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The venom composition of the parasitic wasp Chelonus inanitus resolved by combined expressed sequence tags analysis and proteomic approach

Bruno Vincent1, Martha Kaeslin2, Thomas Roth2, Manfred Heller3, Julie Poulain4, François Cousserans5, Johann Schaller6, Marylène Poirié7, Beatrice Lanzrein2, Jean-Michel Drezen1 and Sébastien JM Moreau1*

Author Affiliations

1 UMR 6035 CNRS, Institut de Recherche sur la Biologie de l'Insecte, Faculté des Sciences et Techniques, Université François-Rabelais, Parc Grandmont, 37200 Tours, France

2 Institute of Cell Biology, University of Berne, Baltzerstrasse 4, CH-3012 Berne, Switzerland

3 Department of Clinical Research, University of Bern, Murtenstrasse 35, CH-3010 Berne, Switzerland

4 CEA, DSV, Institut de Génomique, Genoscope, 2 rue Gaston Crémieux, CP5706, 91057 Evry, France

5 UMR INRA-UM2 1231, Laboratoire Biologie Intégrative et Virologie des Insectes, Université de Montpellier 2, Place E. Bataillon, CC54, 34095 Montpellier cedex 05, France

6 Department of Chemistry and Biochemistry, University of Berne, Freiestrasse 3, CH-3012 Berne, Switzerland

7 UMR INRA (1301)-CNRS (6243)-Université Nice Sophia Antipolis, "Interactions Biotiques et Santé Végétale", Institut Agrobiotech, 400 Route des Chappes, 06903 Sophia Antipolis, France

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BMC Genomics 2010, 11:693  doi:10.1186/1471-2164-11-693

Published: 7 December 2010

Additional files

Additional file 1:

Table of peptide identification. Peptidic sequences obtained from the nano-LC-MS/MS analysis of venom proteins from C. inanitus are shown in blue into the corresponding amino acid sequences encoded by ORFs obtained from the transcriptome analysis of C. inanitus venom glands.

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Additional file 2:

Amino acid sequence alignment of Ci-23a and the venom protein from C. sp near curvimaculatus. The amino acid sequence of the venom protein from C. sp near curvimaculatus was retrieved from GenBank [GenBank:ACI70208.1]. The position of a potential cleavage site for both N-arginine dibasic convertase and subtilisin-like proprotein convertase is boxed in black in the Ci-23a sequence. Red and green arrows indicate the beginning of the predicted signal peptide and mature protein sequences of Ci-23a, respectively. Serine residues that potentially serve as glycosaminoglycan attachment sites are indicated by blue triangles under the sequence of the venom protein from C. sp near curvimaculatus. Sequence printed in bold was also obtained by N-terminal sequencing of the Ci-23a protein.

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Additional file 3:

Amino acid sequence alignment of representative chitinases from different insect species. The sequence of the Ci-45 venom chitinase from C. inanitus was aligned with sequences of chitinases from the following species: the parasitic wasps C. sp. near curvimaculatus [GenBank:AAA61639.1], T. nigriceps [GenBank:AAX69085.1] and N. vitripennis [GenBank:NP_001128139.2] and the beetle Monochamus alternatus [GenBank:BAF49605.1]. The four conserved regions are boxed. Black triangles indicate catalytic residues. Locations of the glycosyl hydrolase family 18 and chitin-binding Peritrophin-A (CBM_14) domains are indicated by blue and green lines, respectively. Red and green arrows indicate the beginning of the predicted signal peptide and mature protein sequences of Ci-45, respectively. Sequence printed in bold was also obtained by N-terminal sequencing of the Ci-45 protein.

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Additional file 4:

Amino acid sequence alignment of Imaginal disc Growth Factors (IDGFs)-like proteins from different insect species. The sequence of the Ci-48b from C. inanitus was aligned with sequences from the following species: N. vitripennis [GenBank:XP_001599305.1], A. mellifera [GenBank:XP_396769.2] and Manduca sexta [GenBank:ACW82749.1]. The conserved region II is boxed. Triangle indicates a glutamine residue replacing, in these proteins, a glutamic acid residue of functional importance. Location of the glycosyl hydrolase family 18 domain is indicated by a blue line. Red and green arrows indicate the beginning of the predicted signal peptide and mature protein sequences of Ci-48b, respectively. Sequence printed in bold was also obtained by N-terminal sequencing of the Ci-48b protein.

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Additional file 5:

Amino acid sequence alignment of Ci-23c, Ci-220 and AD-873. The sequences of the Ci-23c and Ci-220 proteins from C. inanitus were aligned with the sequence of the AD-873 protein from Anopheles darlingi [GenBank:ACI30179.1]. Location of the chitin-binding Peritrophin-A (CBM_14) domains of Ci-23c are indicated by green lines under the alignment. Serine residues that potentially serve as glycosaminoglycan attachment sites are indicated by blue triangles. Red and green arrows indicate the beginning of the predicted signal peptide and mature protein sequences of Ci-23c, respectively.

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Additional file 6:

Partial amino acid sequence alignment of Ci-300 with insect metalloproteases. The sequence of Ci-300 was aligned with sequences of metalloproteases from the following species: N. vitripennis [NCBI Reference Sequence:XP_001604431.1] and [NCBI Reference Sequence: NP_001155006.1], P. hypochondriaca [GenBank:CAD21587.1] and E. pennicornis [GenBank:ACF60597.1]. The Zn2+-binding motif of HExxHxxGxxH featuring known metalloproteases' partial alignment is boxed in black.

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Additional file 7:

Amino acid sequence alignment of Ci-40a with serine protease homologs (SPHs). The partial sequence of Ci-40a was aligned with sequences of SPHs from the following species: A. mellifera [NCBI Reference Sequence:XP_623150.2], C. rubecula [GenBank:AAP49428.1], N. vitripennis [NCBI Reference Sequence:NP_001166254.1] and [NCBI Reference Sequence:NP_001155014.1] and A. aegypti [NCBI Reference Sequence:XP_001661226.1]. The location of the trypsin-like serine protease domain of Ci40a is indicated by a blue line under the alignment.

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Additional file 8:

Sequence similarities between Ci-48a, Vem17 and Ci-80b and proteins similar to isoforms of lethal (1) G0193. Sequences similarities were determined by comparing the amino acid sequences of Ci-48a, Vem17 and Ci-80 to protein sequences deposited in NCBI nr database using BLASTP algorithm. The percentage of identity and E-value are given for each comparison. E: embryo; n.d.: not determined; n.s.: no significant similarity found (E-value> 1e-04); SG: salivary gland; VG: venom gland.

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Additional file 9:

Phylogeny of the major superfamilies of Hymenoptera. Family and species names discussed in the present paper are indicated on the right side of the figure. The phylogeny of Hymenoptera shown on the left side of the figure is adapted from [9].

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