell D, Rutman A, Smith S, Jeffery P, Cole P & Wilson R (1993). "Mechanism of action of Pseudomona aeruginosa pyocyanin on human ciliary beat in vitro". Infection and Immunity 61: 2848–2853.

[14] Usher L, Lawson R, Gaery I, Taylor C, Bingle C, Taylor G, Whyte M. (2002). "Induction of neutrophil apoptosis by the Pseudomonas aeruginosa exotoxin pyocyanin: a potential mechanism of persistant infection". The Journal of Immunology 4: 1861–1868.

[15] Denning G, Wollenweber L, Railsback M, Cox C, Stoll L & Britigan B (1998). "Pseudomonas pyocyanin increases interleukin-8 expression by human airway epithelial cells". Infection and Immunity 66 (12): 5777–5784. PMC 108730. PMID 9826354.

[16] Kerr J, Taylor G, Rutman A, Hoiby N, Cole P, Wilson R (1998). "Pseudomonas aeruginosa pyocyanin and 1-hydroxyphenazine inhbit fungal growth". Journal of Clinical Pathology 52 (5): 385–387. doi:10.1136/jcp.52.5.385.

[17] Ostedgaard S, Baldursson O, Vermeer D, Welsh M, Robertson A (2001). "Regulation of the cystic fibrosis transmembrane conductance regulator ClK channel by its R domain". Journal of Biological Chemistry 276 (11): 7689–7692. doi:10.1074/jbc.R100001200.

[18] Mahajan-Miklos S, Tan M, Rahme L, Ausubel F (1999). "Molecular mechanisms of bacterial virulence elucidated using a Pseudomonas aeruginosa-Caenorhabditis elegans pathogenesis model". The Cell 96 (1): 47–56. doi:10.1016/S0092-8674(00)80958-7. PMID 9989496.

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