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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

Number of GO categories exclusive and common to each species: (a) biological process, and (b) molecular function.A species was considered to have the category if it had more than 10 transcripts. The radii of the circles are proportional to the number of categories.
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pone.0132286.g003: Number of GO categories exclusive and common to each species: (a) biological process, and (b) molecular function.A species was considered to have the category if it had more than 10 transcripts. The radii of the circles are proportional to the number of categories.

Mentions: The biological processes diverged more among the target species than the molecular functions, as can be observed in Fig 3. More biological processes were identified in the antennae of C. ubica (n = 160, 70 exclusive), than in T. podisi (n = 121, 43 exclusive), E. heros (n = 87, 13 exclusive) and D. melacanthus (n = 39, 1 exclusive). In total, 32 biological processes were shared among the four species, but only two were exclusive to the three stink bug species. More molecular functions were identified in the whole body of T. podisi (n = 121, 39 exclusive), than in the stink bugs C. ubica (n = 107, 14 exclusive), E. heros (n = 99, 7 exclusive), and D. melacanthus (n = 49, none exclusive). The stink bugs shared more molecular functions among themselves than with the parasitoid T. podisi.


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)

Number of GO categories exclusive and common to each species: (a) biological process, and (b) molecular function.A species was considered to have the category if it had more than 10 transcripts. The radii of the circles are proportional to the number of categories.
© Copyright Policy
Related In: Results  -  Collection

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

pone.0132286.g003: Number of GO categories exclusive and common to each species: (a) biological process, and (b) molecular function.A species was considered to have the category if it had more than 10 transcripts. The radii of the circles are proportional to the number of categories.
Mentions: The biological processes diverged more among the target species than the molecular functions, as can be observed in Fig 3. More biological processes were identified in the antennae of C. ubica (n = 160, 70 exclusive), than in T. podisi (n = 121, 43 exclusive), E. heros (n = 87, 13 exclusive) and D. melacanthus (n = 39, 1 exclusive). In total, 32 biological processes were shared among the four species, but only two were exclusive to the three stink bug species. More molecular functions were identified in the whole body of T. podisi (n = 121, 39 exclusive), than in the stink bugs C. ubica (n = 107, 14 exclusive), E. heros (n = 99, 7 exclusive), and D. melacanthus (n = 49, none exclusive). The stink bugs shared more molecular functions among themselves than with the parasitoid T. podisi.

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