scholarly journals Viral Transduction Enhancing Effect of EF‐C Peptide Nanofibrils Is Mediated by Cellular Protrusions

2021 ◽  
pp. 2104814
Author(s):  
Desiree Schütz ◽  
Sascha Rode ◽  
Clarissa Read ◽  
Janis A. Müller ◽  
Bernhard Glocker ◽  
...  
2020 ◽  
Author(s):  
Desiree Schütz ◽  
Sascha Rode ◽  
Clarissa Read ◽  
Janis A. Müller ◽  
Bernhard Glocker ◽  
...  

AbstractSelf-assembling peptide nanofibrils (PNF) have gained increasing attention as versatile molecules in material science and biomedicine. One important application of PNF is to enhance retroviral gene transfer, a technology that has been central to the development of gene therapy. The best-investigated and commercially available PNF is derived from a 12-mer peptide termed EF-C. The mechanism of transduction enhancement depends on the polycationic surface of EF-C PNF, which binds to the negatively charged membranes of viruses and cells thereby overcoming electrostatic repulsion and increasing virion attachment and fusion. Assuming an even distribution of charges at the surfaces of virions and cells would result in an evenly distributed interaction of the virions with the cell surface. However, we here report that PNF do not randomly bind at the cell surface but are actively engaged by cellular protrusions. Chemical suppression of protrusion formation in cell lines and primary CD4+ T cells greatly reduced fibril binding and hence virion binding. Thus, the mechanism of PNF-mediated viral transduction enhancement involves active engagement of virus-loaded fibrils by cellular protrusions.


2018 ◽  
Vol 11 (1) ◽  
pp. 80-85
Author(s):  
Rodrigo Marmo da Costa e Souza ◽  
Felipe Ricardo Pereira Vasconcelos De Arruda ◽  
Jose Anderson Galdino Santos ◽  
Jamerson De Carvalho Andrade ◽  
Suellen Mary Marinho Dos Santos Andrade ◽  
...  

1960 ◽  
Vol 04 (03) ◽  
pp. 462-472 ◽  
Author(s):  
Tage Astrup ◽  
Ida Sterndorff

Summary1. The presence of citrate in the normal fibrin enhanced the fibrinolytic activity of plasminogen activators, including trypsin. The effect of proteases (on normal or on heated fibrin, containing citrate) was not significantly influenced.2. The effect of plasminogen activators was also increased when excess of plasminogen was present in the normal fibrin plates.3. Fumaric acid and maleic acid belong to the polycarboxylic acids producing an enhancing effect.


1963 ◽  
Vol 09 (02) ◽  
pp. 446-458 ◽  
Author(s):  
Rudolf Holemans ◽  
Dionysios Adamis ◽  
James F Horace

SummaryHeparin in high concentration inhibits the fibrinolysis of human plasma clots or bovine fibrin by fibrinolytic agents which produce plasminogen activation. Heparin has no effect on the fibrinolytic activity of plasmin or Aspergillus protease.In order to produce inhibition of plasminogen activation heparin requires the presence of a co-factor which is present in citrated human plasma but absent from its euglobulin fraction.In none of the concentrations tested has heparin an enhancing effect on fibrinolysis.


1971 ◽  
Vol 26 (01) ◽  
pp. 145-166
Author(s):  
E Deutsch ◽  
K Lechner ◽  
K Moser ◽  
L Stockinger

Summary1. The aniline derivative AN 162, Donau Pharmazie, Linz, Austria, has a dual action on the blood coagulation: an anticoagulant and an coagulation enhancing effect.2. The anticoagulant action may only be demonstrated with high concentrations (over 1 X 10”3 M related to plasma) preferentially in PPP. It is partially caused by an inhibition of the endogenous way of generation of the prothrombin converting principle. In addition it is suggested that it interferes with the fibrinogen-fibrin reaction in a manner not yet understood.3. The coagulant action is caused by a greater availability of platelet constituents at low concentrations of AN 162 (over 1 × 10-4 M) and by the induction of a release reaction at higher concentrations. The platelet factors 3 and 4, serotonin, adenine, and acid phosphatase are released.4. AN 162 inhibits platelet aggregation. This inhibition can be demonstrated by the PAT of Breddin and in the stirred aggregation test of Born. It is more effective to inhibit the collagen-induced and the second phase of the adrenaline-induced aggregation than the ADP induced one. The platelet retention (test of Hellem) is also reduced.5. The action of AN 162 on the platelets is caused by a damage of the platelet membrane which becomes permeabel for both, soluble platelet constitutents and granula.6. AN 162 interferes with the energy metabolism of the platelets. It causes a loss of ATP, and inhibits the key-enzymes of glycolysis, citric acid cycle, fatty acid oxydation and glutathione reduction.7. AN 162 inhibits the growth of fibroblasts without influence on mitosis.


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