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Moths use pheromones to ensure intraspecific communication. Nevertheless, few studies are focused on both intra- and intersexual communication based on pheromone recognition. Pheromone-binding proteins (PBPs) are generally believed pivotal for male moths in recognizing female pheromones. Our research revealed that PBP1 of Agriphila aeneociliella (AaenPBP1) serves a dual function in both intra- and intersexual pheromone recognition. Here, a total of 20 odorant-binding protein (OBP) family genes from A. aeneociliella were identified and subjected to transcriptional analysis. Among these, AaenPBP1 was primarily highly expressed in the antennae. Competitive fluorescence binding assays and molecular docking analyses demonstrated that AaenPBP1 exhibits a strong binding affinity for the female sex pheromone (Z)-9-Hexadecenyl acetate and the male pheromone 1-Nonanal. Notably, hydrogen bonds were observed between Ser56 and the ligands. The analysis of pheromone components and PBPs in lepidopteran lineage suggested that their strong and precise interactions, shaped by coevolution, may play a crucial role in facilitating reproductive isolation in moths. Our findings provide valuable insight into the functional significance of PBPs in invertebrates and support the development of behavioral regulation tools as part of an integrated pest management strategy targeting crambid pests.

Odorant binding proteins (Obps) are expressed at extremely high levels in the antennae of insects, and have long been believed essential for carrying hydrophobic odorants to odor receptors. Previously we found that when one functional type of olfactory sensillum in Drosophila was depleted of its sole abundant Obp, it retained a robust olfactory response (Larter et al., 2016). Here we have deleted all the Obp genes that are abundantly expressed in the antennal basiconic sensilla. All of six tested sensillum types responded robustly to odors of widely diverse chemical or temporal structure. One mutant gave a greater physiological and behavioral response to an odorant that affects oviposition. Our results support a model in which many sensilla can respond to odorants in the absence of Obps, and many Obps are not essential for olfactory response, but that some Obps can modulate olfactory physiology and the behavior that it drives.

The giant panda Ailuropoda melanoleuca belongs to the family of Ursidae; however, it is not carnivorous, feeding almost exclusively on bamboo. Being equipped with a typical carnivorous digestive apparatus, the giant panda cannot get enough energy for an active life and spends most of its time digesting food or sleeping. Feeding and mating are both regulated by odors and pheromones; therefore, a better knowledge of olfaction at the molecular level can help in designing strategies for the conservation of this species. In this context, we have identified the odorant-binding protein (OBP) repertoire of the giant panda and mapped the protein expression in nasal mucus and saliva through proteomics. Four OBPs have been identified in nasal mucus, while the other two were not detected in the samples examined. In particular, AimelOBP3 is similar to a subset of OBPs reported as pheromone carriers in the urine of rodents, saliva of the boar, and seminal fluid of the rabbit. We expressed this protein, mapped its binding specificity, and determined its crystal structure. Structural data guided the design and preparation of three protein mutants bearing single-amino acid replacements in the ligand-binding pocket, for which the corresponding binding affinity spectra were measured. We also expressed AimelOBP5, which is markedly different from AimelOBP3 and complementary in its binding spectrum. By comparing our binding data with the structures of bamboo volatiles and those of typical mammalian pheromones, we formulate hypotheses on which may be the most relevant semiochemicals for the giant panda.

Odorant binding proteins (Obps) are remarkable in their number, diversity, and abundance, yet their role in olfactory coding remains unclear. They are widely believed to be required for transporting hydrophobic odorants through an aqueous lymph to odorant receptors. We construct a map of the Drosophila antenna, in which the abundant Obps are mapped to olfactory sensilla with defined functions. The results lay a foundation for an incisive analysis of Obp function. The map identifies a sensillum type that contains a single abundant Obp, Obp28a. Surprisingly, deletion of the sole abundant Obp in these sensilla does not reduce the magnitude of their olfactory responses. The results suggest that this Obp is not required for odorant transport and that this sensillum does not require an abundant Obp. The results further suggest a novel role for this Obp in buffering changes in the odor environment, perhaps providing a molecular form of gain control. Insects use their sense of smell to find mates, to find food and – in the case of insects that transmit diseases such as malaria and Zika – to find us. If we can understand how insect scent detection works at the molecular and cellular level, we may be able to devise new ways of manipulating the insects’ sense of smell and prevent them from finding us. Insects contain a family of proteins called odorant binding proteins that are intriguing in several ways. They are numerous (there are 52 kinds in the fruit fly Drosophila), they are diverse and some are made in remarkably large amounts in the antennae. Fine hair-like structures known as olfactory sensilla protrude from the surface of the antennae. Odorant binding proteins are widely believed to carry odorant molecules through the fluid inside the sensilla to olfactory neurons, which then send signals that trigger the insect’s response to the scent. Larter et al. have now mapped the most abundant odorant binding proteins to the various olfactory sensilla of Drosophila. This revealed that a type of sensillum known as ab8 contained only one abundant odorant binding protein, called Obp28a. Unexpectedly, Larter et al. found that ab8 sensilla that are deprived of this protein respond strongly to odorant molecules. This result suggests that Obp28a is not required to transport odorants to the neurons in ab8; indeed, it appears that these neurons do not require an abundant odorant binding protein in order to respond to a scent. Instead, Obp28a helps to moderate the effects of sudden changes in the level of an odorant in the environment, so that concentrated odors do not trigger too large a response from the olfactory neurons. The details of the role that Obp28a plays in olfactory sensilla remain to be investigated in future studies, and the map created by Larter et al. also lays a foundation for studying the roles of other odorant binding proteins. The discovery that Obp28a is not needed to transport odorant molecules also raises questions about how insects are able to detect smells. Many odorant molecules repel water, so how do these molecules travel through the fluid in the sensilla if odorant binding proteins are not needed to transport them?

