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Thermoplasmonic Vesicle Fusion Reveals Membrane Phase Segregation of Influenza Spike Proteins.
Moreno-Pescador, Guillermo; Arastoo, Mohammad Reza; Ruhoff, Victoria Thusgaard; Chiantia, Salvatore; Daniels, Robert; Bendix, Poul Martin.
  • Moreno-Pescador G; Niels Bohr Institute, University of Copenhagen, Blegdamsvej 17, 2100 København Ø, Denmark.
  • Arastoo MR; Niels Bohr Institute, University of Copenhagen, Blegdamsvej 17, 2100 København Ø, Denmark.
  • Ruhoff VT; Niels Bohr Institute, University of Copenhagen, Blegdamsvej 17, 2100 København Ø, Denmark.
  • Chiantia S; Institute of Biochemistry and Biology, University of Potsdam, Karl-Liebknecht-Str. 24-25, 14476 Potsdam, Germany.
  • Daniels R; Division of Viral Products, Center for Biologics Evaluation and Research, Food and Drug Administration, Silver Spring, Maryland 20993, United States.
  • Bendix PM; Niels Bohr Institute, University of Copenhagen, Blegdamsvej 17, 2100 København Ø, Denmark.
Nano Lett ; 23(8): 3377-3384, 2023 04 26.
Article in English | MEDLINE | ID: covidwho-2317386
ABSTRACT
Many cellular processes involve the lateral organization of integral and peripheral membrane proteins into nanoscale domains. Despite the biological significance, the mechanisms that facilitate membrane protein clustering into nanoscale lipid domains remain enigmatic. In cells, the analysis of membrane protein phase affinity is complicated by the size and temporal nature of ordered and disordered lipid domains. To overcome these limitations, we developed a method for delivering membrane proteins from transfected cells into phase-separated model membranes that combines optical trapping with thermoplasmonic-mediated membrane fusion and confocal imaging. Using this approach, we observed clear phase partitioning into the liquid disordered phase following the transfer of GFP-tagged influenza hemagglutinin and neuraminidase from transfected cell membranes to giant unilamellar vesicles. The generic platform presented here allows investigation of the phase affinity of any plasma membrane protein which can be labeled or tagged with a fluorescent marker.
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Full text: Available Collection: International databases Database: MEDLINE Main subject: Influenza, Human / Spike Glycoprotein, Coronavirus Limits: Humans Language: English Journal: Nano Lett Year: 2023 Document Type: Article Affiliation country: Acs.nanolett.3c00371

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Full text: Available Collection: International databases Database: MEDLINE Main subject: Influenza, Human / Spike Glycoprotein, Coronavirus Limits: Humans Language: English Journal: Nano Lett Year: 2023 Document Type: Article Affiliation country: Acs.nanolett.3c00371