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Transcriptome-Based Identification of Highly Similar Odorant-Binding Proteins among Neotropical Stink Bugs and Their Egg Parasitoid.

Farias LR, Schimmelpfeng PH, Togawa RC, Costa MM, Grynberg P, Martins NF, Borges M, Blassioli-Moraes MC, Laumann RA, Báo SN, Paula DP - PLoS ONE (2015)

Bottom Line: The deduced amino acid sequences of the full-length OBPs had low intraspecific similarity, but very high similarity between two pairs of OBPs from E. heros and C. ubica (76.4 and 84.0%) and between two pairs of OBPs from the parasitoid and its preferred host E. heros (82.4 and 88.5%), confirmed by a high similarity of their predicted tertiary structures.The similar pairs of OBPs from E. heros and C. ubica may suggest that they have derived from a common ancestor, and retain the same biological function to bind a ligand perceived or produced in both species.The T. podisi OBPs similar to E. heros were not orthologous to any known hymenopteran OBPs, and may have evolved independently and converged to the host OBPs, providing a possible basis for the host location of T. podisi using E. heros semiochemical cues.

View Article: PubMed Central - PubMed

Affiliation: University of Brasília, Campus Universitário Darcy Ribeiro, Brasília-DF, 70910-900, Brazil; Embrapa Genetic Resources and Biotechnology, Parque Estação Biológica, W5 Norte, P.O. Box 02372, Brasília, DF, 70770-917, Brazil.

ABSTRACT
Olfaction plays a fundamental role in insect survival through resource location and intra and interspecific communications. We used RNA-Seq to analyze transcriptomes for odorant-binding proteins (OBPs) from major stink bug pest species in Brazil, Euschistus heros, Chinavia ubica, and Dichelops melacanthus, and from their egg parasitoid, Telenomus podisi. We identified 23 OBPs in E. heros, 25 OBPs in C. ubica, 9 OBPs in D. melacanthus, and 7 OBPs in T. podisi. The deduced amino acid sequences of the full-length OBPs had low intraspecific similarity, but very high similarity between two pairs of OBPs from E. heros and C. ubica (76.4 and 84.0%) and between two pairs of OBPs from the parasitoid and its preferred host E. heros (82.4 and 88.5%), confirmed by a high similarity of their predicted tertiary structures. The similar pairs of OBPs from E. heros and C. ubica may suggest that they have derived from a common ancestor, and retain the same biological function to bind a ligand perceived or produced in both species. The T. podisi OBPs similar to E. heros were not orthologous to any known hymenopteran OBPs, and may have evolved independently and converged to the host OBPs, providing a possible basis for the host location of T. podisi using E. heros semiochemical cues.

No MeSH data available.


Related in: MedlinePlus

Alignment of the deduced amino acid sequences of OBPs from the stink bugs and other Hemiptera obtained from GenBank by BLASTx.Similarity is scored by matrix Blosum62 where the black color indicates 100% identity, darker grey 100% > identity ≥ 80%, lighter grey 80% > identity ≥ 60% and white color identity <60%. The sequence logo is at the top of the alignment. The amino acid percentage identity matrix is presented in Table H in S2 File. The conserved Cys are indicated by sequence logo. The species names are abbreviated with four letters, and their full names with all accession numbers of the OBP amino acid sequences are provided in Table I in S2 File.
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pone.0132286.g005: Alignment of the deduced amino acid sequences of OBPs from the stink bugs and other Hemiptera obtained from GenBank by BLASTx.Similarity is scored by matrix Blosum62 where the black color indicates 100% identity, darker grey 100% > identity ≥ 80%, lighter grey 80% > identity ≥ 60% and white color identity <60%. The sequence logo is at the top of the alignment. The amino acid percentage identity matrix is presented in Table H in S2 File. The conserved Cys are indicated by sequence logo. The species names are abbreviated with four letters, and their full names with all accession numbers of the OBP amino acid sequences are provided in Table I in S2 File.

Mentions: The similarity analysis of the mined hypothetical OBPs from the target stink bugs and parasitoid (Fig 4) with other orthologous OBPs from different insect species is represented in Figs 5 and 6 and in Table H in S2 File. The predicted tertiary structure of the stinkbug and parasitoid full-length putative OBPs are individually presented in Figure A in S2 File. In all the alignments the most conserved regions were around the conserved Cys. The sequence similarity among EherOBPs ranged from 5.1 to 25.2%, among CubiOBPs from 9.3 to 25.3%, and among TpodOBPs from 16.3 to 27.5%.


