Working smarter not harder: oxytocin increases domestic dogs’ (Canis familiaris) accuracy, but not attempts, on an object choice task

The neuropeptide oxytocin (OT) has been shown to enhance dogs’ ability to perform an object choice task (OCT) involving the use of human pointing cues, when delivered intranasally. This study aimed at further investigating whether OT enhances task performance by increasing choices made, or by increasing correctness of choices made, and to compare these treatment effects to dog appeasing pheromone (DAP), known to balance emotional activation in dogs. Hence, we compared OCT performance between three groups of dogs: (i) dogs administered OT and a sham collar, (ii) dogs administered a saline placebo and a DAP collar, and (iii) control dogs administered a saline placebo and a sham collar. All three groups consisted of a combination of male and female pet dogs and assistance-dogs-in-training currently living with a volunteer carer. The study also evaluated the effect of intranasal OT and/or DAP on plasma levels of OT, and prolactin; which has previously been linked with anxiety in dogs. The dogs’ emotional state was measured using the Emotional Disorders Evaluation in Dogs (EDED) scale. The owners’/carers’ degree of anxious- and avoidant-style attachment to their dogs was accessed using the Pet Attachment Questionnaire (PAQ). Interesting descriptive data appeared for both treatment groups. Particularly, in OT group, we obtained significant results demonstrating that intranasal OT enhances OCT performance in dogs compared to control, by increasing the percentage of correct choices, but not the number of choices, made. Results also support that the mode of action of intranasal OT is via direct access to the brain and not via the blood, since no elevation of plasma OT (or prolactin) levels were observed after intranasal administration in this study. Similarly, DAP application did not significantly alter OT or prolactin peripheral concentrations. Several differences were observed between fostered and pet dogs, namely: fostered dogs demonstrated higher levels of serum prolactin, made more choices on the OCT compared to pet dogs but were not more likely to be correct, and were fostered by carers with higher avoidant attachment scores than pet dog owners. These findings implicate consideration of potential carer and training consequences for assistance dogs

Inflammation interferes with chemoreception in pigs by altering the neuronal layout of the vomeronasal sensory epithelium

Chemical communication is widely used by animals to exchange information in their environment, through the emission and detection of semiochemicals to maintain social organization and hierarchical rules in groups. The vomeronasal organ (VNO) is one of the main detectors of these messages, and its inflammation has been linked to behavioral changes because it potentially prevents molecule detection and, consequently, the translation of the signal into action. Our previous study highlighted the link between the intensity of vomeronasal sensory epithelium (VNSE) inflammation, probably induced by farm contaminant exposure, and intraspecific aggression in pigs. The aim of this study was to evaluate the cellular and molecular changes that occur during vomeronasalitis in 76 vomeronasal sensorial epithelia from 38 intensive-farmed pigs. Histology was used to evaluate the condition of each VNO and classify inflammation as healthy, weak, moderate, or strong. These data were compared to the thickness of the sensorial epithelium and the number of type 1 vomeronasal receptor cells using anti-Gαi2 protein immunohistochemistry (IHC) and analysis. The presence of odorant-binding proteins (OBPs) in the areas surrounding the VNO was also analyzed by IHC and compared to inflammation intensity since its role as a molecule transporter to sensory neurons has been well-established. Of the 76 samples, 13 (17%) were healthy, 31 (41%) presented with weak inflammation, and 32 (42%) presented with moderate inflammation. No severe inflammation was observed. Epithelial thickness and the number of Gαi2+ cells were inversely correlated with inflammation intensity (Kruskal-Wallis and ANOVA tests, p < 0.0001), while OBP expression in areas around the VNO was increased in inflamed VNO (Kruskal-Wallis test, p = 0.0094), regardless of intensity. This study showed that inflammation was associated with a reduction in the thickness of the sensory epithelium and Gαi2+ cell number, suggesting that this condition can induce different degrees of neuronal loss. This finding could explain how vomeronasalitis may prevent the correct functioning of chemical communication, leading to social conflict with a potential negative impact on welfare, which is one of the most important challenges in pig farming

Pathology and behaviour in feline medicine: investigating the link between vomeronasalitis and aggression

