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1.
J Parasitol Res ; 2013: 247273, 2013.
Article in English | MEDLINE | ID: mdl-23691274

ABSTRACT

In this study, we show that 40.29% of travellers with a possible history of malaria exposure were positive for anti-Plasmodium spp. antibodies, while these individuals were negative by microscopy. The antibody test described here is useful to elucidate malaria exposure in microscopy-negative travellers from endemic countries.

2.
Exp Parasitol ; 127(1): 18-24, 2011 Jan.
Article in English | MEDLINE | ID: mdl-20599996

ABSTRACT

Trypanosoma brucei is the etiological agent responsible for African trypanosomiasis, an infectious pathology which represents a serious problem of public health and economic losses in Sub-Saharan Africa. As one of the foremost neglected illnesses, few resources have been available for the development of vaccines or new drugs, in spite of the current therapeutical drugs showing little efficiency and high toxicity. Hence, it is obviously important to widen effective therapeutics and preventive strategies against African trypanosomiasis. In this work, we use the DNA vaccine model to evaluate immunisation effectiveness in mice challenged with Trypanosoma brucei brucei. We demonstrate that Balb/C mice immunised intramuscularly with a single dose of a DNA plasmid encoding a bloodstream-stage specific invariant surface glycoprotein (ISG) are partially protected from a lethal dose of T. b. brucei. Interestingly, the surviving animals show high levels of IgG2a anti-trypanosoma antibodies, suggesting that the Th1 response profile seems important for the induced mechanisms of immune protection.


Subject(s)
Protozoan Vaccines , Trypanosoma brucei brucei/immunology , Trypanosomiasis, African/prevention & control , Vaccines, DNA , Animals , Antibodies, Protozoan/blood , Blotting, Western , Disease Models, Animal , Enzyme-Linked Immunosorbent Assay , Female , Immunoglobulin G/blood , Membrane Glycoproteins/genetics , Membrane Glycoproteins/immunology , Mice , Mice, Inbred BALB C , Plasmids , Protozoan Proteins/genetics , Protozoan Proteins/immunology , Trypanosoma brucei brucei/genetics
3.
Protein J ; 29(4): 283-9, 2010 May.
Article in English | MEDLINE | ID: mdl-20496101

ABSTRACT

Metalloproteinases (MMP) belong to the family of cation dependent endopeptidases that degrade matrices at physiological pH and to cleave extracellular matrix proteins. They play an important role in diverse physiological and pathological processes; not only there diverse types of MMP differ in structure and functionally, but also their enzymatic activity is regulated at multiple levels. Trying to shed some light over the processes that govern the pathology of African Trypanosomiasis, the aim of the present study was to examine the proteolytic activity of the crude trypanosome protein extract obtained from the bloodstream forms of Trypanosoma brucei brucei parasites. We hereby report the partial biochemical characterization of a neutral Trypanosoma brucei-metalloproteinase that displays marked proteolytic activities on gelatin and casein, with a molecular mass of approximately 40 kDa, whose activity is strongly dependent of pH and temperature. Furthermore, we show that this activity can be inhibited by classical MMP inhibitors such as EDTA, EGTA, phenantroline, and also by tetracycline and derivatives. This study has a relevant role in the search for new therapeutical targets, for the use of metalloproteinases inhibitors as treatment strategies, or as enhancement to trypanocidal drugs used in the treatment of the disease.


Subject(s)
Metalloproteases/chemistry , Trypanosoma brucei brucei/enzymology , Animals , Chromatography, Ion Exchange , Enzyme Precursors/metabolism , Hydrogen-Ion Concentration , Metalloproteases/isolation & purification , Metalloproteases/metabolism , Mice , Mice, Inbred BALB C , Spores, Protozoan/enzymology , Temperature
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