Entamoeba histolytica Schaudinn, 1903 and Entamoeba dispar Brumpt, 1925: Differences in their Cell Surfaces and in the Bacteria-containing Vacuoles

2002 ◽  
Vol 49 (3) ◽  
pp. 209-219 ◽  
Author(s):  
PAULO F. P. PIMENTA ◽  
LOUIS S. DIAMOND ◽  
DAVID MIRELMAN
2009 ◽  
Vol 25 (1) ◽  
pp. 151-159 ◽  
Author(s):  
Zulbey Rivero ◽  
Ángela Bracho ◽  
Marinella Calchi ◽  
Iris Díaz ◽  
Ellen Acurero ◽  
...  

La identificación diferencial de Entamoeba histolytica y Entamoeba dispar es esencial para un tratamiento adecuado del paciente y con fines epidemiológicos. Para determinar la prevalencia de E. histolytica y E. dispar se estandarizó y aplicó un ensayo de PCR, utilizando oligonucleótidos específicos para cada especie. 204 muestras de heces de individuos de la comunidad de Santa Rosa de Agua (Municipio Maracaibo, Estado Zulia, Venezuela), fueron analizadas a través del examen directo con SSF (0,85%) y lugol, concentrado de formol-éter y PCR. Al examen microscópico, 42 individuos (20,58%) presentaron formas evolutivas del complejo E. histolytica/E. dispar; mientras que la técnica de PCR evidenció un total de 47 casos positivos a estas amibas; de los cuales 22 eran portadores de E. histolytica (10,78%), 16 (7,84%) de E. dispar y 9 (4,41%) presentaron infección mixta. No hubo diferencia significativa al relacionar las variables sexo y presencia de E. histolytica y/o E. dispar, ni con los grupos etarios. No existieron casos de estas amibas, en los menores de 2 años. La frecuencia observada de E. histolytica (31/204), demuestra el carácter endémico de la amibiasis en esta comunidad.


Infection ◽  
2011 ◽  
Vol 39 (6) ◽  
pp. 527-535 ◽  
Author(s):  
K.-H. Herbinger ◽  
E. Fleischmann ◽  
C. Weber ◽  
P. Perona ◽  
T. Löscher ◽  
...  

2012 ◽  
Vol 140 (4) ◽  
pp. 476-483 ◽  
Author(s):  
Omaira Y López ◽  
Myriam C López ◽  
Vladimir Corredor ◽  
M. Clara Echeverri ◽  
Análida E Pinilla

Biomédica ◽  
2001 ◽  
Vol 21 (2) ◽  
pp. 167 ◽  
Author(s):  
Claudia E. Guzmán ◽  
Myriam C. López ◽  
Patricia Reyes ◽  
Jorge E. Gómez ◽  
Augusto Corredor ◽  
...  

2000 ◽  
Vol 31 (4) ◽  
pp. S30-S31 ◽  
Author(s):  
Héctor Shibayama-Hernández ◽  
Jesús Pedroza-Gómez ◽  
Bertha Rivero-Baños ◽  
Mineko Shibayama ◽  
Jesús Serrano-Luna ◽  
...  

1997 ◽  
Vol 186 (9) ◽  
pp. 1557-1565 ◽  
Author(s):  
Alexandra Marinets ◽  
Tonghai Zhang ◽  
Nancy Guillén ◽  
Pierre Gounon ◽  
Barbara Bohle ◽  
...  

A panel of monoclonal antibodies was raised from mice immunized with a membrane preparation from Entamoeba histolytica, the pathogenic species causing invasive amebiasis in humans. Antibody EH5 gave a polydisperse band in immunoblots from membrane preparations from different E. histolytica strains, and a much weaker signal from two strains of the nonpathogenic species Entamoeba dispar. Although the exact chemical structure of the EH5 antigen is not yet known, the ability of the antigen to be metabolically radiolabeled with [32P]phosphate or [3H]glucose, its sensitivity to digestion by mild acid and phosphatidylinositol-specific phospholipase C, and its specific extraction from E. histolytica trophozoites by a method used to prepare lipophosphoglycans from Leishmania showed that it could be classified as an amebal lipophosphoglycan. Confocal immunofluorescence and immunogold labeling of trophozoites localized the antigen on the outer face of the plasma membrane and on the inner face of internal vesicle membranes. Antibody EH5 strongly agglutinated amebas in a similar way to concanavalin A (Con A), and Con A bound to immunoaffinity-purified EH5 antigen. Therefore, surface lipophosphoglycans may play an important role in the preferential agglutination of pathogenic amebas by Con A. The protective ability of antibody EH5 was tested in a passive immunization experiment in a severe combined immunodeficient (SCID) mouse model. Intrahepatic challenge of animals after administration of an isotype-matched control antibody or without treatment led to the development of a liver abscess in all cases, whereas 11 out of 12 animals immunized with the EH5 antibody developed no liver abscess. Our results demonstrate the importance and, for the first time, the protective capacity of glycan antigens on the surface of the amebas.


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