Antibody response to a protease secreted by Trichinella spiralis muscle larvae
Authors
Armas Serra, Cristina de; Giménez Pardo, Consuelo; Bernardina, Wilbert E.; Rodríguez Caabeiro, Filomena CrisantaIdentifiers
Permanent link (URI): http://hdl.handle.net/10017/61427DOI: 10.1007/BF00931800
ISSN: 09320113
Date
1995-07Bibliographic citation
PARASITOL RES, 1995, v. 81, n. 6, p. 540-542
Keywords
Trichinella spiralis
respuesta humoral
proteasa purificada
Description / Notes
En el presente estudio analizamos la respuesta humoral de ratones infectados con Trichinella spiralis a una proteasa de 35 kDa (purificada a partir de los productos excretores-secretores de las larvas del músculo de T. espiralis) mediante un procedimiento de transferencia Western y un ensayo inmunoabsorbente ligado a enzimas ( ELISA) utilizando un panel de sueros anti-Trichinella de ratón postinfección. Los resultados demostraron que esta respuesta dependía del tiempo y que los ratones infectados podían distinguirse de los controles. Además, los ensayos de inhibición demostraron que estos antisueros eran capaces de suprimir la actividad proteinasa de la proteasa de 35 kDa in vitro.
Document type
info:eu-repo/semantics/article
Version
info:eu-repo/semantics/aceptedVersion
Rights
Attribution-NonCommercial-NoDerivatives 4.0 International (CC BY-NC-ND 4.0)
© Springer-Verlag 1995
Access rights
info:eu-repo/semantics/openAccess
Abstract
In the present study we analyzed the humoral response of Trichinella spiralis-infected mice to a 35-kDa protease (purified from the excretory-secretory products of T. spiralis muscle larvae) by a Western-blot procedure and an enzyme-linked immunosorbent assay (ELISA) technique using a panel of postinfection mouse anti-Trichinella sera. The results demonstrated that this response was time-dependent and that infected mice could be distinguished from controls. In addition, inhibition assays demonstrated that these antisera were capable of abolishing the proteinase activity of the 35-kDa protease in vitro.
The occurrence of proteases seems to be a very common feature in parasite crude extracts and excretory-secretory products (McKerrow 1989). It is also known that these enzymes are implicated in important host-parasite interactions, and for this reason, recent reports have proposed the use of parasite proteases both as alternative targets for an induced immune response and as a rich source of antigenic material for diagnostic testing (Hotez etal. 1985; Yamasaki etal. 1989; Song et al. 1990; Frank and Grieve 1991; Britton et al. 1992; Song and Chappell 1993).
We have recently purified a protease (mol. wt., 35 kDa) from the excretory-secretory (ES) products of Trichinella Spiralis (GM-1 strain) muscle larvae and established some of the biochemical properties of this protease (Armas-Serra et al. 1994). The present study was undertaken to determine whether this protease would be recognized as an antigenic molecule by the host immune system, as occurs in the case of other parasites, and which effect the host immune response could have on the biochemical activity of the enzyme.
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