Abstract
Human beta-defensin 2 (HBD2) has been shown to interact with pathogenic bacteria and components of the mammalian innate and adaptive immune response. We describe a quick and reliable method for the production of HBD2 in Escherichia coli. HBD2 was expressed as an insoluble fusion, chemically cleaved and oxidised to give a single, folded HBD2 beta-isoform. The purified peptide was analysed by high resolution mass spectrometry, displayed a well-dispersed (1)H NMR spectrum, was a chemoattractant to HEK293 cells expressing CCR6 and acted as an antimicrobial agent against E. coli, P. aeruginosa, C. albicans and S. aureus.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Anti-Infective Agents / chemistry
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Anti-Infective Agents / metabolism*
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Anti-Infective Agents / pharmacology
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Bacteria / drug effects
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Base Sequence
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Cell Line
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Chemotaxis / drug effects
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Escherichia coli / genetics*
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Humans
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Mass Spectrometry
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Molecular Sequence Data
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Nuclear Magnetic Resonance, Biomolecular
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Protein Folding
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Receptors, CCR6 / metabolism
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Recombinant Fusion Proteins / chemistry
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Recombinant Fusion Proteins / genetics
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Recombinant Fusion Proteins / metabolism
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Recombinant Fusion Proteins / pharmacology
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beta-Defensins / chemistry
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beta-Defensins / genetics
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beta-Defensins / metabolism*
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beta-Defensins / pharmacology
Substances
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Anti-Infective Agents
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CCR6 protein, human
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DEFB4A protein, human
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Receptors, CCR6
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Recombinant Fusion Proteins
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beta-Defensins