Homogentisic acid is the primary precursor of melanin synthesis in Vibrio cholerae, a Hyphomonas strain, and Shewanella colwelliana

Kotob, Shaban; Coon, Steven L.; Quintero, Ernesto J.; Weiner, Ronald M.

doi:10.1128/aem.61.4.1620-1622.1995

Cited by 111 publications

(50 citation statements)

References 36 publications

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“…Pyomelanin is also produced by Vibrio cholerae (Ruzafa et al, 1995). Melanin production in V. cholerae is induced in response to stress, particularly hyperosmotic shock and elevated temperatures (Ivins and Holmes, 1981;Coyne and al-Harthi, 1992;Kotob et al, 1995). Pigment formation is initiated in late-to post-exponential growth of V. cholerae (Coyne and al-Harthi, 1992;Kotob et al, 1995).…”

Section: Melanin Synthesis In Bacteriamentioning

confidence: 99%

“…Shewanella colwelliana catalyses pyomelanin utilizing homogentisic acid (Fuqua et al, 1991;Fuqua and Weiner, 1993;Coon et al, 1994;Ruzafa et al, 1994;Kotob et al, 1995;Bridelli, 1998). Pigment production is inhibited by sulcotrione, a specific inhibitor of p-dihydroxyphenylpyruvate dehydrogenase (Turick et al, 2002).…”

Section: Melanin Synthesis In Bacteriamentioning

confidence: 99%

“…Melanin has also been implicated in the thermostability of other melanotic fungi (Zhdanova et al, 1980), including M. fructicola (Rehnstrom and Free, 1997) and may also protect against desiccation (Zhdanova and Pokhodenko, 1973;Kuo and Hoch, 1995;Howard and Valent, 1996;Rehnstrom and Free, 1997). Vibrio cholerae produces melanin in response to hyperosmotic shock and temperature increase (Ivins and Holmes, 1981;Coyne and al-Harthi, 1992;Kotob et al, 1995). The capacity of V. cholerae to synthesize melanin may increase survival of the microbe in estuaries during summer (Coyne and al-Harthi, 1992).…”

Section: Role Of Melanin In Environmental Protectionmentioning

confidence: 99%

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The contribution of melanin to microbial pathogenesis

Nosanchuk

Casadevall

2003

Cellular Microbiology

554

454

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SummaryMelanins are enigmatic pigments that are produced by a wide variety of microorganisms including several species of pathogenic bacteria, fungi and helminthes. The study of melanin is difficult because these pigments defy complete biochemical and structural analysis. Nevertheless, the availability of new reagents in the form of monoclonal antibodies and melaninbinding peptides, combined with the application of various physical techniques, has provided insights into the process of melanization. Melanization is important in microbial pathogenesis because it has been associated with virulence in many microorganisms. Melanin appears to contribute to virulence by reducing the susceptibility of melanized microbes to host defence mechanisms. However, the interaction of melanized microbes and the host is complex and includes immune responses to melanin-related antigens. Production of melanin has also been linked to protection against environmental insults. Interference with melanization is a potential strategy for antimicrobial drug and pesticide development. The process of melanization poses fascinating problems in cell biology and provides a type of pathogenic strategy that is common to highly diverse pathogens.

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Section: Melanin Synthesis In Bacteriamentioning

confidence: 99%

Section: Melanin Synthesis In Bacteriamentioning

confidence: 99%

Section: Role Of Melanin In Environmental Protectionmentioning

confidence: 99%

See 1 more Smart Citation

The contribution of melanin to microbial pathogenesis

Nosanchuk

Casadevall

2003

Cellular Microbiology

554

454

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“…There are several different types of melanin pigments produced by microorganisms (Prota, 1992). One particular type of melanin, pyomelanin, originates from the conversion of tyrosine and/or phenylalanine as part of the fumarate pathway (Lehninger, 1975), and is found in numerous bacterial genera (Yabuuchi & Omyama, 1972;Kotob et al, 1995;Ruzafa et al, 1995;David et al, 1996;Sanchez-Amat et al, 1998), including Shewanella (Fuqua & Weiner, 1993;Coon et al, 1994;Ruzafa et al, 1994;Turick et al, 2002Turick et al, , 2008a, Legionella (Chatfield & Cianciotto, 2007) and Burkholderia (Zughaier et al, 1999). Complete breakdown of these amino acids to acetoacetate and fumarate requires the activities of 4-hydroxyphenylpyruvate dioxygenase (4-HPPD) and homogentisate oxidase (Fuqua & Weiner, 1993;David et al, 1996).…”

