Translocation and nuclear accumulation of monomer and dimer of HIV-1 Tat basic domain in triticale mesophyll protoplasts

Chugh, Archana; Eudes, François

doi:10.1016/j.bbamem.2006.11.012

Cited by 48 publications

(41 citation statements)

References 52 publications

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“…Higher uptake at low temperatures suggests that CPPs transduction does not involve endocytosis but direct translocation across the cell membrane. A similar conclusion was drawn from continuous transduction observed in the presence of inhibitors of endocytisis or macropinocytosis, such as nocodazole, chloroquine, and sodium azide (13,32). As observed in mammalian cell lines, increase of pVEC and transportan fluorescence in plant protoplasts with increases in CPPs concentration also supports a concentration-dependent and nonsaturable uptake of CPPs in protoplast.…”

Section: Mode Of Traffickingsupporting

confidence: 54%

“…Viability of the microspores immediately after treatment with CPPs or their cargoes was also similar to the control microspores (65-70%). We have also seen that CPPs do not have any negative influence on the triticale mesophyll protoplast viability (13,32). Other workers have also found no cytotoxic effects of peptide treatment on root cells of different plants (63,64).…”

Section: Cytotoxicity and Cell Functionsupporting

confidence: 50%

“…Successful nucleic acid (DNA and dsRNA) transfection has been reported in protoplast, tobacco cell suspension culture, mungbean and soyabean root tips, and permeabilized immature wheat embryos (3,13,64,99,103). Posttranscriptional gene silencing was achieved using sense and antisense constructs of 0.4 and 0.9 kb in dsRNA/R12-treated tobacco cell suspension culture (64).…”

Section: Somatic Cellsmentioning

confidence: 99%

“…Recent investigations show that CPPs, such as Tat, Tat2, arginine-rich intracellular delivery peptides (AID), pVEC, transportan, and penetratin, can be taken up by suspensions of protoplasts from tobacco cells and triticale mesophyl cells (13,32,64,99). We studied uptake of pVEC and transportan in various plants tissues (32).…”

Section: Somatic Cellsmentioning

confidence: 99%

“…Single amino acid substitution can lead to the complete inhibition of translocation or nuclear localization such as mutated Tat with its first arginine substituted by alanine [M-Tat, (5)]. Differential uptake of CPPs in the same tissue can be a function of the sequence and length of the peptide (13). The presence of at least six arginine residues is required for effective translocation of Tat, and as the number of arginine residues is increased, the translocation ability also increases (5, 37).…”

Section: Structural-functional Relationship Of Cppsmentioning

confidence: 99%

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Cell‐penetrating peptides: Nanocarrier for macromolecule delivery in living cells

2010

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SummaryNovel classes and applications of cell-penetrating peptides (CPPs) are being constantly discovered since they were first identified 2 decades ago. These short cationic peptides (nanomolecules) either by covalent binding or by noncovalent binding can traverse cell membranes and deliver a variety of molecules that are unable to overcome the permeability barrier in their own capacity. The ability of the CPPs to deliver variety of macromolecules, such as oligonucleotides, therapeutic drugs, proteins, and medical imaging agents, by forming nanoparticulate carriers in a range of cells has led them to emerge as a potential tool for both macromolecule delivery application and to gain insight into the fundamentals of mechanism of cellular uptake across the plasma membrane. This review explores the recent advances, challenges, and future prospects in the field of CPP-mediated cargo delivery in mammalian and plant cells. Studies have been conducted into the peptide chemistry and stability of CPP-macromolecular complexes. Most of the CPPs have been shown to be nontoxic and do not interfere with the functionality of the macromolecules delivered across the cell membrane. The mechanism of uptake of CPP-cargo complexes and the uptake of CPPs alone across the plasma membrane remains unresolved. As the world of CPPs is rapidly advancing in both mammalian and plant system, there is a promising future for the various applications of transduction and transfection into intact cells.

