alexa Characterization of Two Non-Fetuin-Binding Lectins from
ISSN: 2168-958X

Journal of Glycobiology
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Research Article

Characterization of Two Non-Fetuin-Binding Lectins from Tepary Bean (Phaseolus acutifolius) Seeds with Differential Cytotoxicity on Colon Cancer Cells

Iovanna Torres Arteaga3,4, Jose L Castro Guillén1, Elizabeth Mendiola Olaya1, Teresa García Gasca2, Marco Vinicio Ángeles Zaragoza2, Violeta García-Santoyo2, Jorge Ariel Torres Castillo5, Cesar Aguirre3, Brett Phinney6 and Alejandro Blanco-Labra1*

1CINVESTAV of the National Polytechnic Institute, Unit Irapuato, Guanajuato, Mexico

2University of Queretaro, Faculty of Natural Sciences, Mexico

3National Technology of Mexico, Technological Institute of Roque, Celaya, Guanajuato, Mexico

4Polytechnic University of the Bicentennial, Silao Romita State, Guanajuato, Mexico

5University of Tamaulipas, Institute of Applied Ecology, Victoria, Tamaulipas, Mexico

6University of California, Davis - UC Davis Genome Center 451 Health Sciences Drive, USA

*Corresponding Author:
Blanco Labra A
Centro de Investigación y de Estudios Avanzados
del Instituto Politécnico Nacional, Unidad Irapuato
Km. 9.6, Libramiento Norte, Carretera Irapuato-León
A.P. 629. C.P. 36821, Irapuato, Guanajuato, México
Tel: 1052-462-623 9640
E-mail: [email protected]

Received Date: April 27, 2016; Accepted Date: May 23, 2016; Published Date: May 30, 2016

Citation: Torres-Arteaga I, Guillén JLC, Olaya EM, Gasca TG, Zaragoza MVÁ, et al. (2016) Characterization of Two Non-Fetuin-Binding Lectins from Tepary Bean (Phaseolus acutifolius) Seeds with Differential Cytotoxicity on Colon Cancer Cells. J Glycobiol 5:117. doi:10.4172/2168-958X.1000117

Copyright: ©2016 Torres-Arteaga I, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.



Two non-fetuin-binding lectins from tepary bean (Phaseolus acutifolius) seeds were purified and characterized. Both lectins LA and LB showed by two dimensional gel electrophoresis very similar apparent molecular mass, and their isoelectric point for both lectins were also very close. Mass spectrometry analysis confirmed these similarities showing high sequence homology among them, and when these sequences were compared to the Mirkov´s deduced sequence of the phyto-hemagglutinin from Phaseolus acutifolius, LA showed higher homology than LB. On the other hand, when their biological activity was determined, only LA possessed affinity to type A erythrocytes, and when these lectins using a semi pure fraction were measured for their cytotoxic effect on colon cancer cells, they showed a differential effect. In the semi pure protein fraction tested, the rest of no-lectin proteins separated by electrophoresis presented no activity. Our results indicate that despite the high homology in their sequence, isoelectric point, and apparent molecular mass, these two structurally closely related lectins, showed differences in their biological behaviour, represented by their agglutinatination activity, as well as, in their cytotoxic effect on human colon cancer cells.


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