Objectives The aim of the study was to investigate if the feline vomeronasal organ (VNO) can be affected by inflammatory lesions and if these changes are associated with behavioural alterations. Methods VNOs from 20 cats were sampled during necropsy, submitted for routine tissue processing and stained with haematoxylin and eosin for histopathological evaluation. Of the 20 cats, data on the presence of aggressive behaviours towards cats or humans were collected by questionnaire survey at the point of death. Inflammatory lesions were classified depending on the duration of the process as acute or chronic, both in vomeronasal sensory epithelium (VNSE) and in non-sensory epithelium (NSE). Fisher’s exact test was used to compare VNO inflammation with behavioural data. Results The VNSE was inflamed in 11/20 VNOs (55%) while the NSE was inflamed in 13/20 (65%). Overall, the VNO was affected by inflammation in 14/20 (70%) cats, and all the lesions were classified as chronic. Five out of 20 cats (25%) had documented intraspecific aggressive behaviours and 8/20 (40%) had shown aggression towards humans. Fisher’s exact test showed a statistically significant correlation between inflammation of the VNSE and intraspecific aggression (P = 0.038). No statistically correlations were observed between VNSE inflammation and aggression towards humans and between NSE inflammation and aggression towards cats or humans. Conclusions and relevance Our results show, for the first time, the existence of vomeronasalitis in animals and its possible association with intraspecific aggressive behaviours. The inflammatory microenvironment could impair VNSE functionality, causing intraspecific communication alterations, probably through a reduction in chemical communication action and perception. Owing to the pivotal role of the VNO in the social life of cats and other species, this report provides a rationale to further investigate this disease in relation to a variety of behavioural disorders

Vitality in Newborn Farm Animals: Adverse Factors, Physiological Responses, Pharmacological Therapies, and Physical Methods to Increase Neonate Vigor

Publication history: Accepted - 29 April 2023; Published - 4 may 2023.Vitality is the vigor newborn animals exhibit during the first hours of life. It can be assessed by a numerical score, in which variables, such as heart rate, respiratory rate, mucous membranes’ coloration, time the offspring took to stand up, and meconium staining, are monitored. Vitality can be affected by several factors, and therapies are used to increase it. This manuscript aims to review and analyze pharmacological and physical therapies used to increase vitality in newborn farm animals, as well as to understand the factors affecting this vitality, such as hypoxia, depletion of glycogen, birth weight, dystocia, neurodevelopment, hypothermia, and finally, the physiological mechanism to achieve thermostability. It has been concluded that assessing vitality immediately after birth is essential to determine the newborn’s health and identify those that need medical intervention to minimize the deleterious effect of intrapartum asphyxia. Vitality assessment should be conducted by trained personnel and adequate equipment. Evaluating vitality could reduce long-term neonatal morbidity and mortality in domestic animals, even if it is sometimes difficult with the current organization of some farms. This review highlights the importance of increasing the number of stock people during the expected days of parturitions to reduce long-term neonatal morbidity and mortality, and thus, improve the farm’s performance.This research received no external funding

The Major Cat Allergen Fel d 1 Binds Steroid and Fatty Acid Semiochemicals: A Combined In Silico and In Vitro Study

The major cat allergen Fel d 1 is a tetrameric glycoprotein of the secretoglobin superfamily. Structural aspects and allergenic properties of this protein have been investigated, but its physiological function remains unclear. Fel d 1 is assumed to bind lipids and steroids like the mouse androgen-binding protein, which is involved in chemical communication, either as a semiochemical carrier or a semiochemical itself. This study focused on the binding activity of a recombinant model of Fel d 1 (rFel d 1) towards semiochemical analogs, i.e., fatty acids and steroids, using both in silico calculations and fluorescence measurements. In silico analyses were first adopted to model the interactions of potential ligands, which were then tested in binding assays using the fluorescent reporter N-phenyl-1-naphthylamine. Good ligands were fatty acids, such as the lauric, oleic, linoleic, and myristic fatty acids, as well as steroids like androstenone, pregnenolone, and progesterone, that were predicted by in silico molecular models to bind into the central and surface cavities of rFel d 1, respectively. The lowest dissociation constants were shown by lauric acid (2.6 &micro;M) and androstenone (2.4 &micro;M). The specific affinity of rFel d 1 to semiochemicals supports a function of the protein in cat&rsquo;s chemical communication, and highlights a putative role of secretoglobins in protein semiochemistry

Caractérisation du polymorphisme structural et fonctionnel de l'allergène majeur du chatFel D 1

