scholarly journals Multivalent and dynamic interactions of the influenza virus at lipid membrane interfaces

2021 ◽  
Author(s):  
Nico Johan Overeem
Keyword(s):  
Influenza Virus ◽  
Lipid Membrane ◽  
Dynamic Interactions ◽  
Membrane Interfaces

Radiation Effects with a Model Lipid Membrane

1971 ◽  
Vol 49 (8) ◽  
pp. 1187-1196 ◽  
Author(s):  
A. Petkau
Keyword(s):  
Radiation Effects ◽  
Lipid Membrane ◽  
Protonmotive Force ◽  
X Rays ◽  
Phospholipid Membrane ◽  
Nernst Potential ◽  
Membrane Interfaces ◽  
A Cell ◽  
Collimated Beam

A cell is described that permits a model phospholipid membrane and the two adjacent aqueous compartments to be irradiated with a collimated beam of X-rays. During a 2 h irradiation a marked increase in [H+] in the aqueous phases is observed. A protonmotive force, given by the H+ Nernst potential, is generated when one compartment only is irradiated or when both compartments separated by a membrane made structurally asymmetric by the adsorption of alamethicin, are irradiated equally.The results of irradiations in N2O, N2, and O2 indicate that the membrane scavenges the superoxide O2−. The effect is discussed in terms of a clearing field that is derived from the potential at the membrane interfaces.

scholarly journals Immobilization Strategies for Functional Complement Convertase Assembly at Lipid Membrane Interfaces

Langmuir ◽  
2017 ◽  
Vol 33 (29) ◽  
pp. 7332-7342 ◽  
Author(s):  
Saziye Yorulmaz Avsar ◽  
Joshua A. Jackman ◽  
Min Chul Kim ◽  
Bo Kyeong Yoon ◽  
Walter Hunziker ◽  
...  
Keyword(s):  
Lipid Membrane ◽  
Membrane Interfaces

Sodium Deoxycholate Exerts a Direct Destructive Effect on HIV and Influenza Viruses in vitro and Inhibits Retrovirus-Induced Pathology in An Animal Model

1994 ◽  
Vol 5 (3) ◽  
pp. 176-181 ◽  
Author(s):  
J. S. Oxford ◽  
M. A. Zuckerman ◽  
E. Race ◽  
R. Dourmashkin ◽  
K. Broadhurst ◽  
...  
Keyword(s):  
Influenza Virus ◽  
Bile Salts ◽  
Lipid Membrane ◽  
Sodium Deoxycholate ◽  
Influenza Viruses ◽  
Virus Infectivity ◽  
Destructive Effect ◽  
Leukaemia Virus ◽  
Point Of Entry

The bile salt sodium deoxycholate had a virucidal effect on influenza, Rauscher leukaemia and HIV-1 viruses, reducing virus infectivity by a maximum of 6 logs TCID50 ml−1 after 1 h incubation at 37 °C with 50 μg ml−1 of the compound. Electron microscopy demonstrated directly that sodium deoxycholate and other bile salts perturbed influenza virus structure causing partial or complete disruption of the virion lipid membrane, thus allowing entry of phosphotungstate dye to the virion interior. Parenteral administration of sodium deoxycholate (14 mg kg−1) to Balb/C mice abrogated pathology caused by Rauscher leukaemia virus replicating in the spleen and influenza virus replicating in the lung. Bile salts may also have clinical potential as topical virucidal agents at the point of entry of enveloped viruses and particularly against HIV.

scholarly journals Influenza virus binds its host cell using multiple dynamic interactions

2012 ◽  
Vol 109 (34) ◽  
pp. 13626-13631 ◽  
Author(s):  
C. Sieben ◽  
C. Kappel ◽  
R. Zhu ◽  
A. Wozniak ◽  
C. Rankl ◽  
...  
Keyword(s):  
Influenza Virus ◽  
Host Cell ◽  
Dynamic Interactions

scholarly journals A non-linear system patterns Rab5 GTPase on the membrane

2019 ◽  
Author(s):  
A Cezanne ◽  
J Lauer ◽  
A Solomatina ◽  
IF Sbalzarini ◽  
M Zerial
Keyword(s):  
Lipid Bilayers ◽  
Lipid Membrane ◽  
Small Gtpases ◽  
Small Gtpase ◽  
Nucleotide Exchange ◽  
Membrane Composition ◽  
Dynamic Interactions ◽  
Universal System ◽  
Non Linear ◽  
Non Linear System

AbstractProteins can self-organize into spatial patterns via non-linear dynamic interactions on cellular membranes. Modelling and simulations have shown that small GTPases can generate patterns by coupling guanine nucleotide exchange factors (GEF) to effector binding, generating a positive feedback of GTPase activation and membrane recruitment. Here, we reconstituted the patterning of the small GTPase Rab5 and its GEF/effector complex Rabex5/Rabaptin5 on supported lipid bilayers as a model system for membrane patterning. We show that there is a “handover” of Rab5 from Rabex5 to Rabaptin5 upon nucleotide exchange. A minimal system consisting of Rab5, RabGDI and a complex of full length Rabex5/Rabaptin5 was necessary to pattern Rab5 into membrane domains. Surprisingly, a lipid membrane composition mimicking that of the early endosome was required for Rab5 patterning. The prevalence of GEF/effector coupling in nature suggests a possible universal system for small GTPase patterning involving both protein and lipid interactions.

scholarly journals Inhibition of release of lentivirus particles with incorporated human influenza virus haemagglutinin by binding to sialic acid-containing cellular receptors

2001 ◽  
Vol 82 (10) ◽  
pp. 2485-2494 ◽  
Author(s):  
Valerie Bosch ◽  
Beatrice Kramer ◽  
Tanya Pfeiffer ◽  
Lilian Stärck ◽  
David A. Steinhauer
Keyword(s):  
Influenza Virus ◽  
Sialic Acid ◽  
Binding Site ◽  
Lipid Membrane ◽  
Surface Proteins ◽  
Human Influenza ◽  
Receptor Binding Site ◽  
Human Influenza Virus ◽  
Cellular Receptors ◽  
Influenza Virus A

Mutants of the haemagglutinin (HA) gene of human influenza virus A/Aichi/2/68 (H3N2) encoding HA proteins that are proteolytically cleaved intracellularly, defective in binding to cellular receptors or defective for acylation within the cytoplasmic C terminus have been generated. Here, the properties of these mutated HA molecules are described and their incorporation into the lipid membrane of released human immunodeficiency virus (HIV)-like particles is analysed. It is demonstrated that, when produced from cells coexpressing any of the binding-competent Aichi-HA molecules, release of HIV-like particles into the extracellular medium is reduced and the particles that are released fail to incorporate Aichi-HA. These blocks in release and incorporation, respectively, can both be overcome. The release of normal amounts of particles with incorporated HA can be achieved either by mutation of the receptor-binding site on the Aichi-HA molecule or by removal of sialic acid from surface proteins with neuraminidase. In contrast, as a result of blockage of the sialic acid-binding site by sialidated oligosaccharides on the HA itself, the HA of influenza virus A/FPV/Rostock/34 (H7N1) is efficiently incorporated into HIV-like particles. These results, namely that particle release can be inhibited by interactions between the incorporated glycoprotein and the cell surface and/or that interactions with other cellular components can be inhibitory to incorporation into retrovirus envelopes, probably reflect general principles that may hold for many viral and cellular glycoproteins.

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