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Identification of Odorant-Binding Proteins (OBPs) and Functional Analysis of Phase-Related OBPs in the Migratory Locust.

ABSTRACT: Olfactory plasticity, which is one of the major characteristics of density-dependent phase polyphenism, plays critical roles in the large-scale aggregation formation of Locusta migratoria. It is still unknown whether odorant-binding proteins (OBPs) are involved in phase-related olfactory plasticity of locusts, despite the confirmed involvement of several types of olfactory perception genes. In this study, we performed a large-scale search for OBPs and verified their expression patterns in the migratory locust. We identified 17 OBPs in the L. migratoria genome, of which 10 were novel, and we found their scattering distribution characteristics by mapping the genomic loci. Next, we revealed that these OBPs with close phylogenic relationships displayed similar tissue-specific expression profiles by a combined analysis of qRT-PCR and phylogenetic tree reconstruction. In all identified locust OBPs, seven OBPs showed differential mRNA expression levels in antenna tissue between gregarious and solitarious nymphs. Six of these seven OBPs displayed higher mRNA expression in the antennae of gregarious nymphs. The mRNA expression of LmigOBP2 and LmigOBP4 increased during gregarization and decreased during solitarization. RNAi experiments confirmed that only LmigOBP4 regulates the behavioral traits to affect gregarious behavior. These results demonstrated that OBPs also play important roles in the regulation of phase-related behavior of the locusts.

SUBMITTER: Guo W

PROVIDER: S-EPMC6062766 | biostudies-literature |

REPOSITORIES: biostudies-literature

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Project description:Anopheles stephensi is an important vector of malaria in the South Asia, the Middle East, and Eastern Africa. The olfactory system of An. stephensi plays an important role in host-seeking, oviposition, and feeding. Odorant binding proteins (OBPs) are globular proteins that play a pivotal role in insect olfaction by transporting semiochemicals through the sensillum lymph to odorant receptors (ORs). Custom motifs designed from annotated OBPs of Aedes aegypti, Drosophila melanogaster, and Anopheles gambiae were used for the identification of putative OBPs from protein sequences of the An. stephensi Indian strain. Further, BLASTp was also performed to identify missing OBPs and ORs. Subsequently, the presence of domains common to OBPs was confirmed. Identified OBPs were further classified into three sub-classes. Phylogenetic and syntenic analyses were carried out to find homology, and thus the evolutionary relationship between An. stephensi OBPs and ORs with those of An. gambiae, Ae. aegypti and D. melanogaster. Gene structure and physicochemical properties of the OBPs and ORs were also predicted. A total of 44 OBPs and 45 ORs were predicted from the protein sequences of An. stephensi. OBPs were further classified into the classic (27), atypical (10) and plus-C (7) OBP subclasses. The phylogeny revealed close relationship of An. stephensi OBPs and ORs with An. gambiae homologs whereas only five OBPs and two ORs of An. stephensi were related to Ae. aegypti OBPs and ORs, respectively. However, D. melanogaster OBPs and ORs were distantly rooted. Synteny analyses showed the presence of collinear block between the OBPs and ORs of An. stephensi and An. gambiae as well as Ae. aegypti's. No homology was found with D. melanogaster OBPs and ORs. As an important component of the olfactory system, correctly identifying a species' OBPs and ORs provide a valuable resource for downstream translational research that will ultimately aim to better control the malaria vector An. stephensi.

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Identification of Odorant-Binding Proteins (OBPs) and Functional Analysis of Phase-Related OBPs in the Migratory Locust.

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