Abstract
To evaluate the role of the zinc-binding metalloprotease in Bacteroides fragilis toxin (BFT) processing and activity, the zinc-binding consensus sequences (H348, E349, H352, G355, H358, and M366) were mutated by site-directed-mutagenesis. Our results indicated that single point mutations in the zinc-binding metalloprotease motif do not affect BFT processing but do reduce or eliminate BFT biologic activity in vitro.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Motifs
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Bacterial Toxins / metabolism*
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Bacteroides fragilis / enzymology
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Cadherins / metabolism
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Immunoblotting
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Metalloendopeptidases / metabolism*
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Metalloproteases / genetics*
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Metalloproteases / metabolism
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Mutation
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Peptides / metabolism*
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Reverse Transcriptase Polymerase Chain Reaction
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Zinc / metabolism*
Substances
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Bacterial Toxins
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Cadherins
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Peptides
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Metalloproteases
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Bacteroides fragilis toxin
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Metalloendopeptidases
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Zinc