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Related Concept Videos

Influenza01:27

Influenza

Influenza is an acute, highly communicable viral disease that affects the respiratory tract and is responsible for seasonal epidemics worldwide. Influenza A is the most prevalent type associated with widespread outbreaks and is subtyped based on two surface glycoproteins: hemagglutinin (H) and neuraminidase (N), as in H1N1. These glycoproteins are essential for viral infectivity, transmission, and immune recognition. Transmission occurs primarily through respiratory droplets and contaminated...
Inhibitors Of Virion Release01:25

Inhibitors Of Virion Release

Viral replication and dissemination rely on efficient mechanisms for host cell entry, genome replication, assembly, and release. Influenza viruses, such as types A and B, are negative-sense single-stranded RNA viruses with a segmented genome, that depend on two critical surface glycoproteins to carry out these processes: hemagglutinin (HA) and neuraminidase (NA). HA initiates infection by binding to sialic acid residues on the surface of host epithelial cells, facilitating receptor-mediated...
Leaky Scanning02:28

Leaky Scanning

During most eukaryotic translation processes, the small 40S ribosome subunit scans an mRNA from its 5' end until it encounters the first start AUG codon. The large 60S ribosomal subunit then joins the smaller one to initiate protein synthesis. The location of the translation initiation is largely determined by the nucleotides near the start codon as there may be multiple translation initiation sites present on the mRNA.  Marilyn Kozak discovered that the sequence RCCAUGG (where R stands for...
Mechanisms of Membrane-bending01:15

Mechanisms of Membrane-bending

The living membranes are flexible due to their fluid mosaic nature; however, their bending into different shapes is an active process regulated by specific lipids and proteins. The membrane bending can be transient as seen in vesicles or stable for a long time as in microvilli. Cells regulate the size, location, and duration of the membrane curvature.
Membrane bending can happen due to intrinsic changes in lipid composition or extrinsic association with different proteins. The proteins involved...
Formation of Lipopolysaccharides01:19

Formation of Lipopolysaccharides

Lipopolysaccharides (LPS) are crucial components of the outer membrane of Gram-negative bacteria, serving both structural and functional roles. It contributes to membrane stability and protects bacteria from host immune responses. LPS is composed of three major regions—lipid A, a core oligosaccharide, and an O antigen. The biosynthesis and assembly of LPS involve a highly coordinated set of enzymatic reactions and transport mechanisms. Additionally, LPS is recognized as an endotoxin, triggering...
Receptor-mediated Endocytosis01:38

Receptor-mediated Endocytosis

Overview

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Updated: Jun 4, 2026

In Vitro Disassembly of Influenza A Virus Capsids by Gradient Centrifugation
07:24

In Vitro Disassembly of Influenza A Virus Capsids by Gradient Centrifugation

Published on: March 27, 2016

Bending and puncturing the influenza lipid envelope.

Sai Li1, Frederic Eghiaian1, Christian Sieben2

  • 1Drittes Physikalisches Institut, Georg-August-Universität, Göttingen, Germany.

Biophysical Journal
|February 2, 2011
PubMed
Summary

Influenza virus lipid envelopes are surprisingly soft and highly deformable, offering robust protection comparable to protein shells. This flexibility is key to safeguarding the viral genome.

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Area of Science:

  • Biophysics
  • Virology
  • Materials Science

Background:

  • Natural nanocontainers like vesicles and viruses utilize lipid bilayers for protection and content exchange.
  • Understanding the mechanical properties of viral envelopes is crucial for comprehending viral stability and infection mechanisms.

Purpose of the Study:

  • To investigate the mechanical properties of the influenza virus lipid envelope.
  • To determine the deformability and puncture resistance of influenza liposomes.
  • To compare the protective capacity of lipid envelopes with viral protein shells.

Main Methods:

  • Atomic force microscopy (AFM) was used to probe the mechanical response of influenza liposomes to applied forces.
  • Finite element modeling (FEM) was employed to analyze liposome deformation and extract elastic properties of the lipid bilayer.
  • Forces up to 0.2 nN were applied, causing up to 20% elastic deformation, and puncture forces exceeding 1 nN were measured.

Main Results:

  • Influenza liposomes exhibit significantly lower stiffness than expected for a gel phase bilayer, indicating high deformability.
  • Liposome stiffness increased gradually and weakly with temperature, consistent with a lack of major phase transition.
  • Influenza envelopes demonstrated remarkable resilience, withstanding significant deformation and requiring substantial force (>1 nN) to puncture.

Conclusions:

  • The influenza virus lipid envelope is highly flexible and mechanically robust.
  • This lipid envelope provides protection for the viral genome comparable to rigid protein shells.
  • The mechanical properties of the influenza lipid envelope may play a significant role in viral survival and infectivity.