scholarly journals Lipocalins in arthropod chemical communication

Author(s):  
Jiao Zhu ◽  
Alessio Iannucci ◽  
Francesca Romana Dani ◽  
Wolfgang Knoll ◽  
Paolo Pelosi

Abstract Lipocalins represent one of the most successful superfamilies of proteins. Most of them are extracellular carriers for hydrophobic ligands across aqueous media, but other functions have been reported. They are present in most living organisms including bacteria. In animals they have been identified in mammals, molluscs and arthropods; sequences have also been reported for plants. A sub-group of lipocalins, referred to as odorant-binding proteins (OBPs), mediate chemical communication in mammals by ferrying specific pheromones to the vomeronasal organ. So far, these proteins have not been reported as carriers of semiochemicals in other living organisms; instead chemical communication in arthropods is mediated by other protein families structurally unrelated to lipocalins. A search in the databases has revealed extensive duplication and differentiation of lipocalin genes in some species of insects, crustaceans and chelicerates. Their large numbers, ranging from a handful to few dozens in the same species, their wide divergence, both within and between species, and their expression in chemosensory organs suggest that such expansion may have occurred under environmental pressure, thus supporting the hypothesis that lipocalins may be involved in chemical communication in arthropods.

2021 ◽  
Vol 21 (1) ◽  
Author(s):  
Sunita Janssenswillen ◽  
Kim Roelants ◽  
Sebastien Carpentier ◽  
Hilde de Rooster ◽  
Mieke Metzemaekers ◽  
...  

Abstract Background Chemical communication is an important aspect of the behavioural ecology of a wide range of mammals. In dogs and other carnivores, anal sac glands are thought to convey information to conspecifics by secreting a pallet of small volatile molecules produced by symbiotic bacteria. Because these glands are unique to carnivores, it is unclear how their secretions relate to those of other placental mammals that make use of different tissues and secretions for chemical communication. Here we analyse the anal sac glands of domestic dogs to verify the secretion of proteins and infer their evolutionary relationship to those involved in the chemical communication of non-carnivoran mammals. Results Proteomic analysis of anal sac gland secretions of 17 dogs revealed the consistently abundant presence of three related proteins. Homology searches against online databases indicate that these proteins are evolutionary related to ‘odorant binding proteins’ (OBPs) found in a wide range of mammalian secretions and known to contribute to chemical communication. Screening of the dog’s genome sequence show that the newly discovered OBPs are encoded by a single cluster of three genes in the pseudoautosomal region of the X-chromosome. Comparative genomic screening indicates that the same locus is shared by a wide range of placental mammals and that it originated at least before the radiation of extant placental orders. Phylogenetic analyses suggest a dynamic evolution of gene duplication and loss, resulting in large gene clusters in some placental taxa and recurrent loss of this locus in others. The homology of OBPs in canid anal sac glands and those found in other mammalian secretions implies that these proteins maintained a function in chemical communication throughout mammalian evolutionary history by multiple shifts in expression between secretory tissues involved in signal release and nasal mucosa involved in signal reception. Conclusions Our study elucidates a poorly understood part of the biology of a species that lives in close association with humans. In addition, it shows that the protein repertoire underlying chemical communication in mammals is more evolutionarily stable than the variation of involved glands and tissues would suggest.


Biomolecules ◽  
2021 ◽  
Vol 11 (4) ◽  
pp. 509
Author(s):  
Karen Rihani ◽  
Jean-François Ferveur ◽  
Loïc Briand

The survival of insects depends on their ability to detect molecules present in their environment. Odorant-binding proteins (OBPs) form a family of proteins involved in chemoreception. While OBPs were initially found in olfactory appendages, recently these proteins were discovered in other chemosensory and non-chemosensory organs. OBPs can bind, solubilize and transport hydrophobic stimuli to chemoreceptors across the aqueous sensilla lymph. In addition to this broadly accepted “transporter role”, OBPs can also buffer sudden changes in odorant levels and are involved in hygro-reception. The physiological roles of OBPs expressed in other body tissues, such as mouthparts, pheromone glands, reproductive organs, digestive tract and venom glands, remain to be investigated. This review provides an updated panorama on the varied structural aspects, binding properties, tissue expression and functional roles of insect OBPs.


Heliyon ◽  
2021 ◽  
Vol 7 (3) ◽  
pp. e06427
Author(s):  
Haixia Zhan ◽  
Du Li ◽  
Youssef Dewer ◽  
Changying Niu ◽  
Fengqi Li ◽  
...  

2019 ◽  
Vol 27 (5) ◽  
pp. 1019-1030 ◽  
Author(s):  
Ling Wang ◽  
Ying‐Dong Bi ◽  
Ming Liu ◽  
Wei Li ◽  
Miao Liu ◽  
...  

2010 ◽  
Vol 36 (7) ◽  
pp. 787-794 ◽  
Author(s):  
Zhao Liu ◽  
Diogo M. Vidal ◽  
Zainulabeuddin Syed ◽  
Yuko Ishida ◽  
Walter S. Leal

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