Fel d1, l'allergène majeur du chat, est au 1er rang des allergènes d'animaux domestiques. Cette protéine glycosylée, dont le polymorphisme reste non élucidé, fait partie de la famille des sécrétoglobines. Fel d1 est tétramétrique, composée de 2 sous-unités identiques, elles-mêmes constituées par 2 chaînes peptidiques reliées par 3 ponts disulfures, formant une poche plutôt hydrophobe à l'intérieur. Jusqu'ici sa fonction biologique reste inconnue. Bien que l'éviction de l'animal reste la meilleure thérapie possible pour le patient, cela n'est pas toujours acceptable pour des raisons affectives évidentes, ni véritablement utile car Fel d 1 est une protéine extrêmement résistante, qui persiste longtemps dans l'environnement. ce travail a consisté à caractérisé le polymorphisme structural de Fel d 1 ainsi que son éventuelle interaction avec sa fonction biologique. Premièrement, nous avons démontré l'existence de multiples formes moléculaires de Fel d1, dépendanrtes des zones de production de la protéine mais pas des chats. Nous avons aussi souligné l'importance de ce polymorphisme et son impact sur le dosage et la calibration de Fel d1, indispensables pour la mise au point des préparations utilisées en diagnostic et immunothérapie. Afin de déterminer l'impact de ce polymorphisme sur l'allergénicté de Fel d1, nous avons débuté l'analyse de sérums de patients allergiques au chat. Deuxièmement, afin d'élucider la fonction de Fel d1, nous nous sommes intéressés à l'interaction de ce polymorphisme avec le comportement du chat et mis en évidence l'importance du facteur stress chez l'animal. Des études in silico et de liaison des ligands ont également été testées à ces fins.Allergenic proteins are diverse and among the indoor allergen, we find domestic animals allergens with Fel d 1, the major cat allergen, at 1st rank. This glycosylated protein, of which polymorphism keeps not elucidated, belongs to the secretoglobine family. Fel d1 is tetrametric, composed of 2 identical sub-units, these constituted by 2 polypeptidic chains linked by 3 disulfure bonds, shaping a rather hydrophobic pocket inside. Until now, its function is still unknown. Whereas animal eviction is the best therapy possible for the patient, this is neither always acceptable because of obvious affective reasons, nor really useful since Fel d1 is an extremely resistant protein, persisting long time in the environment. This work has tried to tackle this question from an original point of view, interesting and characterizing the Fel d1 structural polymorphism as well as its probable interaction with its biologic function. First, we demonstrated the existence of multiple Fel d 1molecular forms, dependent of the areas of protein production but not on the cats themselves. We also emphasized this polymorphism importance and impact of Fel d 1 measurement and calibration, essential for the development of the preparations used in diagnostic and immunotherapy. In order to determine if this polymorphism impacts of Fel d 1 allergenicity, we started analysing allergic patients' serums. Secondly, in order to elucidate the function of Fel d 1, we interested in the interaction between this polymorphism and the cat behaviour, and highlighted the importance of the stress factor in the animal. In silico and ligand-binding studies were also tested in this goal.AIX-MARSEILLE1-BU Sci.St Charles (130552104) / SudocSudocFranceF

The ABP dimers-steroids residue interactions were predicted using molecular docking.

<p>The ABP dimers-steroids residue interactions were predicted using molecular docking.</p

The selected and validated homology model of ABP with structural superimposition to Fel d 1.

<p>The selected and validated homology model of ABP with structural superimposition to Fel d 1.</p

Another cat and mouse game: Deciphering the evolution of the SCGB superfamily and exploring the molecular similarity of major cat allergen Fel d 1 and mouse ABP using computational approaches

<div><p>The mammalian secretoglobin (SCGB) superfamily contains functionally diverse members, among which the major cat allergen Fel d 1 and mouse salivary androgen-binding protein (ABP) display similar subunits. We searched for molecular similarities between Fel d 1 and ABP to examine the possibility that they play similar roles. We aimed to i) cluster the evolutionary relationships of the SCGB superfamily; ii) identify divergence patterns, structural overlap, and protein-protein docking between Fel d 1 and ABP dimers; and iii) explore the residual interaction between ABP dimers and steroid binding in chemical communication using computational approaches. We also report that the evolutionary tree of the SCGB superfamily comprises seven unique palm-like clusters, showing the evolutionary pattern and divergence time tree of Fel d 1 with 28 ABP paralogs. Three ABP subunits (A27, BG27, and BG26) share phylogenetic relationships with Fel d 1 chains. The Fel d 1 and ABP subunits show similarities in terms of sequence conservation, identical motifs and binding site clefts. Topologically equivalent positions were visualized through superimposition of ABP A27:BG27 (AB) and ABP A27:BG26 (AG) dimers on a heterodimeric Fel d 1 model. In docking, Fel d 1-ABP dimers exhibit the maximum surface binding ability of AG compared with that of AB dimers and the several polar interactions between ABP dimers with steroids. Hence, cat Fel d 1 is an ABP-like molecule in which monomeric chains 1 and 2 are the equivalent of the ABPA and ABPBG monomers, respectively. These findings suggest that the biological and molecular function of Fel d 1 is similar to that of ABP in chemical communication, possibly via pheromone and/or steroid binding.</p></div

Molecular docking of ABP dimers with steroids.

<p>The 2D-residue map of steroid interaction with ABP dimers; the residues within 4.0 Å of the steroids are shown. (A-C). Residue interactions of progesterone (P), testosterone (T), and dihydrotestosterone (DHT) with the AB dimer. (D-F). Residue interactions of progesterone, testosterone, and dihydrotestosterone with the AG dimer. The protein-ligand interactions are depicted as Van der Waals, conventional hydrogen bonds, and alkyl bonds.</p