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1.
Mem. Inst. Oswaldo Cruz ; 105(4): 492-495, July 2010. tab, ilus
Article in English | LILACS | ID: lil-554819

ABSTRACT

This paper evaluates the alterations in the glycogen content of tissues (digestive gland and cephalopedal mass) and glucose in the haemolymph of Biomphalaria glabrata BH strain infected with Schistosoma mansoni BH strain and exposed to the latex of Euphorbia splendens var. hislopii. A reduction in the glycogen deposits was observed in infected snails exposed and not exposed to latex. However, the exposure to latex caused a greater depletion of the glycogen levels in both sites analysed, especially from the third week onward. The utilisation of latex as a molluscicide to control the population of infected B. glabrata selectively is proposed.


Subject(s)
Animals , Biomphalaria , Carbohydrate Metabolism , Euphorbia , Glucose , Hemolymph , Latex , Biomphalaria , Schistosomiasis mansoni , Schistosomiasis mansoni/transmission
2.
Mem. Inst. Oswaldo Cruz ; 102(6): 671-674, Sept. 2007. tab
Article in English | LILACS | ID: lil-463470

ABSTRACT

The reproductive activity of Biomphalaria glabrata exposed to Euphorbia splendens var. hislopii latex was evaluated. Parameters related to fecundity and fertility were observed. The snails were exposed to the LD50 (1 mg/l) of crude latex. At the first week post exposure (p.e.), the egg laying was reduced. After the fourth week p.e., an increase of the number of eggs/snail occurred. The results showed a marked reduction in the hatching of the snails, revealing an interference of latex exposure with the reproductive process of B. glabrata of E. splendens var. hislopii. The LD50 of the latex may be used as an alternative method to control the size of the populations of B. glabrata in field.


Subject(s)
Animals , Female , Male , Biomphalaria/drug effects , Euphorbia/chemistry , Latex/pharmacology , Biomphalaria/physiology , Latex/isolation & purification , Plant Extracts/pharmacology , Reproduction/drug effects , Reproduction/physiology
3.
Mem. Inst. Oswaldo Cruz ; 97(suppl.1): 115-116, Oct. 2002. ilus
Article in English | LILACS | ID: lil-325028

ABSTRACT

Sm14 was the first fatty acid-binding protein homologue identified in helminths. Thereafter, members of the same family were identified in several helminth species, with high aminoacid sequence homology between them. In addition, immune crossprotection was also reported against Fasciola hepatica infection, in animals previously immunized with the Schistosoma mansoni vaccine candidate, r-Sm14. In the present study, data on preliminary sodium dodecyl sulphate-polyacrylamide gel electrophoresis and Western blotting analysis of nine different helminth extracts focusing the identification of Sm14 related proteins, is reported. Out of these, three extracts - Ascaris suum (males and females), Echinostoma paraensei, and Taenia saginata - presented components that comigrated with Sm14 in SDS-PAGE, and that were recognized by anti-rSm14 policlonal serum, in Western blotting tests


Subject(s)
Animals , Male , Female , Blotting, Western , Electrophoresis, Polyacrylamide Gel , Helminth Proteins , Schistosoma mansoni , Schistosomiasis mansoni , Helminth Proteins
4.
Mem. Inst. Oswaldo Cruz ; 96(suppl): 79-83, Sept. 2001. ilus
Article in English | LILACS | ID: lil-295890

ABSTRACT

In previous studies it was shown that the recombinant molecule, r-Sm14, induces high levels of protection against Schistosoma mansoni infection in two outbred animal models and immune crossprotection against infection by Fasciola hepatica in Swiss outbred mice. r-Sm14 was derived from a living worm extract, called SE, and is being developed as the molecular basis of an anti-helminth bivalent vaccine against the two parasites, for medical and veterinary application. Present data refer to SDS-PAGE and Western Blotting analysis of four different preparations of S. mansoni adult worms focusing Sm14 identification. The extracts correspond to the initial fraction of the SE extraction process, containing products released by living worms (SEi); SE2, reextraction of adult worms in PBS; and SE of separated male and female adult worms. In all extracts it was possible to detect the component of 14 kDa, that was recognized by specific anti-rSm14 antibody raised in rabbits


Subject(s)
Animals , Male , Female , Mice , Helminth Proteins/analysis , Schistosoma mansoni/chemistry , Schistosomiasis mansoni/immunology , Antibodies, Helminth/immunology , Blotting, Western , Carrier Proteins , Electrophoresis, Polyacrylamide Gel , Fatty Acids , Helminth Proteins/immunology , Schistosoma mansoni/immunology , Vaccines/immunology
5.
Mem. Inst. Oswaldo Cruz ; 96(suppl): 131-135, Sept. 2001. ilus, tab
Article in English | LILACS, SES-SP | ID: lil-295892

ABSTRACT

Previous studies carried out with Sm14 in experimental vaccination against Schistosoma mansoni or Fasciola hepatica infections were performed with recombinant Sm14 (rSm14) produced in Escherichia coli by the pGEMEX system (Promega). The rSm14 was expressed as a 40 kDa fusion protein with the major bacteriophage T7 capsid protein. Vaccination experiments with this rSm14 in animal models resulted in consistent high protective activity against S. mansoni cercariae challenge and enabled rSm14 to be included among the vaccine antigens endorsed by the World Health Organization for phase I/II clinical trials. Since the preparation of pGEMEX based rSm14 is time consuming and results in low yield for large scale production, we have tested other E. coli expression systems which would be more suitable for scale up and downstream processing. We expressed two different 6XHis-tagged Sm14 fusion proteins in a T7 promoter based plasmids. The 6XHis-tag fusions allowed rapid purification of the recombinant proteins through a Ni+2-charged resin. The resulted recombinant 18 and 16 kDa proteins were recognized by anti-Sm14 antibodies and also by antiserum against adult S. mansoni soluble secreted/excreted proteins in Western-Blot. Both proteins were also protective against S. mansoni cercariae infection to the same extent as the rSm14 expressed by the pGEMEX system


Subject(s)
Animals , Female , Mice , Schistosoma mansoni/immunology , Recombinant Proteins , Antibodies, Helminth/physiology , Helminth Proteins/physiology , Plasmids , Recombinant Proteins/isolation & purification , Carrier Proteins , Helminth Proteins/isolation & purification , Blotting, Western , Amino Acid Sequence , Vaccination , DNA, Complementary , Models, Animal , Electrophoresis, Polyacrylamide Gel , Escherichia coli , Fatty Acids
6.
Mem. Inst. Oswaldo Cruz ; 90(2): 255-256, Mar.-Apr. 1995.
Article in English | LILACS | ID: lil-319898

ABSTRACT

Molecular cloning of components of protective antigenic preparations have suggested that related parasite fatty acid binding proteins could form the basis of the well documented protective, immune cross reactivity between the parasitic trematode worms Fasciola hepatica and Schistosoma mansoni. We have now confirmed the cross protective potential of parasite fatty acid binding proteins and suggest that it may be possible to produce a single vaccine that would be effective against at least two parasites, F. hepatica and S. mansoni of veterinary and human importance respectively.


Subject(s)
Humans , Animals , Mice , Rabbits , Antigens, Helminth/immunology , Fasciola hepatica , Fascioliasis/prevention & control , Schistosoma mansoni , Schistosomiasis mansoni , Vaccination , Vaccines, Synthetic/immunology , Fatty Acids/immunology , /immunology , Carrier Proteins/immunology
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