No abstract

Respiratory diseases are one of the most important health problems in pig herds. The porcine respiratory disease complex (PRDC) is the term used to describe pneumonic diseases caused by multiple infectious agents that provoke weight loss in animals or death. In the PRDC multiple pathogens (bacteria and/or viruses) work in combination to induce this respiratory disease. Within this complex, Actinobacillus pleuropneumoniae, Streptococcus suis, Pasteurella multocida, Bordetella bronchiseptica, Haemophilus parasuis and Mycoplasma hyopneumoniae are the main bacterial pathogens involved in great economic losses to the swine industry. The aim of this work was to estimate the presence of A. pleuropneumoniae, S. suis, P. multocida, B. bronchiseptica, H. parasuis and M. hyopneumoniae in the upper respiratory tract of pigs in representative swine farms in Aguascalientes, Mexico, using PCR technique. The study was performed in 14 swine farms. We obtained a total of 212 nasal swabs. Near 20% of samples were positive for A. pleuropneumoniae (located in the 79% of farms); 17% were positive for S. suis (in 86% of farms), of these, 3% were S. suis serovar 2; 30% were positive for H. parasuis (93% of farms); 23% of the samples to P. multocida (in 79% of farms); and 19% to M. hyopneumoniae (in 64% of farms). B. bronchiseptica was not detected in this study. The results obtained show that bacterial pathogens of PRDC were present in the upper respiratory tract of pigs in all farms studied; therefore, these pathogens are widely disseminated in pig farms of Aguascalientes, Mexico.

Respiratory pathogens are the main health problem in the swine industry worldwide. These pathogens are transmitted by direct contact between animals or by aerosols and however are not well known yet, if the environment works as its reservoir, inoculum and/or dispersion medium. The objective of this study was to determine the presence of respiratory pathogens in environmental samples from swine farms in Aguascalientes, Mexico, through of PCR and RT-PCR techniques. The bacteria Actinobacillus pleuropneumoniae and Pasteurella multocida were found viable in samples from water, food, soil and air. Streptococcus suis was found in a viable state in water samples. Haemophilus parasuis, Porcine Reproductive and Respiratory Syndrome virus and Swine Influenza virus (H1N1 and H3N2) were detected in drinking water samples. Mycoplasma hyopneumoniae and Porcine Circovirus type 2 (PCV2) were not detected in environmental samples. These results suggest that the environment of the farms acts as a reservoir, inoculum and/or vehicle of dispersion for these pathogens except for M. hyopneumoniae and PCV2.

Entamoeba histolytica is an intestinal parasite that causes dysentery and amebic liver abscess. E. histolytica has the capability to invade host tissue by union of virulence factor Gal/GalNAc lectin; this molecule induces an adherence-inhibitory antibody response as well as to protect against amebic liver abscess (ALA). The present work showed the effect of the immunization with PEΔIII-LC3-KDEL3 recombinant protein. In vitro, this candidate vaccine inhibited adherence of E. histolytica trophozoites to HepG2 cell monolayer, avoiding the cytolysis, and in a hamster model, we observed a vaccine-induced protection against the damage to tissue liver and the inhibition of uncontrolled inflammation. PEΔIII-LC3-KDEL3 reduced the expression of TNF-α, IL-1β, and NF-κB in all immunized groups at 4- and 7-day postinfection. The levels of IL-10, FOXP3, and IFN-γ were elevated at 7 days. The immunohistochemistry assay confirmed this result, revealing an elevated quantity of +IFN-γ cells in the liver tissue. ALA formation in hamsters immunized was minimal, and few trophozoites were identified. Hence, immunization with PEΔIII-LC3-KDEL3 herein prevented invasive amebiasis, avoided an acute proinflammatory response, and activated a protective response within a short time. Finally, this recombinant protein induced an increase of serum IgG.

We report for the first time the design and expression of the recombinant E. histolytica LC3 protein fused to PEΔIII and KDEL3, with potential application as an immunogen.