ß-Caryophyllene-Loaded Microemulsion-Based Topical Hydrogel: A Promising Carrier to Enhance the Analgesic and Anti-Inflammatory Outcomes.

Musculoskeletal pain and inflammation can vary from localised pain like pain in the shoulders and neck to widespread pain like fibromyalgia, and as per estimates, around 90% of humans have experienced such pain. Oral non-steroidal anti-inflammatory drugs (NSAIDs) are frequently prescribed for such conditions but are associated with concerns like gastric irritation and bleeding. In the present study, a microemulsion-based gel comprising ß-caryophyllene, isopropyl myristate, Tween 80, and normal saline was prepared as a topical option for managing topical pain and inflammation. The globules of the microemulsion were below 100 nm with a zetapotential of around -10 mV. The drug entrapment was >87% with a drug loading of >23%. The permeation studies established better skin permeation (20.11 ± 0.96 µg cm-2 h-1) and retention of the drug (4.96 ± 0.02%) from the developed system vis-à-vis the conventional product (9.73 ± 0.35 µg cm-2 h-1; 1.03 ± 0.01%). The dermatokinetic studies established the better pharmacokinetic profile of the bioactive in the epidermis and dermis layers of the skin. The anti-inflammatory potential in carrageenan-induced rat paw oedema was more pronounced than the conventional product (~91% vis-à-vis ~77%), indicating a better pharmacodynamic outcome from the developed system. The nanotechnology-based natural bioactive product with improved efficacy and drug loading can provide a better alternative for the management of musculoskeletal pain.

Molecular characterization and antigenic properties of a novel Babesia gibsoni glutamic acid-rich protein (BgGARP).

Identification and molecular characterization of Babesia gibsoni proteins with potential antigenic properties are crucial for the development and validation of the serodiagnostic method. In this study, we isolated a cDNA clone encoding a novel B. gibsoni 76-kDa protein by immunoscreening of the parasite cDNA library. Computer analysis revealed that the protein presents a glutamic acid-rich region in the C-terminal. Therefore, the protein was designated as B. gibsoni glutamic acid-rich protein (BgGARP). A BLASTp analysis of a translated BgGARP polypeptide demonstrated that the peptide shared a significant homology with a 200-kDa protein of Babesia bigemina and Babesia bovis. A truncated BgGARP cDNA (BgGARPt) encoding a predicted 13-kDa peptide was expressed in Escherichia coli (E. coli), and mouse antisera against the recombinant protein were used to characterize a corresponding native protein. The antiserum against recombinant BgGARPt (rBgGARPt) recognized a 140-kDa protein in the lysate of infected erythrocytes, which was detectable in the cytoplasm of the parasites by confocal microscopic observation. In addition, the specificity and sensitivity of enzyme-linked immunosorbent assay (ELISA) with rBgGARPt were evaluated using B. gibsoni-infected dog sera and specific pathogen-free (SPF) dog sera. Moreover, 107 serum samples from dogs clinically diagnosed with babesiosis were examined using ELISA with rBgGARPt. The results showed that 86 (80.4%) samples were positive by rBgGARPt-ELISA, which was comparable to IFAT and PCR as reference test. Taken together, these results demonstrate that BgGARP is a suitable serodiagnostic antigen for detecting antibodies against B. gibsoni in dogs.

Expression and immunohistochemical localization of the neonatal Fc receptor (FcRn) in the mammary glands of the Egyptian water buffalo.

Although a marginal placental transfer of maternal immunoglobulin (Ig) has been demonstrated in buffalo, the colostrum still provides the main source of immune components and nutrients to neonate buffalo calves. The neonatal Fc receptor (FcRn) transports maternal Ig across the gut wall and is involved in the transport of IgG in the mammary gland. In this study we used RT-PCR to examine the gene expression of FcRn in the mammary gland during several physiological states of the Egyptian water buffalo. The buffalo FcRn showed a high sequence homology to that of other mammalian species and especially the cow. Immunohistochemistry demonstrated positive immunolabelling of FcRn in the epithelial cells of the acini and ducts of the examined mammary gland tissue. Remarkable differences in both the cellular localization and in the intensity of FcRn immunopositivity were observed depending on the functional state of the mammary gland tissues. In late pregnancy, the FcRn immunolabelling was homogeneously distributed in the cytoplasm of the epithelial cells. In recently parturient animals, positive FcRn immunolabelling was mainly located at the luminal surface and apical cytoplasm of the mammary gland epithelium, while in dry and lactating animals, the FcRn immunolabelling was in the apical cytoplasm of the cells. The strongest FcRn immunolabelling was observed in late pregnancy and in recently parturient animals. In conclusion, the present data support the notion that FcRn might be involved in the transfer of maternal immunoglobulins and in the local defense mechanism of the mammary gland.