Fusarium graminearum in a Papilloma Virus Infected Friesian Bull in Vom, Nigeria: Case Report

Importation of exotic cattle to improve the yield and productivityof the local 'White Fulani' breed of cattle has been on the rise inNigeria. The problem most farmers faces with the Friesian hasalways been the adaptation to the weather and endemic diseaseconditions in Nigeria. Fungal infections represent an importantcomplication for immunosuppressed animals and are associatedwith high morbidity and mortality (De Pauw and Meunier, 1999).Fusarium is one of the most important fungal genera, whichincludes many species that are pathogenic to plants and responsible for a broad range of diseases while others are highly mycotoxigenic (Viquez et al., ) and some cause opportunistic infections in humans and in farm animals. Fusarium graminearum (Gibberella zeae) is an importantpathogen of commercial crops such as wheat, maize, and rice.Infection with F. graminearum causes yield losses in grains anddegrades their nutritive, physical and chemical qualities, resultingin their being used for animal feed rather than for human consumption (Charmley et al., 1994). A contaminated crop can be salvaged by feeding it to livestock or poultry, but further losses may be incurred due to the negative effects of mycotoxins on animal performance. Potent toxins such as the estrogenic toxin zearalenone (F-2) have been reported by Vesonder and Hesseltine, (1980) but the most common mycotoxins produced byF. graminearum are deoxynivalenol (DON, also known as vomitoxin), 15-acetyldeoxynivalenol, and nivalenol belonging to a group of compounds known as trichothecenes (Homdork et al., 2000; Council for Agricultural Science and Technology, CAST, 2003). These mycotoxins are known to diminish feed consumption in domestic livestock, especially swine (CAST 2003). Because of their apparent tolerance for higher levels of dietary DON, Fusarium-infested grains are often fed to cattle or sheep asopportunity feeds. This may be due to little or insufficient information describing the pathogenesis and the ability of this plant pathogen to survive as they move through the gastrointestinal tract of cattle or on a compromised skin (Kedar and Gemerlyn, 2008)

Identification of Contractile Vacuole Proteins in Trypanosoma cruzi

Contractile vacuole complexes are critical components of cell volume regulation and have been shown to have other functional roles in several free-living protists. However, very little is known about the functions of the contractile vacuole complex of the parasite Trypanosoma cruzi, the etiologic agent of Chagas disease, other than a role in osmoregulation. Identification of the protein composition of these organelles is important for understanding their physiological roles. We applied a combined proteomic and bioinfomatic approach to identify proteins localized to the contractile vacuole. Proteomic analysis of a T. cruzi fraction enriched for contractile vacuoles and analyzed by one-dimensional gel electrophoresis and LC-MS/MS resulted in the addition of 109 newly detected proteins to the group of expressed proteins of epimastigotes. We also identified different peptides that map to at least 39 members of the dispersed gene family 1 (DGF-1) providing evidence that many members of this family are simultaneously expressed in epimastigotes. Of the proteins present in the fraction we selected several homologues with known localizations in contractile vacuoles of other organisms and others that we expected to be present in these vacuoles on the basis of their potential roles. We determined the localization of each by expression as GFP-fusion proteins or with specific antibodies. Six of these putative proteins (Rab11, Rab32, AP180, ATPase subunit B, VAMP1, and phosphate transporter) predominantly localized to the vacuole bladder. TcSNARE2.1, TcSNARE2.2, and calmodulin localized to the spongiome. Calmodulin was also cytosolic. Our results demonstrate the utility of combining subcellular fractionation, proteomic analysis, and bioinformatic approaches for localization of organellar proteins that are difficult to detect with whole cell methodologies. The CV localization of the proteins investigated revealed potential novel roles of these organelles in phosphate metabolism and provided information on the potential participation of adaptor protein complexes in their biogenesis