The experiment was set to determine the effects of long-term (55-day) use of three commercial prebiotics including Saccharomyces cerevisiae–derived β-glucans and one including inulin on juvenile vimba (Vimba vimba) reared intensively under controlled conditions.

Influenza viruses are potent pathologic agents that cause lethal respiratory disease worldwide. The nonstructural protein (NS1) protein of the influenza virus plays a vital role in the virus replication by the evasion of host innate immune system. NS1 protein was found to be conserved functionally in both Influenza A and B viruses. Recent studies revealed that the NS 1 protein of influenza A and B viruses binds to TRIM 25 ubiquitin ligase that is needed for the post-translation modification of the RIG-I and thereby prevents the interferon signaling cascade. Protacs are the bifunctional molecules that bind to the target protein and an ubiquitin ligase, enabling ubiquitination and destruction of the target protein through the Ubiquitin-Proteasome system. In this minireview, based on earlier studies we propose novel molecules designed to target NS1 protein in order to elicit an interferon response and NEDD4 ligase to prevent the degradation of interferon (IFN)-induced transmembrane protein 3 (IFITM3).

C-reactive protein (CRP) is an acute phase protein, which is used to evaluate and monitor the response of the innate immune system to a variety of inflammatory processes in the dog. The purpose of this study was to analytically validate a point-of-care assay (IDEXX Catalyst CRP Test) and an immunoturbidimetric assay (Gentian Canine CRP Immunoassay) for the measurement of serum CRP concentrations in dogs. These 2 assays (Catalyst, Gentian) were compared to a previously validated enzyme-linked immunosorbent assay (Tridelta Development EIA Canine CRP Assay). Linearity, precision, reproducibility, and accuracy were assessed using leftover serum samples. Agreement between assays was assessed using leftover serum samples and serum from clinically healthy dogs. Observed to expected ratios (O/E) for dilutional parallelism were 83.9 to 163.1% and 108.3 to 160.6% for the Catalyst and the Gentian assays, respectively. Coefficients of variation for intra-assay variability ranged from 6.4 to 9.5% for the Catalyst assay and 1.5 to 2.6% for the Gentian assay. Coefficients of variation for inter-assay variability ranged from 3.8 to 18.2% for the Catalyst assay and 4.5 to 5.8% for the Gentian assay. The mean O/E for recovery were 97.9% and 98.5% for the Catalyst and Gentian assays, respectively. Correlations between assays were as follows: Catalyst and Tridelta (R 2 = 0.76), Gentian and Tridelta (R 2 = 0.79), and Catalyst and Gentian (R (2) = 0.98). The Catalyst and Gentian assays are both acceptable for measuring CRP in dog serum, but their results are not directly comparable with the Tridelta assay.

Objective: The present study aimed to produce and analyze antibody against a synthetic amino acid sequence fragment of PIP-HP of Bali cattle saliva. Materials and Methods: The synthetic amino acid sequence of the PIP-HP (VIRELGICPDDWAVIPIKANRF) was developed, conjugated to bovine serum albumin and was used to immunize Indonesian local rabbits. Positive sera that specific against the PIP-HP were pooled and purified sequentially by implying ammonium sulfate precipitation and protein A affinity methods. Purified antibody was then employed to analyze of PIP-HP in the ruminants saliva by means of westernblot assays. Results: A polyclonal antibody specific to asynthetic amino acid sequence fragment of PIP-HP of Bali cattle saliva was successfully produced. Our results show that the antibody potentially to be used to develop an immuno-diagnostic kit. Furthermore, the antibody was also able to inhibit the growth of both Escherichia coli and Staphylococcus aureus cultures significantly (P [J Adv Vet Anim Res 2018; 5(2.000): 182-187]

Objective: Previously, we have shown that predicted zymogen granule protein 16 homolog B (P-G3MZ19) existed in Bali cattle (Bos javanicus) saliva. It was suggested that P-G3MZ19 is a mem¬ber of the mannose-binding lectin family that plays an essential role in innate immunity. In the present study, we aimed to analyze the structure and ligand-binding of P-3MZ19 in Bali cattle saliva. Materials and Methods: Saliva of four adult healthy Bali cattle was collected, lyophilized, and subjected to two-dimensional (2-D) gel electrophoresis. The target spot of around 17 kDa related to P-G3MZ19 was excised for matrix-assisted laser desorption ionization time-of-flight mass spec¬trometer/time-of-flight mass spectrometer mass spectrometry analysis and sequencing. The structure and the ligand-binding of P-3MZ19 were analyzed using bioinformatics software pro¬grams published elsewhere. Results: Based on Iterative Threading ASSEmbly Refinement the 3D model of P-G3MZ19 was suggested to have similarities to exo-alpha-sialidase (EC 3.2.1.18); while its ligand-binding sites consisted of seven residues, i.e., 25aa-26aa (Gly-Gly), 95aa (Phe), 138aa (Tyr), 140aa (Leu), 141aa (Gly), and 143aa (Thr). Conclusion: The structure of P-G3MZ19 of Bali cattle saliva and its ligand-binding sites have been successfully determined by using bioinformatics techniques. The biological and immunological roles of the peptide are currently under investigation based on P-G3MZ19 synthetic peptides. [J Adv Vet Anim Res 2021; 8(2.000): 224-229]