1887

Abstract

colonizes the murine intestine and has been associated with hepatic inflammation and neoplasia in susceptible mouse strains. In this study, the catalase of an enterohepatic was characterized for the first time. catalase is a highly conserved enzyme that may be important for bacterial survival in the mammalian intestine. Recombinant catalase was expressed in in order to verify its enzymic activity . catalase comprises 478 amino acids with a highly conserved haem-ligand domain. Three conserved motifs (R-F-Y-D, RERIPER and VVHAKG) in the haem-ligand domain and three surface-predicted motifs were identified in catalase and are shared among bacterial and mammalian catalases. catalase is present in the cytoplasmic and periplasmic compartments. Mice infected with demonstrated immune responses to murine and catalase, suggesting that catalase contains conserved structural motifs and may contribute to autoimmune responses. Antibodies to catalase recognized murine hepatocyte catalase in hepatic tissue from infected mice. Antibodies from sera of -infected mice reacted with peptides comprising two conserved surface-predicted motifs in catalase. Catalases are highly conserved enzymes in bacteria and mammals that may contribute to autoimmune responses in animals infected with catalase-producing pathogens.

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2007-04-01
2020-04-03
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