Multiple dual-mode centrifugal partition chromatography as an efficient method for the purification of a mycosporine from a crude methanolic extract of Lichina pygmaea

Roullier, Catherine; Chollet-Krugler, Marylène; Bernard, Aurélie; Boustié, Joël

doi:10.1016/j.jchromb.2009.05.040

Cited by 42 publications

(41 citation statements)

References 25 publications

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“…Four peaks at retention times (t R ) of 5.6 min, 6.4 min, 7.3 min, and 8.1 min were increased compared to those of the controls. Peaks I and II (t R ϭ 5.6 and 6.4 min, respectively) had UV absorbance maxima of 310 nm, similar to those of other MAA compounds, including mycosporine-glycine, mycosporine-serinol, mycosporine-glutaminol, mycosporine-glutaminol, and glutamicol-glucoside (26)(27)(28)(29)(30)(31). Peaks III and IV (t R ϭ 7.3 and 8.1 min, respectively) were not studied in detail because their expression rates were very low.…”

Section: Resultsmentioning

confidence: 68%

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Heterologous Production of Cyanobacterial Mycosporine-Like Amino Acids Mycosporine-Ornithine and Mycosporine-Lysine in Escherichia coli

Katoch

Mazmouz

Chau

et al. 2016

Appl Environ Microbiol

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Mycosporine-like amino acids (MAAs) are an important class of secondary metabolites known for their protection against UV radiation and other stress factors. Cyanobacteria produce a variety of MAAs, including shinorine, the active ingredient in many sunscreen creams. Bioinformatic analysis of the genome of the soil-dwelling cyanobacterium Cylindrospermum stagnale PCC 7417 revealed a new gene cluster with homology to MAA synthase from Nostoc punctiforme. This newly identified gene cluster is unusual because it has five biosynthesis genes (mylA to mylE), compared to the four found in other MAA gene clusters. Heterologous expression of mylA to mylE in Escherichia coli resulted in the production of mycosporine-lysine and the novel compound mycosporine-ornithine. To our knowledge, this is the first time these compounds have been heterologously produced in E. coli and structurally characterized via direct spectral guidance. This study offers insight into the diversity, biosynthesis, and structure of cyanobacterial MAAs and highlights their amenability to heterologous production methods. M ycosporine-like amino acids (MAAs) are commonly found in marine microbes exposed to high levels of UV radiation, including aquatic fungi, eukaryotic algae, and cyanobacteria (1-6). These small (Ͻ400 Da), colorless, water-soluble compounds are composed of a 4-deoxygadusol core conjugated with an amino acid or alcohol (7). Their absorption maxima typically range from 310 to 360 nm and their molar extinction coefficients (ε) range from 28,100 to 50,000 M Ϫ1 cm Ϫ1 (8, 9). Commonly termed "microbial sunscreens," MAAs can dissipate UV energy as heat without generating free oxygen radicals (7).While UV exposure is necessary to elicit the synthesis of MAAs (10), some studies suggest that other factors, including osmotic stress, may also be involved in MAA regulation (11). Indeed, MAAs are widely considered to be multifunctional compounds offering protection against oxidative, osmotic, and thermal stress as well as UV radiation (12-17). However, this may not be true for all MAAs (11). Due to their diverse biological properties, MAAs are promising candidates for pharmaceutical and cosmetic applications (3, 18). For example, shinorine, produced by the cyanobacterium Anabaena variabilis, has already been commercialized as an active ingredient in sunscreen creams (Helioguard 365 and Helionori) (14).The biosynthesis of shinorine ( Fig. 1) was recently elucidated via heterologous expression in Escherichia coli (19,20) and is a model pathway for MAA biosynthesis. In A. variabilis ATCC 29413, the shinorine biosynthesis gene cluster consists of four genes: ava_3855 to ava_3858. The first step in the biosynthesis of shinorine is the conversion of sedoheptulose-7-phosphate (SH-7P) to 2-demethyl-4-deoxygadusol (DDG) by a DDG synthase (Ava_3858). Following this, DDG is converted to the mycosporine core compound 4-deoxygadusol (4-DG) by an O-methyltransferase (O-MT) (Ava_3857). Glycylation of 4-DG is catalyzed by a C-N ligase (Ava_3856), resulting ...

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Section: Resultsmentioning

confidence: 68%

“…and marine sea anemones (33,34). Mycosporine-serinol was found in cyanolichens Lichina pygmaea and Lichina confinis and different species of Peltigera (26,27). However, whether the cyanobacterial symbionts or the fungal hosts are the true producers of mycosporineserinol is currently unknown.…”

Section: And 3172 [M ϩ H]mentioning

confidence: 99%

Heterologous Production of Cyanobacterial Mycosporine-Like Amino Acids Mycosporine-Ornithine and Mycosporine-Lysine in Escherichia coli

Katoch

Mazmouz

Chau

et al. 2016

Appl Environ Microbiol

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“…This finding is probably due to our experimental approach of identifying MAAs using ESI-MS and NMR rather than relying on the more typically used HPLC with UV detection, which can be relatively imprecise [16] [17]. Thus, we propose that there exists a much greater diversity of MAAs than is currently known.…”

