Document Detail


Structure and function of a unique pore-forming protein from a pathogenic acanthamoeba.
MedLine Citation:
PMID:  23143413     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
Human pathogens often produce soluble protein toxins that generate pores inside membranes, resulting in the death of target cells and tissue damage. In pathogenic amoebae, this has been exemplified with amoebapores of the enteric protozoan parasite Entamoeba histolytica. Here we characterize acanthaporin, to our knowledge the first pore-forming toxin to be described from acanthamoebae, which are free-living, bacteria-feeding, unicellular organisms that are opportunistic pathogens of increasing importance and cause severe and often fatal diseases. We isolated acanthaporin from extracts of virulent Acanthamoeba culbertsoni by tracking its pore-forming activity, molecularly cloned the gene of its precursor and recombinantly expressed the mature protein in bacteria. Acanthaporin was cytotoxic for human neuronal cells and exerted antimicrobial activity against a variety of bacterial strains by permeabilizing their membranes. The tertiary structures of acanthaporin's active monomeric form and inactive dimeric form, both solved by NMR spectroscopy, revealed a currently unknown protein fold and a pH-dependent trigger mechanism of activation.
Authors:
Matthias Michalek; Frank D Sönnichsen; Rainer Wechselberger; Andrew J Dingley; Chien-Wen Hung; Annika Kopp; Hans Wienk; Maren Simanski; Rosa Herbst; Inken Lorenzen; Francine Marciano-Cabral; Christoph Gelhaus; Thomas Gutsmann; Andreas Tholey; Joachim Grötzinger; Matthias Leippe
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-11-11
Journal Detail:
Title:  Nature chemical biology     Volume:  -     ISSN:  1552-4469     ISO Abbreviation:  Nat. Chem. Biol.     Publication Date:  2012 Nov 
Date Detail:
Created Date:  2012-11-12     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101231976     Medline TA:  Nat Chem Biol     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Affiliation:
1] Zoological Institute, Zoophysiology, Christian-Albrechts Universität zu Kiel, Kiel, Germany. [2] Institute of Biochemistry, Christian-Albrechts Universität zu Kiel, Kiel, Germany.
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