scholarly journals Cell Membrane Penetration without Pore Formation: Chameleonic Properties of Dendrimers in Response to Hydrophobic and Hydrophilic Environments

2020 ◽  
Vol 3 (7) ◽  
pp. 1900152
Author(s):  
Sergio Luca ◽  
Prasenjit Seal ◽  
Harendra S. Parekh ◽  
Karnaker R. Tupally ◽  
Sean C. Smith
Keyword(s):  
Cell Membrane ◽  
Pore Formation ◽  
Membrane Penetration

scholarly journals Macrophage Damage by Leishmania amazonensis Cytolysin: Evidence of Pore Formation on Cell Membrane

2000 ◽  
Vol 68 (8) ◽  
pp. 4578-4584 ◽  
Author(s):  
Fátima S. M. Noronha ◽  
Jader S. Cruz ◽  
Paulo S. L. Beirão ◽  
M. Fátima Horta
Keyword(s):  
Cell Membrane ◽  
Patch Clamp ◽  
Pore Formation ◽  
Cell Damage ◽  
Leishmania Amazonensis ◽  
Temperature Dependent ◽  
Patch Clamp Technique ◽  
Protein Subunits ◽  
Target Cell Membrane ◽  
Target Membrane

ABSTRACT We have previously shown that both promastigotes and amastigotes ofLeishmania amazonensis contain a lytic protein that damages erythrocytes and nucleated cells, including macrophages (F. S. M. Noronha, F. J. Ramalho-Pinto, and M. F. Horta, Infect. Immun. 64:3975–3982, 1996). Using the patch-clamp technique, we show here that cell damage by parasite extracts is mediated by the formation of nonselective pores on the target membrane. This demonstrates that L. amazonensis cytolysin is a pore-forming protein (PFP), here named leishporin. We show that the diameters of the pores formed by parasite extracts are heterogeneous, varying from ∼1.6 to >6.1 nm according to cytolysin concentration or time. We also show that pore formation involves the binding of the PFP to the target cell membrane, a temperature-independent event that is necessary but not sufficient to lyse cells. This is followed by a temperature-dependent step that triggers lysis, probably the insertion and the polymerization of protein subunits in the lipid bilayer. We provide evidence that suggests that polymerization of single subunits must occur for pore formation. We show, in addition, that L. amazonensis expresses molecules antigenically homologous to other PFPs.

scholarly journals Conformational-transited protein corona regulated cell-membrane penetration and induced cytotoxicity of ultrasmall Au nanoparticles

RSC Advances ◽  
2019 ◽  
Vol 9 (8) ◽  
pp. 4435-4444 ◽  
Author(s):  
Huayan Yang ◽  
Meng Wang ◽  
Yanmin Zhang ◽  
Feng Li ◽  
Shaoning Yu ◽  
...  
Keyword(s):  
Cell Membrane ◽  
Cell Membranes ◽  
Au Nanoparticles ◽  
Protein Corona ◽  
Membrane Disruption ◽  
Membrane Penetration

This study demonstrate that the AuNP–HSA corona could penetrate cell membranes and companied by substantial membrane disruption. However, the ultrasmall AuNPs can be internalized by cells without the destruction of cell membranes.

scholarly journals Restricted movement of lipid and aqueous dyes through pores formed by influenza hemagglutinin during cell fusion.

1994 ◽  
Vol 127 (6) ◽  
pp. 1885-1894 ◽  
Author(s):  
J Zimmerberg ◽  
R Blumenthal ◽  
D P Sarkar ◽  
M Curran ◽  
S J Morris
Keyword(s):  
Cell Membrane ◽  
Membrane Fusion ◽  
Cell Fusion ◽  
Pore Formation ◽  
Fusion Pore ◽  
Restricted Movement ◽  
Influenza Hemagglutinin ◽  
Simultaneous Measurements ◽  
Cell Membrane Capacitance ◽  
Total Fusion

The fusion of cells by influenza hemagglutinin (HA) is the best characterized example of protein-mediated membrane fusion. In simultaneous measurements of pairs of assays for fusion, we determined the order of detectable events during fusion. Fusion pore formation in HA-triggered cell-cell fusion was first detected by changes in cell membrane capacitance, next by a flux of fluorescent lipid, and finally by flux of aqueous fluorescent dye. Fusion pore conductance increased by small steps. A retardation of lipid and aqueous dyes occurred during fusion pore fluctuations. The flux of aqueous dye depended on the size of the molecule. The lack of movement of aqueous dyes while total fusion pore conductance increased suggests that initial HA-triggered fusion events are characterized by the opening of multiple small pores: the formation of a "sieve".

