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Tytuł pozycji:

Anthrax toxin channel: What we know based on over 30 years of research.

Tytuł:
Anthrax toxin channel: What we know based on over 30 years of research.
Autorzy:
Liu W; Department of Biology, The Catholic University of America, 620 Michigan Ave, Washington, DC 20064, USA.
Nestorovich EM; Department of Biology, The Catholic University of America, 620 Michigan Ave, Washington, DC 20064, USA. Electronic address: .
Źródło:
Biochimica et biophysica acta. Biomembranes [Biochim Biophys Acta Biomembr] 2021 Nov 01; Vol. 1863 (11), pp. 183715. Date of Electronic Publication: 2021 Jul 30.
Typ publikacji:
Journal Article; Research Support, N.I.H., Extramural; Review
Język:
English
Imprint Name(s):
Original Publication: Amsterdam : Elsevier
MeSH Terms:
Antigens, Bacterial/*metabolism
Bacterial Toxins/*metabolism
Antigens, Bacterial/chemistry ; Antigens, Bacterial/immunology ; Bacterial Toxins/chemistry ; Bacterial Toxins/immunology ; Hydrogen-Ion Concentration ; Lipid Bilayers ; Protein Conformation ; Protein Transport
Grant Information:
R15 AI099897 United States AI NIAID NIH HHS
Contributed Indexing:
Keywords: Channel-mediated transport; Ion channel conductance; Protein fluctuation dynamics; Protein translocation; Targeted toxin; Tripartite anthrax toxin
Substance Nomenclature:
0 (Antigens, Bacterial)
0 (Bacterial Toxins)
0 (Lipid Bilayers)
0 (anthrax toxin)
Entry Date(s):
Date Created: 20210801 Date Completed: 20211117 Latest Revision: 20211117
Update Code:
20240105
DOI:
10.1016/j.bbamem.2021.183715
PMID:
34332985
Czasopismo naukowe
Protective antigen channel is the central component of the deadly anthrax exotoxin responsible for binding and delivery of the toxin's enzymatic lethal and edema factor components into the cytosol. The channel, which is more than three times longer than the lipid bilayer membrane thickness and has a 6-Å limiting diameter, is believed to provide a sophisticated unfoldase and translocase machinery for the foreign protein transport into the host cell cytosol. The tripartite toxin can be reengineered, one component at a time or collectively, to adapt it for the targeted cancer therapeutic treatments. In this review, we focus on the biophysical studies of the protective antigen channel-forming activity, small ion transport properties, enzymatic factor translocation, and blockage comparing it with the related clostridial binary toxin channels. We address issues linked to the anthrax toxin channel structural dynamics and lipid dependence, which are yet to become generally recognized as parts of the toxin translocation machinery.
(Copyright © 2021 Elsevier B.V. All rights reserved.)

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