Cargando…

Plectreurys tristis venome: A proteomic and transcriptomic analysis

Spider venoms are complex cocktails rich in peptides, proteins and organic molecules that collectively act to immobilize prey. Venoms of the primitive hunting spider, Plectreurys tristis, have numerous neurotoxic peptides called “plectoxins” (PLTX), a unique acylpolyamine called bis(agmatine)oxalami...

Descripción completa

Detalles Bibliográficos
Autores principales: Zobel-Thropp, Pamela A, Thomas, Emily Z, David, Cynthia L, Breci, Linda A, Binford, Greta J
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Library Publishing Media 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4231235/
https://www.ncbi.nlm.nih.gov/pubmed/25400903
_version_ 1782344409114738688
author Zobel-Thropp, Pamela A
Thomas, Emily Z
David, Cynthia L
Breci, Linda A
Binford, Greta J
author_facet Zobel-Thropp, Pamela A
Thomas, Emily Z
David, Cynthia L
Breci, Linda A
Binford, Greta J
author_sort Zobel-Thropp, Pamela A
collection PubMed
description Spider venoms are complex cocktails rich in peptides, proteins and organic molecules that collectively act to immobilize prey. Venoms of the primitive hunting spider, Plectreurys tristis, have numerous neurotoxic peptides called “plectoxins” (PLTX), a unique acylpolyamine called bis(agmatine)oxalamide, and larger unidentified protein components. These spiders also have unconventional multi-lobed venom glands. Inspired by these unusual characteristics and their phylogenetic position as Haplogynes, we have partially characterized the venome of P. tristis using combined transcriptomic and proteomic methods. With these analyses we found known venom neurotoxins U(1)-PLTX-Pt1a, U(3)-PLTX-Pt1a, and we discovered new groups of potential neurotoxins, expanding the U(1)- and ω-PLTX families and adding U(4)-through U(9)-PLTX as six new groups. The venom also contains proteins that are homologs of astacin metalloproteases that, combined with venom peptides, make up 94% of components detected in crude venom, while the remaining 6% is a single undescribed protein with unknown function. Other proteins detected in the transcriptome were found to be members of conserved gene families and make up 20% of the transcripts. These include cDNA sequences that match venom proteins from Mesobuthus and Hottentotta scorpions, Loxosceles and Dysdera spiders, and also salivary and secreted peptide sequences from Ixodes, Amblyomma and Rhipicephalus ticks. Finally, we show that crude venom has neurotoxic effects and an effective paralytic dose on crickets of 3.3µg/gm.
format Online
Article
Text
id pubmed-4231235
institution National Center for Biotechnology Information
language English
publishDate 2014
publisher Library Publishing Media
record_format MEDLINE/PubMed
spelling pubmed-42312352014-11-14 Plectreurys tristis venome: A proteomic and transcriptomic analysis Zobel-Thropp, Pamela A Thomas, Emily Z David, Cynthia L Breci, Linda A Binford, Greta J J Venom Res Research Article Spider venoms are complex cocktails rich in peptides, proteins and organic molecules that collectively act to immobilize prey. Venoms of the primitive hunting spider, Plectreurys tristis, have numerous neurotoxic peptides called “plectoxins” (PLTX), a unique acylpolyamine called bis(agmatine)oxalamide, and larger unidentified protein components. These spiders also have unconventional multi-lobed venom glands. Inspired by these unusual characteristics and their phylogenetic position as Haplogynes, we have partially characterized the venome of P. tristis using combined transcriptomic and proteomic methods. With these analyses we found known venom neurotoxins U(1)-PLTX-Pt1a, U(3)-PLTX-Pt1a, and we discovered new groups of potential neurotoxins, expanding the U(1)- and ω-PLTX families and adding U(4)-through U(9)-PLTX as six new groups. The venom also contains proteins that are homologs of astacin metalloproteases that, combined with venom peptides, make up 94% of components detected in crude venom, while the remaining 6% is a single undescribed protein with unknown function. Other proteins detected in the transcriptome were found to be members of conserved gene families and make up 20% of the transcripts. These include cDNA sequences that match venom proteins from Mesobuthus and Hottentotta scorpions, Loxosceles and Dysdera spiders, and also salivary and secreted peptide sequences from Ixodes, Amblyomma and Rhipicephalus ticks. Finally, we show that crude venom has neurotoxic effects and an effective paralytic dose on crickets of 3.3µg/gm. Library Publishing Media 2014-09-20 /pmc/articles/PMC4231235/ /pubmed/25400903 Text en © Copyright The Author(s) http://creativecommons.org/licenses/by-nc/3.0 First Published by Library Publishing Media. This is an open access article, published under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0). This license permits non-commercial use, distribution and reproduction of the article, provided the original work is appropriately acknowledged with correct citation details.
spellingShingle Research Article
Zobel-Thropp, Pamela A
Thomas, Emily Z
David, Cynthia L
Breci, Linda A
Binford, Greta J
Plectreurys tristis venome: A proteomic and transcriptomic analysis
title Plectreurys tristis venome: A proteomic and transcriptomic analysis
title_full Plectreurys tristis venome: A proteomic and transcriptomic analysis
title_fullStr Plectreurys tristis venome: A proteomic and transcriptomic analysis
title_full_unstemmed Plectreurys tristis venome: A proteomic and transcriptomic analysis
title_short Plectreurys tristis venome: A proteomic and transcriptomic analysis
title_sort plectreurys tristis venome: a proteomic and transcriptomic analysis
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4231235/
https://www.ncbi.nlm.nih.gov/pubmed/25400903
work_keys_str_mv AT zobelthropppamelaa plectreurystristisvenomeaproteomicandtranscriptomicanalysis
AT thomasemilyz plectreurystristisvenomeaproteomicandtranscriptomicanalysis
AT davidcynthial plectreurystristisvenomeaproteomicandtranscriptomicanalysis
AT brecilindaa plectreurystristisvenomeaproteomicandtranscriptomicanalysis
AT binfordgretaj plectreurystristisvenomeaproteomicandtranscriptomicanalysis