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1.
Am J Trop Med Hyg ; 76(3): 508-15, 2007 Mar.
Artículo en Inglés | MEDLINE | ID: mdl-17360876

RESUMEN

An examination of peridomestic area organization and triatomine collection in an endemic village for Chagas disease (Jalisco State) identified the habitat of Triatoma longipennis (dominant species) and the risk factors of peridomestic infestation. In 100 visited peridomestic areas, 369 structures (permanent, temporary, and natural) were submitted to active manual research of triatomines. Storage shelters had a higher infestation of T. longipennis than piles of brick and tile; baked clay material had higher degrees of infestation than others. The secondary species Triatoma barberi shares a wide range of peridomicilary habitats with T. longipennis. Peridomestic area infestation risks (evaluated with multivariate logistic regression analysis) are number of closed storage shelters, number of brick and tile piles, number of houses per peridomestic areas, and distance of peridomicile from natural environment. Because both species present great adaptability to different artificial habitats, strategies of control must involved improving the overall management of peridomestic areas to prevent stable colonization.


Asunto(s)
Enfermedad de Chagas/transmisión , Insectos Vectores , Triatoma , Animales , Humanos , México , Factores de Riesgo , Población Rural
2.
Am J Trop Med Hyg ; 74(2): 303-5, 2006 Feb.
Artículo en Inglés | MEDLINE | ID: mdl-16474087

RESUMEN

Feeding sources of triatomine vectors (Triatoma longipennis) collected in peridomiciles in Mexico were identified by a heteroduplex assay developed with triatomine blood meals. Trypanosoma cruzi parasites were also characterized in the same blood meal samples by multiplex-polymerase chain reaction assay of mini-exon gene inter-genic regions. The main blood meal source was from rats, but the bugs were able to feed on a wide variety of hosts, and human blood meals were identified. Trypanosoma cruzi was the only flagellate species identified in the blood meals. All populations belong to the T. cruzi I lineage, a result that is consistent with the previously assumed predominance of this lineage in Mexico. This combination of blood meal and T. cruzi lineage identification provides a powerful tool for understanding T. cruzi transmission cycles.


Asunto(s)
Enfermedad de Chagas/transmisión , Insectos Vectores/fisiología , Triatoma/fisiología , Trypanosoma cruzi/clasificación , Animales , Enfermedad de Chagas/parasitología , Conducta Alimentaria , Femenino , Humanos , Insectos Vectores/parasitología , Masculino , México/epidemiología , Reacción en Cadena de la Polimerasa/métodos , Ratas , Triatoma/parasitología
3.
Med Sci (Paris) ; 21(5): 523-9, 2005 May.
Artículo en Francés | MEDLINE | ID: mdl-15885204

RESUMEN

To survive within erythrocytes, Plasmodium parasites have to put into place different membrane and sub-cellular compartments in order to import different nutrients and to export proteins/antigens. Infected cells pose not only a major world health risk by killing two million people per year, but also a very interesting cell biology problem, as within the erythrocyte the parasite resides inside a vacuole called the parasitophorous vacuole and as a consequence, it is separated from the blood stream by three membrane barriers, its own plasma membrane, the parasitophorous vacuole membrane and the erythrocyte plasma membrane. In spite of these three barriers the parasite is capable of secreting antigens and importing nutrients, and to do this, it has developed a complex vesicular system that extends into the red blood cell cytoplasm to the plasma membrane. Understanding how the parasite controls this extensive vesicular traffic has driven research into Plasmodium Rabs, whose potential role is discussed.


Asunto(s)
Eritrocitos/parasitología , Plasmodium/fisiología , Transporte de Proteínas/fisiología , Animales , Eritrocitos/ultraestructura , Humanos , Proteínas de Unión al GTP rab/fisiología
4.
Mol Microbiol ; 51(1): 33-46, 2004 Jan.
Artículo en Inglés | MEDLINE | ID: mdl-14651609

RESUMEN

In search of key enzymes in Plasmodium phospholipid metabolism, we demonstrate the presence of a parasite-encoded phosphatidylserine decarboxylase (PSD) in the membrane fraction of Plasmodium falciparum-infected erythrocytes. PSD cDNA, encoding phosphatidylserine decarboxylase (PfPSD), was cloned by screening a directional cDNA library derived from the trophozoite erythrocytic stage. The corresponding PfPSD gene is located on chromosome 9 of P. falciparum, contains one intron of 938 nucleotides and is transcribed into a 3.7 kb mRNA. PfPSD cDNA encodes a putative protein of 362 amino acids, with a predicted molecular mass of 42.6 kDa, which clearly belongs to the type I PSD family. Only a 35 kDa polypeptide was detected in the parasite using a specific rabbit antiserum. PfPSD has a 314VGSS317 sequence near its carboxyl-terminus that is related to the Escherichia coli, yeast and human LGST motif, which is the site of proenzyme processing. PSD enzyme was expressed in E. coli with a KM of 63 +/- 19 microM and a VMAX of 680 +/- 49 nmol of phosphatidylethanolamine formed h-1 mg-1 protein. Site-directed mutagenesis of the VGSS active site demonstrated that the PfPSD proenzyme was processed into two non-identical subunits (alpha and beta) and revealed the crucial role played by each residue in enzyme processing and activity. Using indirect immunofluorescence, PfPSD labelling was co-localized with an endoplasmic reticulum marker, but not with a mitochondrial vital dye. This P. falciparum PSD is the first type I PSD identified in the endoplasmic reticulum compartment.


Asunto(s)
Carboxiliasas/genética , Plasmodium falciparum/enzimología , Secuencia de Aminoácidos , Animales , Secuencia de Bases , Southern Blotting , Carboxiliasas/química , Clonación Molecular , ADN Complementario , Eritrocitos/parasitología , Escherichia coli/enzimología , Escherichia coli/genética , Biblioteca de Genes , Intrones/genética , Datos de Secuencia Molecular , Sondas de Oligonucleótidos , Plasmodium falciparum/genética , Proteínas Recombinantes/química , Proteínas Recombinantes/metabolismo
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