Abstract

Pheromones are odoriferous volatile chemical cues produced by animals for communication among conspecifics so as to regulate their social behaviors. In general, the odor compounds are recognized by receptors in the nasal cavity. Odorant-binding protein (OBP), a lipocalin family protein, mediates the air-borne odor cues to nasal receptors through nasal mucus. The presence of OBP in several mammalian species is well documented but to-date there is no report of a nasal OBP in buffalo. Hence, the present study was undertaken to investigate if OBP is present in buffalo nasal mucus. Uni- and two-dimensional gel electrophoresis of the nasal mucus suggested the presence of OBP, which was confirmed using mass spectrometry. In silico homology model of the OBP was generated and its structural similarity with other mammalian OBPs was assessed. Finally, molecular-docking and -dynamics simulations analysis revealed the efficiency of buffalo nasal OBP (bunOBP) to bind with buffalo pheromones as well as other reported chemical cues. Taken together, the occurrence of nasal OBP in buffalo and its putative role in odor binding are reported for the first time. The potential association of this protein with estrus-specific volatiles could be taken to advantage for non-invasive detection of estrus in buffaloes.

Highlights

  • Pheromones are odoriferous volatile chemical cues produced by animals for communication among conspecifics so as to regulate their social behaviors

  • Three peptides matched bovine Odorant-binding protein (OBP) and the same de novo sequences were plotted (Fig. 2A–C), and the buffalo nasal OBP protein sequence was employed to homology modeling (Fig. 3A)

  • The odorant/chemical cues are volatiles that are small molecules, produced by specific glands and released in minute quantities. They are transported/ discharged in a form bound to specific proteins called pheromone-binding proteins. When these odor molecules are perceived they invariably bind to specific OBPs and in this form they are presented to the specific receptors to elicit the appropriate response

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Summary

Introduction

Pheromones are odoriferous volatile chemical cues produced by animals for communication among conspecifics so as to regulate their social behaviors. Odorant binding proteins (OBP), a subclass of soluble proteins called outlier lipocalins, has been reported as a major shuttle for odor perception, olfactory stimulus and chemical communication, especially in insects and mammals. Many isoforms of OBP are known which have been isolated, purified and characterized from the nasal mucus of several mammals such as bovine, porcine, rabbit, rodents, etc.[1,2,3,4,5,6] These are 19–23 kDa acidic proteins, which are produced in sero-mucus glands of the respiratory and olfactory epithelia. Certain OBPs are involved in aspects of pheromone/odor communication in mammalian species through body fluids[8]. Such protein are MUP (Major Urinary Proteins) in mouse[9], urinary and/or preputial gland www.nature.com/scientificreports/. A similar structure has been previously reported, adopting X-ray crystallography, for human retinol-binding protein[23] and rodent urinary protein[10]

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