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Calreticulin-like molecule in trophozoites of Entamoeba histolytica HM1:IMSS (Swissprot: accession P83003).

Enrique GonzálezDepto. de Medicina Experimental, Facultad de Medicine, UNAM, México, DF, México.

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Guadalupe RicoDepto. de Medicina Experimental, Facultad de Medicine, UNAM, México, DF, México.

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Guillermo MendozaDepto. de Medicina Experimental, Facultad de Medicine, UNAM, México, DF, México.

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Fernando RamosDepto. de Medicina Experimental, Facultad de Medicine, UNAM, México, DF, México.

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Gabriela GarcíaDepto. de Medicina Experimental, Facultad de Medicine, UNAM, México, DF, México.

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Patricia MoránDepto. de Medicina Experimental, Facultad de Medicine, UNAM, México, DF, México.

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Alicia ValadezDepto. de Medicina Experimental, Facultad de Medicine, UNAM, México, DF, México.

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Emma I MelendroDepto. de Medicina Experimental, Facultad de Medicine, UNAM, México, DF, México.

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Cecilia XiménezDepto. de Medicina Experimental, Facultad de Medicine, UNAM, México, DF, México.

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In this work, we report the partial sequence of a 51 kDa protein of Entamoeba histolytica that is highly immunogenic in humans. Partial sequencing of the N-terminal end showed that 18 of the first 20 amino acid residues of the protein were identified uniquely, indicating that the final product was a homogeneous protein preparation. The N-terminal sequence that was found was: KVYFEETFENGWKXIWSKW. Comparing the 19-amino acid sequence of the protein in automated databases shows significant similarity with amino acid sequences of the calreticulin-like protein of spinach leaves (77%) and of the calreticulin precursor of Dictyostelium discoideum (60%).

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