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dc.contributor.author | Sanghamitra, Nusrat J M | en |
dc.contributor.author | Inaba, Hiroshi | en |
dc.contributor.author | Arisaka, Fumio | en |
dc.contributor.author | Ohtan Wang, Dan | en |
dc.contributor.author | Kanamaru, Shuji | en |
dc.contributor.author | Kitagawa, Susumu | en |
dc.contributor.author | Ueno, Takafumi | en |
dc.contributor.alternative | 稲葉, 央 | ja |
dc.contributor.alternative | 北川, 進 | ja |
dc.date.accessioned | 2015-10-09T02:35:49Z | - |
dc.date.available | 2015-10-09T02:35:49Z | - |
dc.date.issued | 2014-08-01 | - |
dc.identifier.issn | 1742-206X | - |
dc.identifier.uri | http://hdl.handle.net/2433/200240 | - |
dc.description | Accepted 25 Jul 2014. | en |
dc.description.abstract | Plasma membrane translocation is challenging due to the barrier of the cell membrane. Contrary to the synthetic cell-penetrating materials, tailed bacteriophages use cell-puncturing protein needles to puncture the cell membranes as an initial step of the DNA injection process. Cell-puncturing protein needles are thought to remain functional in the native phages. In this paper, we found that a bacteriophage T4 derived protein needle of 16 nm length spontaneously translocates through the living cell membrane. The β-helical protein needle (β-PN) internalizes into human red blood cells that lack endocytic machinery. By comparing the cellular uptake of β-PNs with modified surface charge, it is shown that the uptake efficiency is maximum when it has a negative charge corresponding to a zeta potential value of -16 mV. In HeLa cells, uptake of β-PN incorporates endocytosis independent mechanisms with partial macropinocytosis dependence. The endocytosis dependence of the uptake increases when the surface charges of β-PNs are modified to positive or negative. Thus, these results suggest that natural DNA injecting machinery can serve as an inspiration to design new class of cell-penetrating materials with a tailored mechanism. | en |
dc.format.mimetype | application/pdf | - |
dc.language.iso | eng | - |
dc.publisher | Royal Society of Chemistry | en |
dc.rights | This journal is © The Royal Society of Chemistry 2014. | en |
dc.rights | This is not the published version. Please cite only the published version. | en |
dc.rights | この論文は出版社版でありません。引用の際には出版社版をご確認ご利用ください。 | ja |
dc.subject.mesh | Amino Acid Motifs | en |
dc.subject.mesh | Bacteriophage T4/metabolism | en |
dc.subject.mesh | Cell Membrane/metabolism | en |
dc.subject.mesh | Erythrocytes/metabolism | en |
dc.subject.mesh | HeLa Cells | en |
dc.subject.mesh | Humans | en |
dc.subject.mesh | Membrane Potentials | en |
dc.subject.mesh | Models, Molecular | en |
dc.subject.mesh | Protein Conformation | en |
dc.subject.mesh | Protein Interaction Domains and Motifs | en |
dc.subject.mesh | Protein Transport | en |
dc.subject.mesh | Proteins/chemistry | en |
dc.subject.mesh | Proteins/metabolism | en |
dc.subject.mesh | Viral Proteins/genetics | en |
dc.subject.mesh | Viral Proteins/metabolism | en |
dc.title | Plasma membrane translocation of a protein needle based on a triple-stranded β-helix motif. | en |
dc.type | journal article | - |
dc.type.niitype | Journal Article | - |
dc.identifier.ncid | AA12052142 | - |
dc.identifier.jtitle | Molecular BioSystems | en |
dc.identifier.volume | 10 | - |
dc.identifier.issue | 10 | - |
dc.identifier.spage | 2677 | - |
dc.identifier.epage | 2683 | - |
dc.relation.doi | 10.1039/c4mb00293h | - |
dc.textversion | author | - |
dc.startdate.bitstreamsavailable | 2015-07-25 | - |
dc.identifier.pmid | 25082560 | - |
dcterms.accessRights | open access | - |
出現コレクション: | 学術雑誌掲載論文等 |
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