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Transcriptome-Based Identification of Highly Similar Odorant-Binding Proteins among Neotropical Stink Bugs and Their Egg Parasitoid
Author(s) -
Luciana Ramalho de Farias,
Pedro H. C. Schimmelpfeng,
Roberto Coiti Togawa,
Marcos M. C. Costa,
Priscila Grynberg,
N. F. Martins,
Miguel Borges,
Maria Carolina BlassioliMoraes,
Raúl Alberto Laumann,
Sônia Nair Báo,
Débora Pires Paula
Publication year - 2015
Publication title -
plos one
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.99
H-Index - 332
ISSN - 1932-6203
DOI - 10.1371/journal.pone.0132286
Subject(s) - biology , parasitoid , intraspecific competition , zoology , hymenoptera
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.

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