Related Experiment Video

Updated: May 10, 2026

Production of High-Titer Infectious Influenza Pseudotyped Particles with Envelope Glycoproteins from Highly Pathogenic H5N1 and Avian H7N9 Viruses
08:10

Production of High-Titer Infectious Influenza Pseudotyped Particles with Envelope Glycoproteins from Highly Pathogenic H5N1 and Avian H7N9 Viruses

Published on: January 15, 2020

Envelope protein dynamics in paramyxovirus entry

Philippe Plattet1, Richard K Plemper

  • 1Division of Neurological Sciences, DCR-VPH, Vetsuisse Faculty, University of Bern, Bern, Switzerland. philippe.plattet@vetsuisse.unibe.ch

Mbio
|July 4, 2013
PubMed

Insights

Paramyxoviruses use attachment and fusion (F) proteins for cell entry. Recent studies reveal how attachment proteins trigger F protein activation, improving understanding of viral entry and therapeutic development.

Area of Science:

  • Virology
  • Molecular Biology
  • Structural Biology

Background:

  • Paramyxoviruses are significant global pathogens impacting health and economy.
  • Cell entry relies on two surface glycoproteins: attachment and fusion (F) proteins.
  • Receptor-induced conformational changes in attachment proteins are thought to activate F protein.

Purpose of the Study:

  • To review recent findings on the paramyxovirus cell entry mechanism.
  • To elucidate the precise link between receptor engagement and F protein triggering.
  • To highlight similarities and differences in entry strategies across paramyxovirus family members.

Main Methods:

  • Review of recent structural and mechanistic studies on paramyxovirus entry.
  • Analysis of data from various paramyxovirus family members.
  • Synthesis of current understanding of viral cell adhesion and membrane fusion.

Main Results:

  • Recent reports have significantly advanced the understanding of the F protein triggering mechanism.
  • Key similarities and differences in entry strategies among paramyxoviruses are illuminated.
  • A broader mechanistic understanding of the paramyxovirus cell entry system is provided.

Conclusions:

  • Recent findings offer a comprehensive view of paramyxovirus cell entry.
  • Understanding the attachment protein's role in F triggering is crucial.
  • These insights pave the way for developing novel paramyxovirus therapeutics.

More Related Videos

Production of Pseudotyped Particles to Study Highly Pathogenic Coronaviruses in a Biosafety Level 2 Setting08:40

Production of Pseudotyped Particles to Study Highly Pathogenic Coronaviruses in a Biosafety Level 2 Setting

Published on: March 1, 2019

In Vitro Disassembly of Influenza A Virus Capsids by Gradient Centrifugation07:24

In Vitro Disassembly of Influenza A Virus Capsids by Gradient Centrifugation

Published on: March 27, 2016

Related Concept Videos

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...
Intracellular Movement of Viruses and Bacteria01:10

Intracellular Movement of Viruses and Bacteria

Intracellular bacteria and viruses often comprise a group of highly infectious pathogens that can cause several diseases. Bacterial pathogens include those belonging to the genus Rickettsia responsible for conditions such as rocky mountain spotted fever and the Mediterranean spotted fever; Chlamydia, a genus responsible for a sexually transmitted disease; Coxiella burnetii, an agent responsible for Q fever. Viral pathogens include vaccinia—a poxvirus, and herpes simplex virus—a virus that...
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...
Viral Structure00:56

Viral Structure

Viruses are extraordinarily diverse in shape and size, but they all have several structural features in common. All viruses have a core that contains a DNA- or RNA-based genome. The core is surrounded by a protective coat of proteins called the capsid. The capsid is composed of subunits called capsomeres. The capsid and genome-containing core are together known as the nucleocapsid.
Intralumenal Vesicles and Multivesicular Bodies01:38

Intralumenal Vesicles and Multivesicular Bodies

Intraluminal vesicles (ILVs) are small vesicles 50-80 nm in diameter formed during the maturation of early endosomes. A specialized endosome containing numerous ILVs is called a multivesicular body (MVB). ILVs contain internalized molecules such as antigens, nucleic acids, proteins, and metabolites. Some of these molecules are released from the MVBs inside exosomes and are transported to other cells. Other MVBs contain molecules that are retained in the ILVs and are later degraded within the...
Coat Assembly and GTPases01:33

Coat Assembly and GTPases

Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...