Transcriptome-Based Identification of Highly Similar Odorant-Binding Proteins among Neotropical Stink Bugs and Their Egg Parasitoid.

Farias LR, Schimmelpfeng PH, Togawa RC, Costa MM, Grynberg P, Martins NF, Borges M, Blassioli-Moraes MC, Laumann RA, Báo SN, Paula DP - PLoS ONE (2015)

Alignment of the deduced amino acid sequences of OBPs from the stink bugs and other Hemiptera obtained from GenBank by BLASTx.Similarity is scored by matrix Blosum62 where the black color indicates 100% identity, darker grey 100% > identity ≥ 80%, lighter grey 80% > identity ≥ 60% and white color identity <60%. The sequence logo is at the top of the alignment. The amino acid percentage identity matrix is presented in Table H in S2 File. The conserved Cys are indicated by sequence logo. The species names are abbreviated with four letters, and their full names with all accession numbers of the OBP amino acid sequences are provided in Table I in S2 File.
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4498631&req=5

pone.0132286.g005: Alignment of the deduced amino acid sequences of OBPs from the stink bugs and other Hemiptera obtained from GenBank by BLASTx.Similarity is scored by matrix Blosum62 where the black color indicates 100% identity, darker grey 100% > identity ≥ 80%, lighter grey 80% > identity ≥ 60% and white color identity <60%. The sequence logo is at the top of the alignment. The amino acid percentage identity matrix is presented in Table H in S2 File. The conserved Cys are indicated by sequence logo. The species names are abbreviated with four letters, and their full names with all accession numbers of the OBP amino acid sequences are provided in Table I in S2 File.
Mentions: The similarity analysis of the mined hypothetical OBPs from the target stink bugs and parasitoid (Fig 4) with other orthologous OBPs from different insect species is represented in Figs 5 and 6 and in Table H in S2 File. The predicted tertiary structure of the stinkbug and parasitoid full-length putative OBPs are individually presented in Figure A in S2 File. In all the alignments the most conserved regions were around the conserved Cys. The sequence similarity among EherOBPs ranged from 5.1 to 25.2%, among CubiOBPs from 9.3 to 25.3%, and among TpodOBPs from 16.3 to 27.5%.

Bottom Line: The deduced amino acid sequences of the full-length OBPs had low intraspecific similarity, but very high similarity between two pairs of OBPs from E. heros and C. ubica (76.4 and 84.0%) and between two pairs of OBPs from the parasitoid and its preferred host E. heros (82.4 and 88.5%), confirmed by a high similarity of their predicted tertiary structures.The similar pairs of OBPs from E. heros and C. ubica may suggest that they have derived from a common ancestor, and retain the same biological function to bind a ligand perceived or produced in both species.The T. podisi OBPs similar to E. heros were not orthologous to any known hymenopteran OBPs, and may have evolved independently and converged to the host OBPs, providing a possible basis for the host location of T. podisi using E. heros semiochemical cues.

View Article: PubMed Central - PubMed

Affiliation: University of Brasília, Campus Universitário Darcy Ribeiro, Brasília-DF, 70910-900, Brazil; Embrapa Genetic Resources and Biotechnology, Parque Estação Biológica, W5 Norte, P.O. Box 02372, Brasília, DF, 70770-917, Brazil.

ABSTRACT
Olfaction plays a fundamental role in insect survival through resource location and intra and interspecific communications. We used RNA-Seq to analyze transcriptomes for odorant-binding proteins (OBPs) from major stink bug pest species in Brazil, Euschistus heros, Chinavia ubica, and Dichelops melacanthus, and from their egg parasitoid, Telenomus podisi. We identified 23 OBPs in E. heros, 25 OBPs in C. ubica, 9 OBPs in D. melacanthus, and 7 OBPs in T. podisi. The deduced amino acid sequences of the full-length OBPs had low intraspecific similarity, but very high similarity between two pairs of OBPs from E. heros and C. ubica (76.4 and 84.0%) and between two pairs of OBPs from the parasitoid and its preferred host E. heros (82.4 and 88.5%), confirmed by a high similarity of their predicted tertiary structures. The similar pairs of OBPs from E. heros and C. ubica may suggest that they have derived from a common ancestor, and retain the same biological function to bind a ligand perceived or produced in both species. The T. podisi OBPs similar to E. heros were not orthologous to any known hymenopteran OBPs, and may have evolved independently and converged to the host OBPs, providing a possible basis for the host location of T. podisi using E. heros semiochemical cues.

No MeSH data available.


Related in: MedlinePlus