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confidence: 90%

Isolation and Structural Elucidation of Novel Mycosporine‐Like Amino Acids as Alarm Cues in the Defensive Ink Secretion of the Sea Hare Aplysia californica

Kamio

Kicklighter

Nguyen

et al. 2011

Helvetica Chimica Acta

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Three new mycosporine-like amino acids (MAAs), aplysiapalythines A, B, and C (1, 2, and 3, resp.) were isolated from opaline, a glandular component of the defensive ink secretion of sea hares (Aplysia californica) collected from waters off southern California. Here, we report the structure of these MAAs determined by mass spectrometry and NMR data. These new MAAs are structurally related to two known MAAs that are also present in sea hare opaline, i.e., asterina 330 (4) and palythine (5), and for which we also provide detailed data here for comparison. The fact that three of the five MAAs that we identified from sea hare opaline are novel molecules is interesting given that this represents a relatively large addition to the current list of known MAAs. This is likely because most researchers have identified MAAs through HPLC with UV detection, which is imprecise given similarities in UV spectra for different MAAs. Our findings suggest that there is much greater diversity of MAAs than is currently known. Results published elsewhere show that 1, 2, and 4 are alarm cues for conspecific sea hares at natural concentrations, but 3 and 5 are not.Introduction. -Mycosporine-like amino acids (MAAs) are widely distributed in marine organisms including bacteria, plants, invertebrates, and vertebrates [1]. Animals are generally thought to be incapable of synthesizing MAAs, but rather they are thought to sequester MAAs from their diet or from symbionts; however, this view has been questioned [2]. MAAs, of which ca. 30 are known, are traditionally considered to be screens against solar radiation, but other functions have also been proposed, including anti-oxidants, osmotic regulation, providing a source of amino acids in embryonic development, and induction of spawning [3 -10].A new function for MAAs was recently identified from our work on chemical defenses of sea hares (Aplysia californica) collected from the waters of southern California [11]. We found that MAAs are present in high concentrations in opaline, which is one of the glandular products of the sea hares ink secretion. Of the five major MAAs in opaline of these sea hares, three are novel, and two of these novel MAAs, together with nucleic acids and nucleosides in the ink component of the sea hares ink secretion, function as intraspecific alarm cues [11]. In this article, we describe the isolation and the structure elucidation of these novel MAAs.

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“…Yet, the impact of air pollution is minimum in Himalaya region, and UV-exposure seems to be playing key role in sustainability of lichen species having UV-protecting compounds. Oxo MAAs are commonly found in some lichen species, i.e., Peltula (Roullier et al 2009(Roullier et al , 2011Torres et al 2004;Büdel et al 1997). Yet, the occurrence of imino MAAs requires further mechanistic explanation.…”

Section: Resultsmentioning

confidence: 99%

Characterization of the diversity of mycosporine-like amino acids in lichens from high altitude region of Himalaya

et al. 2015

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Lichens are tolerant to a number of environmental variables including high-intensity solar radiations, which is mainly due to the presence of chemical substances in the thallus. Especially, cyanobacterial lichens synthesize a unique class of chemical substances known as mycosporine-like amino acids (MAAs) the primary characteristic of which is strong ultraviolet (UV) absorption between 300 and 360 nm. In view of its UV-protecting potential, the applicability of mass spectral fragmentation using electrospray ionization tandem mass spectrometric analysis for the characterization of MAAs in lichen samples was explored. MAA compounds were characterized in four cyanobacteria-containing lichen species belonging to genus Peltigera, Stereocaulon and Lobaria. Among them, Peltigera and Lobaria are true cyanobacteria containing lichens (cyanolichens) while Stereocaulon is a tripartite lichen, as it contains both green algae (in the thallus) and cyanobacteria (in the cephalodia), collected from higher altitudes of Himalaya (Tungnath-Chopta in Garhwal Himalaya, 3432 m) from an exposed locality experiencing high light intensity. Mass spectral data of distinctive fragmentation pattern revealed that all the four species have good diversity of MAA compounds, especially Lobaria retigera was found to be enriched with highest diversity of oxo and imino MAAs. Overall, different numbers of oxo and imino MAA compounds were detected in the remaining lichen species. Good diversity of imino MAAs has ecological significance which is required to be investigated further. Moreover, the impressive diversity characterized in each lichen species suggests that lichens should be thoroughly studied for their MAAs contents.

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Multiple dual-mode centrifugal partition chromatography as an efficient method for the purification of a mycosporine from a crude methanolic extract of Lichina pygmaea

Cited by 42 publications

References 25 publications

Heterologous Production of Cyanobacterial Mycosporine-Like Amino Acids Mycosporine-Ornithine and Mycosporine-Lysine in Escherichia coli

Heterologous Production of Cyanobacterial Mycosporine-Like Amino Acids Mycosporine-Ornithine and Mycosporine-Lysine in Escherichia coli

Isolation and Structural Elucidation of Novel Mycosporine‐Like Amino Acids as Alarm Cues in the Defensive Ink Secretion of the Sea Hare Aplysia californica

Characterization of the diversity of mycosporine-like amino acids in lichens from high altitude region of Himalaya

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