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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...
Pinching-off of Coated Vesicles01:32

Pinching-off of Coated Vesicles

Vesicle budding is orchestrated by distinct cytosolic proteins such as adaptor proteins, coat proteins, and GTPases. To initiate vesicle budding, membrane-bending proteins containing crescent-shaped BAR domains bind to the lipid heads in the bilayer and distort the membrane to form a protein-coated vesicle bud. Adaptors proteins such as AP2 for clathrin-coated vesicles can nucleate on the deformed membrane. Finally, coat proteins such as clathrin or COPI and COPII assemble into a coat forming...
Inhibitors of Virion Maturation and Assembly01:19

Inhibitors of Virion Maturation and Assembly

As part of their replication cycle, certain viruses synthesize long precursor proteins called polyproteins within infected host cells. In human immunodeficiency virus (HIV), two major polyproteins are produced: Gag and Gag-Pol. The Gag polyprotein supplies the structural components of the virus, while Gag-Pol includes essential viral enzymes such as reverse transcriptase, integrase, and protease. After synthesis, these polyproteins move to the host cell membrane, where they assemble into an...
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...
Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...

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Related Experiment Video

Updated: Jun 5, 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

Influenza virus assembly and budding.

Jeremy S Rossman1, Robert A Lamb

  • 1Department of Molecular Biosciences, Northwestern University, Evanston, IL 60208-3500, USA.

Virology
|January 18, 2011
PubMed
Summary
This summary is machine-generated.

Influenza A virus assembly involves viral proteins HA and NA clustering in cell membranes, initiating budding. M1 and M2 proteins then facilitate virion structure formation and release, crucial for influenza virus replication.

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Purification and Visualization of Influenza A Viral Ribonucleoprotein Complexes
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Purification and Visualization of Influenza A Viral Ribonucleoprotein Complexes

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Simple and Robust in vivo and in vitro Approach for Studying Virus Assembly

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Last Updated: Jun 5, 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

Purification and Visualization of Influenza A Viral Ribonucleoprotein Complexes
09:35

Purification and Visualization of Influenza A Viral Ribonucleoprotein Complexes

Published on: February 9, 2009

Simple and Robust in vivo and in vitro Approach for Studying Virus Assembly
09:47

Simple and Robust in vivo and in vitro Approach for Studying Virus Assembly

Published on: March 1, 2012

Area of Science:

  • Virology
  • Cell Biology
  • Molecular Biology

Background:

  • Influenza A virus poses a significant global health threat, causing seasonal epidemics and pandemics.
  • It is an enveloped virus with a segmented negative-strand RNA genome.
  • Virus assembly and budding are critical for progeny virion release.

Purpose of the Study:

  • To provide a step-by-step analysis of influenza virus assembly and budding.
  • To review the latest research on the molecular mechanisms of influenza virus replication.

Main Methods:

  • Literature review of recent studies on influenza virus assembly and budding.
  • Analysis of the roles of viral proteins (HA, NA, M1, M2) in the budding process.

Main Results:

  • Hemagglutinin (HA) and neuraminidase (NA) proteins target lipid rafts, initiating membrane deformation and budding.
  • Matrix protein 1 (M1) polymerizes to form the virion interior and recruits RNPs and M2.
  • M2 protein stabilizes budding sites, facilitates matrix polymerization, and mediates membrane scission for virion release.

Conclusions:

  • Influenza virus assembly and budding are complex, multi-step processes orchestrated by viral proteins within lipid rafts.
  • Understanding these mechanisms is key to developing antiviral strategies targeting influenza virus replication.