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Proteomic profile of Ortleppascaris sp.: A helminth parasite of Rhinella marina in the Amazonian region.


ABSTRACT: Ortleppascaris sp. is a helminth that, in its larval stage, infects the liver parenchyma of the amphibian Rhinella marina, resulting in severe physiological and pathological changes. This study used a proteomic approach to determine the overall profile of proteins expressed in a somatic extract from the nematodes to investigate the relationship between the parasite and its host. A total of 60 abundant proteins were selected from the two-dimensional electrophoresis, identified by peptide mass fingerprinting, and grouped based on their Gene Ontology by the biological processes in which they are potentially involved. Important helminthic derivatives, such as the immunoreactive As37 antigen, guanylyl cyclases, proteolytic enzymes, and other proteins conserved among different parasites, were identified through homology. This study represents a new approach to helminth-related proteomic studies using an amphibian animal model. Furthermore, this study identified protein markers that are important to the host-parasite relationship and the viability, development, infectivity, and virulence of helminths.

SUBMITTER: E Silva JP 

PROVIDER: S-EPMC4142265 | biostudies-literature | 2014 Aug

REPOSITORIES: biostudies-literature

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Proteomic profile of Ortleppascaris sp.: A helminth parasite of Rhinella marina in the Amazonian region.

E Silva Jefferson Pereira JP   Furtado Adriano Penha AP   Dos Santos Jeannie Nascimento JN  

International journal for parasitology. Parasites and wildlife 20140406 2


Ortleppascaris sp. is a helminth that, in its larval stage, infects the liver parenchyma of the amphibian Rhinella marina, resulting in severe physiological and pathological changes. This study used a proteomic approach to determine the overall profile of proteins expressed in a somatic extract from the nematodes to investigate the relationship between the parasite and its host. A total of 60 abundant proteins were selected from the two-dimensional electrophoresis, identified by peptide mass fin  ...[more]

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