In Drosophila melanogaster and other insects, the seminal fluid proteins (SFPs) and male sex pheromones that enter the female with sperm during mating are essential for fertility and induce profound post-mating effects on female physiology. The SFPs in D. melanogaster and other taxa include several members of the large gene family known as odorant binding proteins (Obps). Work in Drosophila has shown that some Obp genes are highly expressed in the antennae and can mediate behavioral responses to odorants, potentially by binding and carrying these molecules to odorant receptors. These observations have led to the hypothesis that the seminal Obps might act as molecular carriers for pheromones or other compounds important for male fertility, though functional evidence in any species is lacking. Here, we used functional genetics to test the role of the seven seminal Obps in D. melanogaster fertility and the post-mating response (PMR). We found that Obp56g is required for male fertility and the induction of the PMR, whereas the other six genes are dispensable. We found males lacking Obp56g fail to form a mating plug in the mated female’s reproductive tract, leading to ejaculate loss and reduced sperm storage, likely due to its expression in the male ejaculatory bulb. We also examined the evolutionary history of these seminal Obp genes, as several studies have documented rapid evolution and turnover of SFP genes across taxa. We found extensive lability in gene copy number and evidence of positive selection acting on two genes, Obp22a and Obp51a . Comparative RNAseq data from the male reproductive tract of multiple Drosophila species revealed that Obp56g shows high male reproductive tract expression in a subset of taxa, though conserved head expression across the phylogeny. Together, these functional and expression data suggest that Obp56g may have been co-opted for a reproductive function over evolutionary time.

Background Olfaction and gustation underlie behaviors that are crucial for insect fitness, such as host and mate selection. The detection of semiochemicals is mediated via proteins from large and rapidly evolving chemosensory gene families; however, the links between a species’ ecology and the diversification of these genes remain poorly understood. Hence, we annotated the chemosensory genes from genomes of select wood-boring coleopterans, and compared the gene repertoires from stenophagous species with those from polyphagous species. Results We annotated 86 odorant receptors (ORs), 60 gustatory receptors (GRs), 57 ionotropic receptors (IRs), 4 sensory neuron membrane proteins (SNMPs), 36 odorant binding proteins (OBPs), and 11 chemosensory proteins (CSPs) in the mountain pine beetle ( Dendroctonus ponderosae ), and 47 ORs, 30 GRs, 31 IRs, 4 SNMPs, 12 OBPs, and 14 CSPs in the emerald ash borer ( Agrilus planipennis ). Four SNMPs and 17 CSPs were annotated in the polyphagous wood-borer Anoplophora glabripennis. The gene repertoires in the stenophagous D. ponderosae and A. planipennis are reduced compared with those in the polyphagous A. glabripennis and T. castaneum , which is largely manifested through small gene lineage expansions and entire lineage losses. Alternative splicing of GR genes was limited in D. ponderosae and apparently absent in A. planipennis , which also seems to have lost one carbon dioxide receptor (GR1). A. planipennis has two SNMPs, which are related to SNMP3 in T. castaneum. D. ponderosae has two alternatively spliced OBP genes, a novel OBP “tetramer”, and as many as eleven IR75 members . Simple orthology was generally rare in beetles; however, we found one clade with orthologues of putative bitter-taste GRs (named the “GR215 clade”), and conservation of IR60a from Drosophila melanogaster. Conclusions Our genome annotations represent important quantitative and qualitative improvements of the original datasets derived from transcriptomes of D. ponderosae and A. planipennis , facilitating evolutionary analysis of chemosensory genes in the Coleoptera where only a few genomes were previously annotated. Our analysis suggests a correlation between chemosensory gene content and host specificity in beetles. Future studies should include additional species to consolidate this correlation, and functionally characterize identified proteins as an important step towards improved control of these pests.

