Fasciola hepatica : Parasite-secreted proteinases degrade all human IgG subclasses

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Fasciola hepatica : Parasite-secreted proteinases degrade all human IgG subclasses

Tema

FASCIOLA HEPATICA
PROTEINASAS
BIBLIOGRAFIA NACIONAL QUIMICA
2000

Abstract

Berasain, P., Carmona, C., Frangione, B., Dalton, J. P., and Gon˜i, by cathepsins on digested proteins, its actions on IgG subclasses were F. 2000. Fasciola hepatica: Parasite-secreted proteinases degrade all specific and restricted; thus, all the fragments produced could be potenhuman IgG subclasses: Determination of the specific cleavage sites tially involved in the mechanisms used by the parasite to evade the and identification of the immunoglobulin fragments produced. Experi- host immune response. q 2000 Academic Press mental Parasitology 94, 99–110. The study was focused on the relation- Index Descriptors and Abbreviations: Fasciola hepatica; trematode; ship of Fasciola hepatica-secreted proteinases and human IgG sub- excretion–secretion (E/S); cysteine proteinase; cathepsin L1 (CL1); classes. Each IgG was incubated at different pH values and lengths of cathepsin L2 (CL2); newly excysted juveniles (NEJs); IgG subclasses; time with either the adult parasite excretion–secretion products or the enzyme specificity; cathepsin L cleavage site; immune evasion; 7- purified cysteinyl proteinases cathepsin L1 and cathepsin L2. The Ig aminomethylcoumarin (NHMec); Coomassie brilliant blue (CBB); sofragments produced were isolated and characterized by Western blot dium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS– analysis, and the specific cleavage sites were determined by amino PAGE); heavy (H); light (L). acid sequence analysis. Parasite excretion–secretion products and both cathepsins L produced similar degradation patterns and cleaved all human IgG subclasses at the hinge region, yielding at pH 7.3 and 378C Fab and Fc fragments in the case of IgG1 and IgG3 or Fab2 and Fc in IgG2 and IgG4. While IgG1 and IgG3 were readily degraded by E/ S products either in the presence or in the absence of reducing agents, INTRODUCTION IgG2 and IgG4 were resistant to proteolysis and were only digested in the presence of 0.1 M dithiothreitol. The cathepsins L needed the presence of dithiothreitol to digest IgG1, IgG2, and IgG4 whereas IgG3 was identically cleaved under both reducing and nonreducing Fasciola hepatica, the common liver fluke, is the causconditions. The main cleavage sites produced by E/S products, CL1, ative agent of fasciolosis in mammals. When infecting rumior CL2 were located at the positions peptide bonds: His237-Thr238, nants, like cattle and sheep, it causes significant economical Glu237-Cys239, Gly233-Asp234, and Ser241-Cys242 for g 1, g 2, g 3, or g 4, respectively. The enzymes gave additional splitting sites on the losses in agricultural-based countries. Moreover, recent remiddle hinge of IgG3 to produce shorter Fc fragments and also produce ports indicate that fasciolosis, as a zoonosis that affects Fd degradation of the IgG4. No cleavage specificity differences were humans, is more important than previously thought (Bjorland found between CL1 and CL2, but they differed in the kinetics of IgG3 et al. 1995; Esteban et al. 1997). The trematode burrows degradation. By lowering the pH, only the E/S products produced through the gut wall of its mammalian host and spends concomitant destruction of the Fc while preserving the Fab portion. Under all the conditions assayed the enzymes produced an Fc8-like approximately 2 months migrating within the liver before fragment of 14–15 kDa corresponding to the whole CH3 domain of entering the bile ducts where they reach sexual maturation the immunoglobulin. Contrary to the extensive degradation produced

Autor

Berasain, P
Carmona, C
Frangione, B
Dalton, J.P
Goñi, F

Fuente

Experimental Parasitology v. 94, , 2000. -- p. 99-110

Editor

Academic Press

Fecha

2000

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Artículo

Identificador

DOI:10.1006/expr.1999.4479
Fecha de agregación
April 28, 2015
Colección
Bibliografía Nacional Química
Tipo de Elemento
Document
Etiquetas
,
Citación
Berasain, P, “Fasciola hepatica : Parasite-secreted proteinases degrade all human IgG subclasses,” RIQUIM - Repositorio Institucional de la Facultad de Química - UdelaR, accessed November 29, 2020, http://riquim.fq.edu.uy/items/show/2903.
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