Pdl1 is a putative lipase that enhances Photorhabdus toxin complex secretion.

The Toxin Complex (TC) is a large multi-subunit toxin first characterized in the insect pathogens Photorhabdus and Xenorhabdus, but now seen in a range of pathogens, including those of humans. These complexes comprise three protein subunits, A, B and C which in the Xenorhabdus toxin are found in a 4...

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Autores principales: Guowei Yang, Carmen Sara Hernández-Rodríguez, Michael L Beeton, Paul Wilkinson, Richard H Ffrench-Constant, Nicholas R Waterfield
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Publicado: Public Library of Science (PLoS) 2012
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spelling oai:doaj.org-article:53a05a92a6d74129aee1d7c64942f0d12021-11-18T06:04:26ZPdl1 is a putative lipase that enhances Photorhabdus toxin complex secretion.1553-73661553-737410.1371/journal.ppat.1002692https://doaj.org/article/53a05a92a6d74129aee1d7c64942f0d12012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22615559/pdf/?tool=EBIhttps://doaj.org/toc/1553-7366https://doaj.org/toc/1553-7374The Toxin Complex (TC) is a large multi-subunit toxin first characterized in the insect pathogens Photorhabdus and Xenorhabdus, but now seen in a range of pathogens, including those of humans. These complexes comprise three protein subunits, A, B and C which in the Xenorhabdus toxin are found in a 4:1:1 stoichiometry. Some TCs have been demonstrated to exhibit oral toxicity to insects and have the potential to be developed as a pest control technology. The lack of recognisable signal sequences in the three large component proteins hinders an understanding of their mode of secretion. Nevertheless, we have shown the Photorhabdus luminescens (Pl) Tcd complex has been shown to associate with the bacteria's surface, although some strains can also release it into the surrounding milieu. The large number of tc gene homologues in Pl make study of the export process difficult and as such we have developed and validated a heterologous Escherichia coli expression model to study the release of these important toxins. In addition to this model, we have used comparative genomics between a strain that releases high levels of Tcd into the supernatant and one that retains the toxin on its surface, to identify a protein responsible for enhancing secretion and release of these toxins. This protein is a putative lipase (Pdl1) which is regulated by a small tightly linked antagonist protein (Orf53). The identification of homologues of these in other bacteria, linked to other virulence factor operons, such as type VI secretion systems, suggests that these genes represent a general and widespread mechanism for enhancing toxin release in gram negative pathogens.Guowei YangCarmen Sara Hernández-RodríguezMichael L BeetonPaul WilkinsonRichard H Ffrench-ConstantNicholas R WaterfieldPublic Library of Science (PLoS)articleImmunologic diseases. AllergyRC581-607Biology (General)QH301-705.5ENPLoS Pathogens, Vol 8, Iss 5, p e1002692 (2012)
institution DOAJ
collection DOAJ
language EN
topic Immunologic diseases. Allergy
RC581-607
Biology (General)
QH301-705.5
spellingShingle Immunologic diseases. Allergy
RC581-607
Biology (General)
QH301-705.5
Guowei Yang
Carmen Sara Hernández-Rodríguez
Michael L Beeton
Paul Wilkinson
Richard H Ffrench-Constant
Nicholas R Waterfield
Pdl1 is a putative lipase that enhances Photorhabdus toxin complex secretion.
description The Toxin Complex (TC) is a large multi-subunit toxin first characterized in the insect pathogens Photorhabdus and Xenorhabdus, but now seen in a range of pathogens, including those of humans. These complexes comprise three protein subunits, A, B and C which in the Xenorhabdus toxin are found in a 4:1:1 stoichiometry. Some TCs have been demonstrated to exhibit oral toxicity to insects and have the potential to be developed as a pest control technology. The lack of recognisable signal sequences in the three large component proteins hinders an understanding of their mode of secretion. Nevertheless, we have shown the Photorhabdus luminescens (Pl) Tcd complex has been shown to associate with the bacteria's surface, although some strains can also release it into the surrounding milieu. The large number of tc gene homologues in Pl make study of the export process difficult and as such we have developed and validated a heterologous Escherichia coli expression model to study the release of these important toxins. In addition to this model, we have used comparative genomics between a strain that releases high levels of Tcd into the supernatant and one that retains the toxin on its surface, to identify a protein responsible for enhancing secretion and release of these toxins. This protein is a putative lipase (Pdl1) which is regulated by a small tightly linked antagonist protein (Orf53). The identification of homologues of these in other bacteria, linked to other virulence factor operons, such as type VI secretion systems, suggests that these genes represent a general and widespread mechanism for enhancing toxin release in gram negative pathogens.
format article
author Guowei Yang
Carmen Sara Hernández-Rodríguez
Michael L Beeton
Paul Wilkinson
Richard H Ffrench-Constant
Nicholas R Waterfield
author_facet Guowei Yang
Carmen Sara Hernández-Rodríguez
Michael L Beeton
Paul Wilkinson
Richard H Ffrench-Constant
Nicholas R Waterfield
author_sort Guowei Yang
title Pdl1 is a putative lipase that enhances Photorhabdus toxin complex secretion.
title_short Pdl1 is a putative lipase that enhances Photorhabdus toxin complex secretion.
title_full Pdl1 is a putative lipase that enhances Photorhabdus toxin complex secretion.
title_fullStr Pdl1 is a putative lipase that enhances Photorhabdus toxin complex secretion.
title_full_unstemmed Pdl1 is a putative lipase that enhances Photorhabdus toxin complex secretion.
title_sort pdl1 is a putative lipase that enhances photorhabdus toxin complex secretion.
publisher Public Library of Science (PLoS)
publishDate 2012
url https://doaj.org/article/53a05a92a6d74129aee1d7c64942f0d1
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AT paulwilkinson pdl1isaputativelipasethatenhancesphotorhabdustoxincomplexsecretion
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