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rdf:type |
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lifeskim:mentions |
umls-concept:C0003320,
umls-concept:C0040715,
umls-concept:C0051962,
umls-concept:C0332120,
umls-concept:C0439799,
umls-concept:C0599718,
umls-concept:C0599813,
umls-concept:C0599893,
umls-concept:C0964849,
umls-concept:C1522702,
umls-concept:C1548602,
umls-concept:C1550548,
umls-concept:C1555714,
umls-concept:C1705654
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pubmed:issue |
48
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pubmed:dateCreated |
2004-12-1
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pubmed:abstractText |
Entry of the enzymatic components of anthrax toxin [lethal factor (LF) and edema factor] into the cytosol of mammalian cells depends on the ability of the activated protective antigen (PA63) component to form a channel (pore) in the membrane of an acidic intracellular compartment. To investigate the mechanism of translocation, we characterized N-terminally truncated forms of the PA63-binding domain of LF (LFN). Deleting 27 or 36 residues strongly inhibited acid-triggered translocation of LFN across the plasma membrane of CHO-K1 cells and ablated the protein's ability to block PA63 channels in planar lipid bilayers at a small positive voltage (+20 mV). Fusing a H6-tag to the N terminus of the truncated proteins restored both translocation and channel-blocking activities. At +20 mV, N-terminal H6 and biotin tags were accessible to Ni2+ and streptavidin, respectively, added to the trans compartment of a planar bilayer. On the basis of these findings, we propose that the N terminus of PA63-bound LF or edema factor enters the PA63-channel under the influence of acidic pH and a positive transmembrane potential and initiates translocation in an N- to C-terminal direction.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/15548616-10320374,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15548616-10828989,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15548616-11113126,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15548616-11700563,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15548616-11741919,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15548616-11790132,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15548616-11997439,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15548616-12668662,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15548616-1438214,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15548616-14570563,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15548616-15243628,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15548616-15313199,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15548616-15326297,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15548616-15337774,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15548616-15533442,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15548616-1704045,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15548616-2467303,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15548616-4362061,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15548616-7512762,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15548616-7543106,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15548616-7783638,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15548616-7927776,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15548616-8051159,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15548616-8132565,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15548616-8304433,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15548616-8710889,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15548616-8868045,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15548616-9039918,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15548616-9251786,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15548616-9521715,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15548616-9539735,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15548616-9843379
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
30
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pubmed:volume |
101
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
16756-61
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:15548616-Amino Acid Sequence,
pubmed-meshheading:15548616-Animals,
pubmed-meshheading:15548616-Antigens, Bacterial,
pubmed-meshheading:15548616-Bacterial Toxins,
pubmed-meshheading:15548616-Base Sequence,
pubmed-meshheading:15548616-CHO Cells,
pubmed-meshheading:15548616-Cell Membrane,
pubmed-meshheading:15548616-Cricetinae,
pubmed-meshheading:15548616-DNA Primers,
pubmed-meshheading:15548616-Lipid Bilayers,
pubmed-meshheading:15548616-Molecular Sequence Data,
pubmed-meshheading:15548616-Protein Transport,
pubmed-meshheading:15548616-Sequence Homology, Amino Acid
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pubmed:year |
2004
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pubmed:articleTitle |
Evidence that translocation of anthrax toxin's lethal factor is initiated by entry of its N terminus into the protective antigen channel.
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pubmed:affiliation |
Department of Microbiology and Molecular Genetics, Harvard Medical School, 200 Longwood Avenue, Boston, MA 02115, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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