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A putative gene cluster from a Lyngbya wollei bloom that encodes paralytic shellfish toxin biosynthesis.

Mihali TK, Carmichael WW, Neilan BA - PLoS ONE (2011)

Bottom Line: Here we report the isolation, sequencing, annotation, and predicted pathway of the saxitoxin biosynthetic gene cluster in the cyanobacterium Lyngbya wollei.The gene cluster spans 36 kb and encodes enzymes for the biosynthesis and export of the toxins.These findings will enable the creation of toxin probes, for water monitoring purposes, as well as proof-of-concept for the combinatorial biosynthesis of these natural occurring alkaloids for the production of novel, biologically active compounds.

View Article: PubMed Central - PubMed

Affiliation: School of Biotechnology and Biomolecular Sciences, The University of New South Wales, Sydney, Australia.

ABSTRACT
Saxitoxin and its analogs cause the paralytic shellfish-poisoning syndrome, adversely affecting human health and coastal shellfish industries worldwide. Here we report the isolation, sequencing, annotation, and predicted pathway of the saxitoxin biosynthetic gene cluster in the cyanobacterium Lyngbya wollei. The gene cluster spans 36 kb and encodes enzymes for the biosynthesis and export of the toxins. The Lyngbya wollei saxitoxin gene cluster differs from previously identified saxitoxin clusters as it contains genes that are unique to this cluster, whereby the carbamoyltransferase is truncated and replaced by an acyltransferase, explaining the unique toxin profile presented by Lyngbya wollei. These findings will enable the creation of toxin probes, for water monitoring purposes, as well as proof-of-concept for the combinatorial biosynthesis of these natural occurring alkaloids for the production of novel, biologically active compounds.

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Structure of the saxitoxin analogs identified in Lyngbya wollei (adapted from [7]).
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pone-0014657-g001: Structure of the saxitoxin analogs identified in Lyngbya wollei (adapted from [7]).

Mentions: Lyngbya wollei a cyanobacterium belonging to the cyanobacterial order Oscillatoriales, has been reported from south-eastern United States lakes and water reservoirs for the past 100 years and has become increasingly common in the last three decades [25]. L. wollei has been shown to produce various PSTs, including decarbamoyl saxitoxins (dcSTX) and decarbamoyl gonyautoxins (dcGTX2, dcGTX3), as well as six novel analogs denoted 1-6 (Figure 1), which are characterized by the presence of acetate at C-13 and a carbinol at C-12 [7]. The toxin profile of L. wollei does not resemble the profile of any other characterized PST-producing cyanobacteria, such as Anabaena circinalis, Aphanizomenon sp. and Cylindrospermopsin raciborskii. The major PSTs found in A. circinalis are STX, the GTXs, and C1 and C2 [15], [26], while the major PST toxins found in Aph. flos-aquae (Aph. sp. NH-5) are neoSTX and STX [14].


A putative gene cluster from a Lyngbya wollei bloom that encodes paralytic shellfish toxin biosynthesis.

Mihali TK, Carmichael WW, Neilan BA - PLoS ONE (2011)

Structure of the saxitoxin analogs identified in Lyngbya wollei (adapted from [7]).
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC3037375&req=5

pone-0014657-g001: Structure of the saxitoxin analogs identified in Lyngbya wollei (adapted from [7]).
Mentions: Lyngbya wollei a cyanobacterium belonging to the cyanobacterial order Oscillatoriales, has been reported from south-eastern United States lakes and water reservoirs for the past 100 years and has become increasingly common in the last three decades [25]. L. wollei has been shown to produce various PSTs, including decarbamoyl saxitoxins (dcSTX) and decarbamoyl gonyautoxins (dcGTX2, dcGTX3), as well as six novel analogs denoted 1-6 (Figure 1), which are characterized by the presence of acetate at C-13 and a carbinol at C-12 [7]. The toxin profile of L. wollei does not resemble the profile of any other characterized PST-producing cyanobacteria, such as Anabaena circinalis, Aphanizomenon sp. and Cylindrospermopsin raciborskii. The major PSTs found in A. circinalis are STX, the GTXs, and C1 and C2 [15], [26], while the major PST toxins found in Aph. flos-aquae (Aph. sp. NH-5) are neoSTX and STX [14].

Bottom Line: Here we report the isolation, sequencing, annotation, and predicted pathway of the saxitoxin biosynthetic gene cluster in the cyanobacterium Lyngbya wollei.The gene cluster spans 36 kb and encodes enzymes for the biosynthesis and export of the toxins.These findings will enable the creation of toxin probes, for water monitoring purposes, as well as proof-of-concept for the combinatorial biosynthesis of these natural occurring alkaloids for the production of novel, biologically active compounds.

View Article: PubMed Central - PubMed

Affiliation: School of Biotechnology and Biomolecular Sciences, The University of New South Wales, Sydney, Australia.

ABSTRACT
Saxitoxin and its analogs cause the paralytic shellfish-poisoning syndrome, adversely affecting human health and coastal shellfish industries worldwide. Here we report the isolation, sequencing, annotation, and predicted pathway of the saxitoxin biosynthetic gene cluster in the cyanobacterium Lyngbya wollei. The gene cluster spans 36 kb and encodes enzymes for the biosynthesis and export of the toxins. The Lyngbya wollei saxitoxin gene cluster differs from previously identified saxitoxin clusters as it contains genes that are unique to this cluster, whereby the carbamoyltransferase is truncated and replaced by an acyltransferase, explaining the unique toxin profile presented by Lyngbya wollei. These findings will enable the creation of toxin probes, for water monitoring purposes, as well as proof-of-concept for the combinatorial biosynthesis of these natural occurring alkaloids for the production of novel, biologically active compounds.

Show MeSH
Related in: MedlinePlus