<i>In Silico</i> Analysis of Putative Paralytic Shellfish Poisoning Toxins Export Proteins in Cyanobacteria

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dc.contributor.authorSoto-Liebe, Katia
dc.contributor.authorLopez-Cortes, Xaviera A.
dc.contributor.authorJose Fuentes-Valdes, Juan
dc.contributor.authorStucken, Karina
dc.contributor.authorGonzalez-Nilo, Fernando
dc.contributor.authorVasquez, Monica
dc.date.accessioned2025-01-24T00:04:36Z
dc.date.available2025-01-24T00:04:36Z
dc.date.issued2013
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 L(398)XGLQD(403) (SxtM) and L(390)VGLRD(395) (SxtF) in toxin recognition.
dc.description.funderFondo Nacional de Desarrollo Cientifico y Tecnologico (FONDECYT)
dc.fuente.origenWOS
dc.identifier.doi10.1371/journal.pone.0055664
dc.identifier.issn1932-6203
dc.identifier.urihttps://doi.org/10.1371/journal.pone.0055664
dc.identifier.urihttps://repositorio.uc.cl/handle/11534/101805
dc.identifier.wosidWOS:000315603700016
dc.issue.numero2
dc.language.isoen
dc.revistaPlos one
dc.rightsacceso restringido
dc.subject.ods13 Climate Action
dc.subject.ods06 Clean Water and Sanitation
dc.subject.ods15 Life on Land
dc.subject.ods14 Life Below Water
dc.subject.odspa13 Acción por el clima
dc.subject.odspa06 Agua limpia y saneamiento
dc.subject.odspa15 Vida de ecosistemas terrestres
dc.subject.odspa14 Vida submarina
dc.title<i>In Silico</i> Analysis of Putative Paralytic Shellfish Poisoning Toxins Export Proteins in Cyanobacteria
dc.typeartículo
dc.volumen8
sipa.indexWOS
sipa.trazabilidadWOS;2025-01-12
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