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Section: Mode Of Traffickingsupporting

confidence: 54%

Section: Cytotoxicity and Cell Functionsupporting

confidence: 50%

Section: Somatic Cellsmentioning

confidence: 99%

Section: Somatic Cellsmentioning

confidence: 99%

Section: Structural-functional Relationship Of Cppsmentioning

confidence: 99%

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Cell‐penetrating peptides: Nanocarrier for macromolecule delivery in living cells

2010

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CD and NMR conformational studies of a peptide encompassing the Mid Loop interface of Ship2–Sam

et al. 2014

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The lipid phosphatase Ship2 is a protein that intervenes in several diseases such as diabetes, cancer, neurodegeneration, and atherosclerosis. It is made up of a catalytic domain and several protein docking modules such as a C-terminal Sam (Sterile alpha motif) domain. The Sam domain of Ship2 (Ship2-Sam) binds to the Sam domains of the EphA2 receptor (EphA2-Sam) and the PI3K effector protein Arap3 (Arap3-Sam). These heterotypic Sam-Sam interactions occur through formation of dimers presenting the canonical "Mid Loop/End Helix" binding mode. The central region of Ship2-Sam, spanning the C-terminal end of α2, the α3 and α4 helices together with the α2α3 and α3α4 interhelical loops, forms the Mid Loop surface that is needed to bind partners Sam domains. A peptide encompassing most of the Ship2-Sam Mid Loop interface (Shiptide) capable of binding to both EphA2-Sam and Arap3-Sam, was previously identified. Here we investigated the conformational features of this peptide, through solution CD and NMR studies in different conditions. These studies reveal that the peptide is highly flexible in aqueous buffer, while it adopts a helical conformation in presence of 2,2,2-trifluoroethanol. The discovered structural insights and in particular the identification of a helical motif, may lead to the design of more constrained and possibly cell permeable Shiptide analogs that could work as efficient antagonists of Ship2-Sam heterotypic interactions and embrace therapeutic applications.

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Using the Peptide Bp100 as a Cell‐Penetrating Tool for the Chemical Engineering of Actin Filaments within Living Plant Cells

Eggenberger

Mink²,

Wadhwani³

et al. 2010

ChemBioChem

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The delivery of externally applied macromolecules or nanoparticles into living cells still represents a critically limiting step before the full capabilities of chemical engineering can be explored. Molecular transporters such as cell-penetrating peptides, peptoids, and other mimetics can be used to carry cargo across the cellular membrane, but it is still difficult to find suitable sequences that operate efficiently for any particular type of cell. Here we report that BP100 (KKLFKKILKYL-amide), originally designed as an antimicrobial peptide against plant pathogens, can be employed as a fast and efficient cell-penetrating agent to transport fluorescent test cargoes into the cytosol of walled plant cells. The uptake of BP100 proceeds slightly more slowly than the endocytosis of fluorescent dextranes, but BP100 accumulates more efficiently and to much higher levels (by an order of magnitude). The entry of BP100 can be efficiently blocked by latrunculin B; this suggests that actin filaments are essential to the uptake mechanism. To test whether this novel transporter can also be used to deliver functional cargoes, we designed a fusion construct of BP100 with the actin-binding Lifeact peptide (MGVADLIKKFESISKEE). We demonstrated that the short BP100 could transport the attached 17-residue sequence quickly and efficiently into tobacco cells. The Lifeact construct retained its functionality as it successfully labeled the actin bundles that tether the nucleus in the cell center.

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Translocation and nuclear accumulation of monomer and dimer of HIV-1 Tat basic domain in triticale mesophyll protoplasts

Cited by 48 publications

References 52 publications

Cell‐penetrating peptides: Nanocarrier for macromolecule delivery in living cells

Cell‐penetrating peptides: Nanocarrier for macromolecule delivery in living cells

CD and NMR conformational studies of a peptide encompassing the Mid Loop interface of Ship2–Sam

Using the Peptide Bp100 as a Cell‐Penetrating Tool for the Chemical Engineering of Actin Filaments within Living Plant Cells

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