Section: Introductionmentioning

confidence: 99%

The role of 4-hydroxyphenylpyruvate dioxygenase in enhancement of solid-phase electron transfer by Shewanella oneidensis MR-1

Turick

Beliaev

Zakrajsek

et al. 2009

FEMS Microbiology Ecology

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Summary 1While mechanistic details of dissimilatory metal reduction are far from being understood, it 2 is postulated that the electron transfer to solid metal oxides is mediated by outer membrane-3 associated c-type cytochromes and redox active electron shuttling compounds. This study 4 focuses on the production of homogensitate in Shewanella oneidensis MR-1, an intermediate 5 of tyrosine degradation pathway, which is a precursor of a redox cycling metabolite, 6 pyomelanin. In this study, we determined that two enzymes involved in this pathway, 4-7 hydroxyphenylpyruvate dioxygenase (4HPPD) and homogentisate 1,2-dioxygenase are 8 responsible for homogentisate production and oxidation, respectively. Inhibition of 4-HPPD 9 activity with the specific inhibitor sulcotrione ([2-(2-chloro-4-methane sulfonylbenzoyl)-10

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“…HPD proteins or cDNAs encoding HPD or proteins exhibiting significant similarity with HPD and endowed with dioxygenase activity have been isolated from a variety of species including bacteria (Denoya et al, 1994;Fuqua et al, 1991;Kotob et al, 1995;Rü etschi et al, 1992;Ruzafa et al, 1995), protozoan (Hummel et al, 1992), fungi (Wyckoff et al, 1995), plants (Garcia et al, 1997), and mammals (Endo et al, 1992). In mammals high levels of HPD activity have been detected in liver and kidney, whereas no HPD activity could be detected in heart, muscle or brain (Fellman et al, 1972).…”

Section: Introductionmentioning

confidence: 99%

Tissue distribution, intracellular localization and proteolytic processing of rat 4‐hydroxyphenylpyruvate dioxygenase

Neve

Aarenstrup

Tornehave

et al. 2003

Cell Biology International

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4-hydroxyphenylpyruvate dioxygenase (HPD) is an important enzyme involved in tyrosine catabolism. HPD was shown to be identical to a protein named the F-antigen, exploited by immunologists because of its unique immunological properties. Congenital HPD deficiency is a rare, relatively benign condition known as hereditary type III tyrosinemia. Decreased expression of HPD is often observed in association with the severe type I tyrosinemia, and interestingly, inhibition of HPD activity seems to ameliorate the clinical symptoms of type I tyrosinemia. In this study we present a comprehensive analysis of tissue specific expression and intracellular localization of HPD in the rat. By combined use of in situ hybridization and immunohistochemistry we confirm previously known sites of expression in liver and kidney. In addition, we show that HPD is abundantly expressed in neurons in the cortex, cerebellum and hippocampus. By using immunoelectron microscopy and confocal laser scanning microscopy, we provide evidence that HPD contrary to earlier assumptions specifically localizes to membranes of the endoplasmic reticulum and the Golgi apparatus. Detailed mass spectrometric analyses of HPD purified from rat liver revealed N-terminal and C-terminal processing of HPD, and expression of recombinant HPD suggested that C-terminal processing enhances the enzymatic activity.

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Homogentisic acid is the primary precursor of melanin synthesis in Vibrio cholerae, a Hyphomonas strain, and Shewanella colwelliana

Cited by 111 publications

References 36 publications

The contribution of melanin to microbial pathogenesis

The contribution of melanin to microbial pathogenesis

The role of 4-hydroxyphenylpyruvate dioxygenase in enhancement of solid-phase electron transfer by Shewanella oneidensis MR-1

Tissue distribution, intracellular localization and proteolytic processing of rat 4‐hydroxyphenylpyruvate dioxygenase

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