Insecticide resistance has become a critical issue threatening global agricultural production and food security. Previous studies have primarily focused on resistance mechanisms such as target-site mutations, enhanced metabolic detoxification, and reduced cuticular penetration. However, growing evidence in recent years indicates that odorant-binding proteins (OBPs) and chemosensory proteins (CSPs)—beyond their roles in chemoreception—also play key roles in the development of insecticide resistance. Research has revealed that these proteins significantly modulate insect susceptibility to insecticides through various mechanisms, including direct binding to insecticides, regulation of detoxification metabolic pathways, and influence on behavioral adaptations in pests. This review also systematically summarizes modern research strategies employed to investigate OBPs/CSPs functions, including high-throughput omics technologies, RNA interference, CRISPR-Cas9 gene editing, and molecular docking, while discussing the potential of targeting these proteins for developing novel insecticides and resistance management strategies. Although significant progress has been made in laboratory studies, the practical application of OBPs/CSPs-mediated resistance mechanisms still faces multiple challenges. Future research should prioritize multi-gene targeting strategies, cross-species functional validation, and field trial implementation to facilitate the development of green and precise pest control approaches based on OBPs and CSPs, thereby offering new pathways for sustainable agriculture.

Animals can easily detect hundreds of thousands of odors in the environment with high sensitivity and selectivity. With the progress of biological olfactory research, scientists have extracted multiple biomaterials and integrated them with different transducers thus generating numerous biosensors. Those biosensors inherit the sensing ability of living organisms and present excellent detection performance. In this paper, we mainly introduce odor biosensors based on substances from animal olfactory systems. Several instances of organ/tissue-based, cell-based, and protein-based biosensors are described and compared. Furthermore, we list some other biological materials such as peptide, nanovesicle, enzyme, and aptamer that are also utilized in odor biosensors. In addition, we illustrate the further developments of odor biosensors.

The genus Solenopsis is also known as imported fire ants and comprises several invasive species, including the highly aggressive Solenopsis invicta (RIFA). Imported fire ants have spread from South America to every continent due to international trade and climate change, affecting agriculture, ecosystems, and even human health. Conventional chemical insecticides are widely used for controlling Solenopsis spp., however, their application results in environmental and health risks, including toxicity to non-target organisms. These concerns have led to growing interest in biopesticides as a safer and more sustainable alternative. This review examines the effects of plant-derived biopesticides on Solenopsis spp., with particular emphasis on RIFA as a model system and essential oils and their main volatiles as a safe agroecological control alternative. Overall, a solid background suggests that azadirachtin, eugenol, carvacrol, citral, and isothiocyanates induce rapid mortality and behavioral disruption in fire ants, often through blocking acetylcholinesterase (AChE) and glutathione S-transferase (GST). In addition to these enzymatic targets, growing evidence highlights the role of the chemosensory system, affecting odorant receptors and semiochemical perception. Twenty-four odorant-binding proteins (OBPs) and 23 chemosensory proteins (CSPs) have been identified in RIFA, with differential expression depending on factors such as caste, tissue, foraging activity, and corpse removal. The current state of the art suggests that bait strategies combining toxicants with attractants or repellents may be considered to improve the control efficiency of RIFA. Although biopesticides exhibit low or negligible risks to non-target organisms and the environment, their efficacy, stability, and large-scale application face evident challenges in the short term. Understanding the roles of essential oils and their active compounds may contribute to more effective and sustainable control of imported fire ants.

Our understanding of the biochemical mechanisms that mediate chemoreception in insects has been greatly improved after the discovery of olfactory and taste receptor proteins. However, the presence of soluble polypeptides in high concentration around the dendrites of sensory neurons still poses unanswered questions. More than 2 decades after their discovery and despite the wealth of structural information available, the physiological function of odorant-binding proteins is not well understood. More recently, members of a second family of soluble polypeptides, the chemosensory proteins, were also discovered in the lymph of chemosensilla. Here we review the structural properties of both classes of soluble proteins, their affinity to small ligands, and their expression in the different parts of the insect body and subcellular localisation. Finally, we discuss current ideas and models of the role of such proteins in insect chemoreception.