In Silico Analysis of Putative Paralytic Shellfish Poisoning Toxins Export Proteins in Cyanobacteria

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dc.contributor.authorSoto-Liebe, K.
dc.contributor.authorLópez-Cortés, X.
dc.contributor.authorFuentes-Valdes, J.
dc.contributor.authorStucken, K.
dc.contributor.authorGonzalez-Nilo, F.
dc.contributor.authorVásquez, M.
dc.date.accessioned2023-05-15T17:51:21Z
dc.date.available2023-05-15T17:51:21Z
dc.date.issued2013
dc.descriptionIndexación: Scopus.es
dc.description.abstractParalytic shellfish poisoning toxins (PSTs) are a family of more than 30 natural alkaloids synthesized by dinoflagellates and cyanobacteria whose toxicity in animals is mediated by voltage-gated Na+ channel blocking. The export of PST analogues may be through SxtF and SxtM, two putative MATE (multidrug and toxic compound extrusion) family transporters encoded in PSTs biosynthetic gene cluster (sxt). sxtM is present in every sxt cluster analyzed; however, sxtF is only present in the Cylindrospermopsis-Raphidiopsis clade. These transporters are energetically coupled with an electrochemical gradient of proton (H+) or sodium (Na+) ions across membranes. Because the functional role of PSTs remains unknown and methods for genetic manipulation in PST-producing organisms have not yet been developed, protein structure analyses will allow us to understand their function. By analyzing the sxt cluster of eight PST-producing cyanobacteria, we found no correlation between the presence of sxtF or sxtM and a specific PSTs profile. Phylogenetic analyses of SxtF/M showed a high conservation of SxtF in the Cylindrospermopsis-Raphidiopsis clade, suggesting conserved substrate affinity. Two domains involved in Na+ and drug recognition from NorM proteins (MATE family) of Vibrio parahaemolyticus and V. cholerae are present in SxtF/M. The Na+ recognition domain was conserved in both SxtF/M, indicating that Na+ can maintain the role as a cation anti-transporter. Consensus motifs for toxin binding differed between SxtF and SxtM implying differential substrate binding. Through protein modeling and docking analysis, we found that there is no marked affinity between the recognition domain and a specific PST analogue. This agrees with our previous results of PST export in R. brookii D9, where we observed that the response to Na+ incubation was similar to different analogues. These results reassert the hypothesis regarding the involvement of Na+ in toxin export, as well as the motifs L398XGLQD403 (SxtM) and L390VGLRD395 (SxtF) in toxin recognition.es
dc.description.urihttps://journals.plos.org/plosone/article?id=10.1371/journal.pone.0055664
dc.identifier.citationPLoS ONE, Volume 8, Issue 215, February 2013, Article number e55664es
dc.identifier.doi10.1371/journal.pone.0055664
dc.identifier.issn1932-6203
dc.identifier.urihttps://repositorio.unab.cl/xmlui/handle/ria/49636
dc.language.isoenes
dc.publisherPublic Library of Sciencees
dc.rights.licenseAttribution 2.0 Generic (CC BY 2.0)
dc.rights.urihttps://plos.org/open-science/open-access/
dc.subjectParalytic Shellfish Toxinses
dc.subjectSaxitoxinses
dc.subjectDinoflagellatees
dc.subjectBacterial Proteinses
dc.subjectBiological Transpores
dc.subjectComputer Simulationes
dc.subjectCylindrospermopsises
dc.subjectMarine Toxinses
dc.titleIn Silico Analysis of Putative Paralytic Shellfish Poisoning Toxins Export Proteins in Cyanobacteriaes
dc.typeArtículoes
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