The bacteriophage ϕ29 tail possesses a pore-forming loop for cell membrane penetration

Nature ◽  
2016 ◽  
Vol 534 (7608) ◽  
pp. 544-547 ◽  
Author(s):  
Jingwei Xu ◽  
Miao Gui ◽  
Dianhong Wang ◽  
Ye Xiang
Keyword(s):  
Cell Membrane ◽  
Membrane Penetration

scholarly journals Molecular and biochemical characterization of a cytolysin from the Scorpaena plumieri (scorpionfish) venom: Evidence of pore formation on erythrocyte cell membrane

Toxicon ◽  
2013 ◽  
Vol 74 ◽  
pp. 92-100 ◽  
Author(s):  
Helena L. Gomes ◽  
Filipe Andrich ◽  
Consuelo L. Fortes-Dias ◽  
Jonas Perales ◽  
André Teixeira-Ferreira ◽  
...  
Keyword(s):  
Cell Membrane ◽  
Pore Formation ◽  
Biochemical Characterization

B102 Study of relation between the cell cortex structure and cell membrane penetration by nanoneedle

2009 ◽  
Vol 2009.20 (0) ◽  
pp. 31-32
Author(s):  
Takanori KIHARA ◽  
Hideki KAMIISHI ◽  
Chikashi NAKAMURA ◽  
Noriyuki NAKAMURA ◽  
Jun MIYAKE
Keyword(s):  
Cell Membrane ◽  
Cell Cortex ◽  
Membrane Penetration

Mild lipid extraction and anisotropic cell membrane penetration of α-phase phosphorene carbide nanoribbons by molecular dynamics simulation studies

2020 ◽  
Vol 22 (40) ◽  
pp. 23268-23275
Author(s):  
Yang Liu ◽  
Yanmei Yang ◽  
Yuanyuan Qu ◽  
Yong-Qiang Li ◽  
Mingwen Zhao ◽  
...  
Keyword(s):  
Molecular Dynamics ◽  
Molecular Dynamics Simulation ◽  
Cell Membrane ◽  
Lipid Extraction ◽  
Dynamics Simulation ◽  
Simulation Studies ◽  
Membrane Penetration ◽  
Α Phase ◽  
Zigzag Direction ◽  
Armchair Direction

α-PC penetrates the interior of membrane efficiently only along its zigzag direction rather than its armchair direction.

scholarly journals An invasive podosome-like structure promotes fusion pore formation during myoblast fusion

2010 ◽  
Vol 191 (5) ◽  
pp. 1013-1027 ◽  
Author(s):  
Kristin L. Sens ◽  
Shiliang Zhang ◽  
Peng Jin ◽  
Rui Duan ◽  
Guofeng Zhang ◽  
...  
Keyword(s):  
Cell Membrane ◽  
Pore Formation ◽  
Actin Polymerization ◽  
Single Channel ◽  
Myoblast Fusion ◽  
Fusion Pore ◽  
Cellular Mechanisms ◽  
Cytoskeletal Remodeling ◽  
Specific Manner ◽  
Cell Type Specific

Recent studies in Drosophila have implicated actin cytoskeletal remodeling in myoblast fusion, but the cellular mechanisms underlying this process remain poorly understood. Here we show that actin polymerization occurs in an asymmetric and cell type–specific manner between a muscle founder cell and a fusion-competent myoblast (FCM). In the FCM, a dense F-actin–enriched focus forms at the site of fusion, whereas a thin sheath of F-actin is induced along the apposing founder cell membrane. The FCM-specific actin focus invades the apposing founder cell with multiple finger-like protrusions, leading to the formation of a single-channel macro fusion pore between the two muscle cells. Two actin nucleation–promoting factors of the Arp2/3 complex, WASP and Scar, are required for the formation of the F-actin foci, whereas WASP but not Scar promotes efficient foci invasion. Our studies uncover a novel invasive podosome-like structure (PLS) in a developing tissue and reveal a previously unrecognized function of PLSs in facilitating cell membrane juxtaposition and fusion.

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