Author Correction: Buffalo nasal odorant-binding protein (bunOBP) and its structural evaluation with putative pheromones

Muthukumar, Subramanian; Rajesh, Durairaj; Selvam, Ramu Muthu; Saibaba, Ganesan; Suvaithenamudhan, Suvaiyarasan; Akbarsha, Mohammad Abdulkader; Gulyás, Balázs; Archunan, ‪Govindaraju

doi:10.1038/s41598-018-29894-6

Cited by 2 publications

(7 citation statements)

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“…In our study, we conducted an RMSD analysis to gauge the conformational flexibility of these complexes, which revealed interesting findings . The RMSD of six ligands with buffalo nasal OBP (bunOBP) attained equilibrium at around three ns and remained relatively constant throughout the simulation, suggesting that bunOBP binds to the odors (ligands) and facilitates sexual communication in buffalo . However, it is worth noting that we observed highly fluctuating RMSD values for some of the protein–ligand complexes during the simulation.…”

Section: Discussionmentioning

confidence: 86%

“…However, other quinoline complexes (pheromaxein–quinoline, SAL–quinoline, and VEGP–quinoline) showed higher energy values, suggesting that quinoline may be less effective in binding with pheromaxein, SAL, and VEGP compared to the steroidal ligands. In other studies, ligand-binding assays have revealed high-affinity interactions, such as the binding of oleic acid and p-cresol with buffalo nasal OBPs and lauric acid with Fel d1. , The docking score of p-cresol with β-lactoglobulin and OBP revealed the high-affinity binding of p-cresol with OBP . It is not surprising that p-cresol is an estrus-specific pheromone identified in many body fluids. − Docking of mice pheromones (farnesol and 2-isobutyl-3-methoxypyranize) with estrus urinary lipocalin protein revealed high binding energy .…”

Section: Discussionmentioning

confidence: 99%

“…Muthukumar et al. attested OBP in the nasal mucus of buffalo and highlighted their role in the binding of pheromones . Both boars and sows also have OBPs, salivary lipocalin (SAL), and von Ebner’s gland protein (VEGP) in their nasal mucosa and VNO .…”

Section: Introductionmentioning

confidence: 99%

“…attested OBP in the nasal mucus of buffalo and highlighted their role in the binding of pheromones. 11 Both boars and sows also have OBPs, salivary lipocalin (SAL), and von Ebner’s gland protein (VEGP) in their nasal mucosa and VNO. 12 Pheromaxein identified in the submandibular glands of boars binds to the steroid molecules.…”

Section: Introductionmentioning

confidence: 99%

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Mechanistic Insights into the Binding of Boar Salivary Pheromones and Putative Molecule with Receptor Proteins: A Comparative Computational Approach

Sankarganesh,

Balasundaram,

Doss C

et al. 2024

ACS Omega

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Precise estrus detection in sows is pivotal in increasing the productivity within the pork industry. Sows in estrus exhibit exclusive behaviors when exposed to either a live boar or the steroid pheromones androstenone and androstenol. Recently, a study employing solid-phase microextraction-gas chromatography−mass spectrometry has identified a novel salivary molecule in boars, known as quinoline. This finding has intriguing implications as a synthetic mixture of androstenone, androstenol, and quinoline induces estrus behaviors in sows. Nevertheless, the precise pheromonal characteristics of quinoline remain elusive. In this study, we validate and compare the binding efficiency of androstenone, androstenol, and quinoline with porcine olfactory receptor proteins (odorant-binding protein [OBP], pheromaxein, salivary lipocalin [SAL], and Von Ebner's gland protein [VEGP]) using molecular docking and molecular dynamics simulations. All protein−ligand complexes demonstrated stability, as evidenced by the root-mean-square deviation (RMSD), root-mean-square fluctuation (RMSF), radius of gyration (R g ), solvent-accessible surface area (SASA), and hydrogen-bond (H-bond) plots. Furthermore, quinoline displayed higher binding efficiency with OBP, measured at −85.456 ± 8.268 kJ/mol, compared to androstenone and androstenol, as determined by molecular mechanics�Poisson−Boltzmann surface area (MM-PBSA) calculations. Conversely, quinoline exhibited a lower binding efficacy when interacting with SAL, pheromaxein, and VEGP compared to androstenone and androstenol. These findings, in part, suggest the binding possibility of quinoline with carrier proteins and warrant further investigation to support the role of quinoline in porcine chemical communication.

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Section: Discussionmentioning

confidence: 86%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Mechanistic Insights into the Binding of Boar Salivary Pheromones and Putative Molecule with Receptor Proteins: A Comparative Computational Approach

Sankarganesh,

Balasundaram,

Doss C

et al. 2024

ACS Omega

Self Cite

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“…Pheromone-binding OBPs in body fluids and odor-binding OBP in nasal mucus are identical in structure, although they may have different chemical and physiological properties. They can be found in the epithelium but at low concentrations [11].…”

Section: Discussionmentioning

confidence: 99%

Clinical Characteristics and Sensitization Profile of Patients Allergic to Cow Epithelium

Guzmán

Orjales

Paris

et al. 2023

Int Arch Allergy Immunol

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Introduction: Cow epithelium allergy (CEA) has been described in workers highly exposed to cattle, such as farmers and veterinarians, being a health problem in this population since it is their main livelihood. This study aimed to characterize the main clinical manifestations and define the sensitization profile of the cow epithelium-allergic population treated in our health area. Methods: This is a retrospective study including a total of 34 patients with a clinical diagnosis of CEA, confirmed by skin tests, bovine epithelium-specific IgE levels and allergen-specific conjunctival challenge test in some cases. They were distributed by age, sex, profession, clinical symptoms, specific IgE levels to other mammalian epithelia, pollens, mites, and foods. Immunoblotting was performed with extracts from cow dander, cow body fluids (urine and saliva), bull urine, and 17 sera from immunotherapy-untreated CEA patients. Results: The mean age of the patients was 44 years, with a higher incidence in cattle farmers. Rhinoconjunctivitis occurred in 100% of cases, with 35% having monosensitization to cow epithelium. Sera from most patients detected a 20-kDa IgE-binding band in cow dander, cow saliva, cow urine, and bull urine, corresponding to the major allergen Bos d 2 (bovine lipocalin). In 70% of the patients, a 25-kDa band was detected in cow and bull urine extracts, whose identification by mass spectrometry and investigation with protein databases led to the identification of a Bos taurus lipocalin (UniProt protein ID: A0A3Q1LGU7_BOVIN). Conclusion: CEA should be considered in patients exposed to cattle and as a cause of occupational disease. The IgE immunodetection revealed sensitization to a protein present in cow and bull urine (odorant-binding protein) not previously described.

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Author Correction: Buffalo nasal odorant-binding protein (bunOBP) and its structural evaluation with putative pheromones

Abstract: In addition, in the Supplementary file 'Figure S1 S2 S3 Table S1 S2' , the Present Addresses for the authors Ramu Muthu Selvam and Mohammad Abdulkader Akbarsha were omitted.

Cited by 2 publications

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Mechanistic Insights into the Binding of Boar Salivary Pheromones and Putative Molecule with Receptor Proteins: A Comparative Computational Approach

Mechanistic Insights into the Binding of Boar Salivary Pheromones and Putative Molecule with Receptor Proteins: A Comparative Computational Approach

Clinical Characteristics and Sensitization Profile of Patients Allergic to Cow Epithelium

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