Protein sites of attack of N-chlorotaurine in Escherichia coli.

Abstract

N-Chlorotaurine sodium (NCT) is a promising microbicidal agent for topical treatment of infections. Its targets of attack in Escherichia coli have been investigated by proteomics. Incubation in 1% NCT for 10 and 30 min revealed a change of the charge and a separation of numerous proteins into a series of spots with a different pI. Charge differences could be related to oxidation of cysteine residues to their corresponding sulfonic acids. Heat shock protein 60 appeared, while ribosome-releasing factor, d-ribose periplasmic binding protein, and malonyl-CoA transacylase spots decreased. These results indicate penetration of oxidation capacity into the bacteria and destruction of essential proteins by NCT.

• Authors: Roland Arnitz, Bettina Sarg, Helmut W Ott, Andreas Neher, Herbert Lindner, Markus Nagl
• Journal: Proteomics (Proteomics) Vol. 6 Issue 3 Pg. 865-9 (Feb 2006) ISSN: 1615-9853 [Print] Germany
• PMID: 16372277 (Publication Type: Comparative Study, Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Bacterial Proteins
• Chaperonin 60
• Enzyme Inhibitors
• Periplasmic Binding Proteins
• Ribosomal Proteins
• Sulfonic Acids
• ribosome releasing factor
• Taurine
• N-chlorotaurine
• Acyl-Carrier Protein S-Malonyltransferase
• Protein Serine-Threonine Kinases
• Cysteine

Topics

• Acyl-Carrier Protein S-Malonyltransferase (metabolism)
• Bacterial Proteins (drug effects)
• Chaperonin 60 (metabolism)
• Cysteine (chemistry)
• Electrophoresis, Gel, Two-Dimensional
• Enzyme Inhibitors (pharmacology)
• Escherichia coli (drug effects, metabolism)
• Oxidation-Reduction
• Periplasmic Binding Proteins (metabolism)
• Protein Serine-Threonine Kinases (antagonists & inhibitors)
• Proteomics
• Ribosomal Proteins (metabolism)
• Spectrometry, Mass, Electrospray Ionization
• Sulfonic Acids (metabolism)
• Taurine (analogs & derivatives, pharmacology)