Organizing the interface—Plasma membrane architecture and receptor dynamics in virus‐cell interactions

Plasma membranes are organized into dynamic nanoscale domains that regulate lipid and protein distribution, diffusion, and receptor availability. Because viruses act on similar length scales, this organization shapes early infection steps, including attachment, membrane exploration, receptor engagement, and entry. This review summarizes how pre-existing receptor nanoplatforms promote viral capture and how virus binding can remodel plasma membrane nanoarchitecture. Using influenza A virus and human immunodeficiency virus 1 as examples, we discuss how multivalent, low-affinity glycoprotein-glycan interactions exploit clustered attachment factors to increase avidity and tune receptor dynamics. We also address transbilayer lipid asymmetry and how its perturbation-particularly phosphatidylserine exposure and apoptotic mimicry-is exploited by enveloped viruses.

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Publication Details

Journal
FEBS Letters
Published
2026-04-27
DOI
https://doi.org/10.1002/1873-3468.70347
Primary Topic
Lipid Membrane Structure and Behavior
Type
article
Field-Weighted Citation Impact
0.00

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article

Organizing the interface—Plasma membrane architecture and receptor dynamics in virus‐cell interactions

Christian Sieben, Jan Schlegel
FEBS Letters
Lipid Membrane Structure and Behavior
article

Organizing the interface—Plasma membrane architecture and receptor dynamics in virus‐cell interactions

Christian Sieben, Jan Schlegel
article en

Abstract

Plasma membranes are organized into dynamic nanoscale domains that regulate lipid and protein distribution, diffusion, and receptor availability. Because viruses act on similar length scales, this organization shapes early infection steps, including attachment, membrane exploration, receptor engagement, and entry. This review summarizes how pre-existing receptor nanoplatforms promote viral capture and how virus binding can remodel plasma membrane nanoarchitecture. Using influenza A virus and human immunodeficiency virus 1 as examples, we discuss how multivalent, low-affinity glycoprotein-glycan interactions exploit clustered attachment factors to increase avidity and tune receptor dynamics. We also address transbilayer lipid asymmetry and how its perturbation-particularly phosphatidylserine exposure and apoptotic mimicry-is exploited by enveloped viruses.

FEBS Letters
Helmholtz Centre for Infection Research (DE), Technische Universität Braunschweig (DE)
Volkswagen Foundation, Niedersächsisches Ministerium für Wissenschaft und Kultur
Openalex Percentile: Top 8%
Lipid Membrane Structure and Behavior
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