Search

The last few decades have seen an increase in intensive buffalo farms worldwide. Such industrialized activity entails human and animal potential health-related hazards as well as for the environment. Given the breadth of the issue, in this study we focused on gathering microbiological air sampling in the Southern Italian buffalo farms in order to obtain further information on airborne microbial flora. In details, we evaluated the bio-aerosol concentration of cultivable bacteria and fungi in ten different buffalo farms. There are evidences showing that exposure to organic dust may exacerbate asthma, just as it may cause mucous membrane irritation and chronic bronchitis. Likewise, studies show that inhaling noninfectious microorganisms and their components may cause inflammation of the respiratory tract. As a result, this is a significant health hazard to these farms’ workers as well as to rural residents living closely to them.

Bacterial derived lipoproteins constitute potent macrophage activators in vivo and are effective stimuli, enhancing the immune response especially with respect to low or non-immunogenic compounds. In the present study we have prepared branched lipopeptide constructs in which different (B- and T-cell) epitopes of Herpes simplex virus type 1, derived from glycoproteins B (gB) and D (gD), are linked to a synthetic lipid core. The ability of the lipid core peptide (LCP) constructs (LCP-gB and LCP-gD) to induce cytokine expression and activate the mitogen-activated protein kinase cascade has been evaluated and compared with the behaviour of the isolated epitopes and the lipid core. In this respect, the use of LCP technology coupled with the use of three different gB or gD peptide epitopes in the same branched constructs could represent an interesting approach in order to obtain efficient delivery systems in the development of a synthetic multiepitopic vaccine for the prevention of viral infections.

Objectives: The deciphering of intracellular signaling pathways that are activated by the interaction between viral fusion peptides and cellular membranes are important for the understanding of both viral replication strategies and host defense mechanisms. Methods: Fusion peptides of several enveloped viruses belonging to different virus families were prepared by standard 9-fluorenylmethoxycarbonyl polyamine solid-phase synthesis and used to stimulate U937 cells in vitro to analyze the phosphorylation patterns of the signaling pathways (PKC, Src, Akt, and MAPK pathways). Immunoprecipitation and Western blotting were carried out by using phosphospecific antibodies. All samples were also assayed for the presence of IL-10 and IFN-β by ELISA and activation of nuclear factors (AP-1 and NF-ĸB). Results: We have demonstrated that hydrophobic domains of fusion proteins are able to induce several transduction pathways that lead to cytokine (IFN-β and IL-10) production, an event that appears to be dependent on early activation of AP-1 and NF-ĸB. Conclusions: The results obtained on the signaling activity of fusion peptides from different viruses enabled us to shed some light on the complex mechanism of viral entry and more precisely we focused on the exact signaling event induced by hydrophobic domains characteristic of fusion peptides interacting with the cell membrane.