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http://hdl.handle.net/10553/45699
Title: | Targeting essential Eimeria ninakohlyakimovae sporozoite ligands for caprine host endothelial cell invasion with a phage display peptide library | Authors: | Ruiz Reyes, Antonio Pérez Barreto,Davinia Muñoz Ojeda, María Del Carmen Molina Caballero, José Manuel Taubert, Anja Jacobs-Lorena, Marcelo Vega-Rodríguez, Joel López González, Adassa María Hermosilla, Carlos R. |
UNESCO Clasification: | 240112 Parasitología animal | Keywords: | Membrane Antigen 1 Proteins Goats Bovis Eimeria ninakohlyakimovae, et al |
Issue Date: | 2015 | Publisher: | 0932-0113 | Journal: | Parasitology Research | Abstract: | Eimeria ninakohlyakimovae is an important coccidian parasite of goats which causes severe diarrhoea in young animals. Specific molecules that mediate E. ninakohlyakimovae host interactions and molecular mechanisms involved in the pathogenesis are still unknown. Although strong circumstantial evidence indicates that E. ninakohlyakimovae sporozoite interactions with caprine endothelial host cells (ECs) are specific, hardly any information is available about the interacting molecules that confer host cell specificity. In this study, we describe a novel method to identify surface proteins of caprine umbilical vein endothelial cells (CUVEC) using a phage display library. After several panning rounds, we identified a number of peptides that specifically bind to the surface of CUVEC. Importantly, caprine endothelial cell peptide 2 (PCEC2) and PCEC5 selectively reduced the infection rate by E. ninakohlyakimovae sporozoites. These preliminary data give new insight for the molecular identification of ligands involved in the interaction between E. ninakohlyakimovae sporozoites and host ECs. Further studies using this phage approach might be useful to identify new potential target molecules for the development of anti-coccidial drugs or even new vaccine strategies. | URI: | http://hdl.handle.net/10553/45699 | ISSN: | 0932-0113 | DOI: | 10.1007/s00436-015-4666-x | Source: | Parasitology Research [ISSN 0932-0113], v. 114, p. 4327-4331 |
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