INVESTIGADORES
DUHALDE VEGA Maite
artículos
Título:
THE PEPTIDE SPEFIFICITIES OF THE AUTOANTIBODIES ELICITED BY MOUSE HEPATITIS VIRUS A59
Autor/es:
DUHALDE VEGA, M.; LOUREIRO, ME; MATHIEU, PA; RETEGUI, LA
Revista:
JOURNAL OF AUTOIMMUNITY
Referencias:
Año: 2006 vol. 27 p. 203 - 209
ISSN:
0896-8411
Resumen:
Synthetic decapeptides (N = 206) covering the entire sequence of mouse liver
fumarylacetoacetate hydrolase (FAH) were used to analyze the specificities of the autoantibodies (autoAb)
elicited toward this enzyme in mice infected with mouse hepatitis virus (MHV). These autoAb bound mainly
to N- and C-terminal FAH peptides, the most reactive sequences being 1-50 and 390-420, respectively.
Surprisingly, although FAH sequence 1-50 shares a high degree of homology with various MHV proteins,
the C-terminal portion does not. Moreover, whereas the autoAb reacted with homologous peptides
surrounding residues 70 and 360, non-similar sequences around residues 130, 210, 250, and 300 were also
recognized, indicating that autoAb were not restricted to epitopes with sequence homologies. There was
also a lack of correlation between the amount of anti-MHV or anti-FAH antibodies produced and the
reactivity towards the peptides. Moreover, the spectrum of peptides recognized by the autoAb of a given
mouse did not change significantly with time, which suggests that the MHV-elicited autoimmune response
does not induce an epitope recognition spreading. Finally, anti-FAH Ab produced after immunization with rat
liver FAH recognized essentially the same mouse FAH regions than autoAb from MHV-infected mice.
Results indicated that the induction of the autoAb is not related to molecular or structural mimicry, but rather
supports the Danger model, in which any aggression, in this case the MHV infection, is susceptible to trigger
the production of autoAb.
reactivity towards the peptides. Moreover, the spectrum of peptides recognized by the autoAb of a given
mouse did not change significantly with time, which suggests that the MHV-elicited autoimmune response
does not induce an epitope recognition spreading. Finally, anti-FAH Ab produced after immunization with rat
liver FAH recognized essentially the same mouse FAH regions than autoAb from MHV-infected mice.
Results indicated that the induction of the autoAb is not related to molecular or structural mimicry, but rather
supports the Danger model, in which any aggression, in this case the MHV infection, is susceptible to trigger
the production of autoAb.
reactivity towards the peptides. Moreover, the spectrum of peptides recognized by the autoAb of a given
mouse did not change significantly with time, which suggests that the MHV-elicited autoimmune response
does not induce an epitope recognition spreading. Finally, anti-FAH Ab produced after immunization with rat
liver FAH recognized essentially the same mouse FAH regions than autoAb from MHV-infected mice.
Results indicated that the induction of the autoAb is not related to molecular or structural mimicry, but rather
supports the Danger model, in which any aggression, in this case the MHV infection, is susceptible to trigger
the production of autoAb.
reactivity towards the peptides. Moreover, the spectrum of peptides recognized by the autoAb of a given
mouse did not change significantly with time, which suggests that the MHV-elicited autoimmune response
does not induce an epitope recognition spreading. Finally, anti-FAH Ab produced after immunization with rat
liver FAH recognized essentially the same mouse FAH regions than autoAb from MHV-infected mice.
Results indicated that the induction of the autoAb is not related to molecular or structural mimicry, but rather
supports the Danger model, in which any aggression, in this case the MHV infection, is susceptible to trigger
the production of autoAb.
reactivity towards the peptides. Moreover, the spectrum of peptides recognized by the autoAb of a given
mouse did not change significantly with time, which suggests that the MHV-elicited autoimmune response
does not induce an epitope recognition spreading.