Abstract
In vitro growth experiments were conducted to evaluate the ability of vulnibactin, a siderophore produced by Vibrio vulnificus, to sequester transferrin- or lactoferrin bound iron for growth. Comparative studies with the strain producing vulnibactin and its exocellular protease-deficient mutant revealed the involvement of the protease in addition to vulnibactin in effective utilization of iron ion (Fe3+) bound to transferrin and lactoferrin. It appears that the protease causes cleavage of these proteins, thereby making bound iron more accessible to vulnibactin.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Amides / metabolism*
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Bacterial Proteins*
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Ferric Compounds / metabolism
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Iron / metabolism*
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Lactoferrin / metabolism
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Metalloendopeptidases / deficiency
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Metalloendopeptidases / genetics
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Metalloendopeptidases / metabolism*
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Mutation
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Oxazoles / metabolism*
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Siderophores / metabolism*
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Transferrin / metabolism
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Vibrio / metabolism*
Substances
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Amides
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Bacterial Proteins
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Ferric Compounds
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Oxazoles
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Siderophores
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Transferrin
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vulnibactin
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Iron
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Lactoferrin
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Metalloendopeptidases
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vvP protein, Vibrio vulnificus