Marine Biotechnology

, Volume 17, Issue 1, pp 81–98

High Conopeptide Diversity in Conus tribblei Revealed Through Analysis of Venom Duct Transcriptome Using Two High-Throughput Sequencing Platforms

  • Neda Barghi
  • Gisela P. Concepcion
  • Baldomero M. Olivera
  • Arturo O. Lluisma
Original Article

DOI: 10.1007/s10126-014-9595-7

Cite this article as:
Barghi, N., Concepcion, G.P., Olivera, B.M. et al. Mar Biotechnol (2015) 17: 81. doi:10.1007/s10126-014-9595-7

Abstract

The venom of each species of Conus contains different kinds of pharmacologically active peptides which are mostly unique to that species. Collectively, the ~500–700 species of Conus produce a large number of these peptides, perhaps exceeding 140,000 different types in total. To date, however, only a small fraction of this diversity has been characterized via transcriptome sequencing. In addition, the sampling of this chemical diversity has not been uniform across the different lineages in the genus. In this study, we used high-throughput transcriptome sequencing approach to further investigate the diversity of Conus venom peptides. We chose a species, Conus tribblei, as a representative of a poorly studied clade of Conus. Using the Roche 454 and Illumina platforms, we discovered 136 unique and novel putative conopeptides belonging to 30 known gene superfamilies and 6 new conopeptide groups, the greatest diversity so far observed from a transcriptome. Most of the identified peptides exhibited divergence from the known conopeptides, and some contained cysteine frameworks observed for the first time in cone snails. In addition, several enzymes involved in posttranslational modification of conopeptides and also some proteins involved in efficient delivery of the conopeptides to prey were identified as well. Interestingly, a number of conopeptides highly similar to the conopeptides identified in a phylogenetically distant species, the generalist feeder Conus californicus, were observed. The high diversity of conopeptides and the presence of conopeptides similar to those in C. californicus suggest that C. tribblei may have a broad range of prey preferences.

Keywords

Conopeptide Transcriptome Conus tribblei Conotoxin Diversity 

Supplementary material

10126_2014_9595_MOESM10_ESM.doc (28 kb)
ESM 1(DOC 27 kb)
10126_2014_9595_MOESM1_ESM.doc (32 kb)
Fig. S 1The putative conopeptide precursors identified by ConoSorter. The prepeptide cleavage sites are shown in bold and are underlined (DOC 31 kb)
10126_2014_9595_MOESM2_ESM.doc (35 kb)
Fig. S 2The truncated putative conopeptide precursors of (a) A-, (b) G- and (c) O1-superfamilies. The conopeptides identified in C. tribblei are shown in black and the conopeptide nomenclature is as described in "Materials and Methods". The name of each conopeptide is presented as Ctr_#_T/N/TN: Ctr: C. tribblei, #: arbitrary assigned number, T: only present in the ‘Trinity conopeptide dataset’, N: only present in the ‘Newbler conopeptide dataset’, TN: present in both Trinity and Newbler conopeptide datasets. The reference sequences are shown in green and cysteine residues are shown in bold italic red. The names of the reference sequences are derived from the ConoServer database unless noted otherwise. The mature regions are underlined and the signal regions are highlighted (DOC 35 kb)
10126_2014_9595_MOESM3_ESM.doc (46 kb)
Fig. S 3The putative conopeptide precursors of (a) M superfamily, (b) con-ikot-ikot and (c) conkunitzin family. The notes are indicated in Fig. S 2 (DOC 46 kb)
10126_2014_9595_MOESM4_ESM.doc (45 kb)
Fig. S 4The putative conopeptide precursors of (a) conopressin/conophysin and (b) conodipine families. Conopressin domain is underlined in red at position 32–40 and conophysin is underlined in gray. The notes are indicated in Fig. S 2 (DOC 45 kb)
10126_2014_9595_MOESM5_ESM.doc (36 kb)
Fig. S 5The putative conopeptide precursors of (a) N-, (b) K- and (c) S-superfamilies. The notes are indicated in Fig. S 2 (DOC 36 kb)
10126_2014_9595_MOESM6_ESM.doc (50 kb)
Fig. S 6The putative conopeptide precursors of (a) I2-, (b) L-, (c) H-, (d) O1- and (e) O2-superfamilies. The notes are indicated in Fig. S 2 (DOC 50 kb)
10126_2014_9595_MOESM7_ESM.doc (34 kb)
Fig. S 7The putative conopeptide precursors of (a) D-, (b) I1- and (c) I3-superfamilies. The notes are indicated in Fig. S 2 (DOC 34 kb)
10126_2014_9595_MOESM8_ESM.doc (40 kb)
Fig. S 8The putative conopeptide precursors of (a) O3-, (b) J-, (c) Y-, (d) F-, and (e) B2-superfamilies. The notes are indicated in Fig. S 2 (DOC 39 kb)
10126_2014_9595_MOESM9_ESM.doc (41 kb)
Fig. S 9The putative conopeptide precursors of (a) P-, (b) R-, (c) W-, (d) Y2- and (e) B1-superfamilies (conantokin family). The notes are indicated in Fig. S 2 (DOC 41 kb)

Copyright information

© Springer Science+Business Media New York 2014

Authors and Affiliations

  • Neda Barghi
    • 1
  • Gisela P. Concepcion
    • 1
    • 2
  • Baldomero M. Olivera
    • 3
  • Arturo O. Lluisma
    • 1
    • 2
  1. 1.Marine Science InstituteUniversity of the PhilippinesQuezon CityPhilippines
  2. 2.Philippine Genome CenterUniversity of the PhilippinesQuezon CityPhilippines
  3. 3.Department of BiologyUniversity of UtahSalt Lake CityUSA