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Comparison of the pH-induced conformational change of different clostridial neurotoxins
Dipartimento di Scienze Biomediche Sperimentali, Università di Padova, I-35121 Padua, Italy.ORCID iD: 0000-0002-9915-002x
2004 (English)In: Biochemical and Biophysical Research Communications - BBRC, ISSN 0006-291X, E-ISSN 1090-2104, Vol. 319, no 1, p. 66-71Article in journal (Refereed) Published
Abstract [en]

Clostridial neurotoxins are internalized inside acidic compartments, wherefrom the catalytic chain translocates across the membrane into the cytosol in a low pH-driven process, reaching its proteolytic substrates. The pH range in which the structural rearrangement of clostridial neurotoxins takes place was determined by 8-anilinonaphthalene-1-sulfonate and tryptophan fluorescence measurements. Half conformational change was attained at pH 4.55, 4.50, 4.40, 4.60, 4.40, and 4.40 for tetanus neurotoxin and botulinum neurotoxin serotypes /A, /B, /C, /E, and /F, respectively. This similarity indicates the key residues for the conformation transition are strongly conserved. Acidic liposomes support the conformational rearrangement shifting the effect versus higher pH values, whereas zwitterionic liposomes do not. The disulfide bridge linking the light and the heavy chains together needs to be oxidized to allow toxin membrane insertion, indicating that in vivo its reduction follows exposure to the cytosol after penetration of the endosomal membrane.

Place, publisher, year, edition, pages
2004. Vol. 319, no 1, p. 66-71
National Category
Microbiology Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:umu:diva-156954DOI: 10.1016/j.bbrc.2004.04.140PubMedID: 15158443OAI: oai:DiVA.org:umu-156954DiVA, id: diva2:1293131
Available from: 2019-03-03 Created: 2019-03-03 Last updated: 2019-03-11Bibliographically approved

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Puhar, Andrea

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