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Related Concept Videos

Fusion of Secretory Vesicles with the Plasma Membrane01:26

Fusion of Secretory Vesicles with the Plasma Membrane

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Proteins and neurotransmitters in secretory vesicles can be released from a cell upon vesicle docking, priming, and fusion with the plasma membrane. Vesicles are docked and primed in preparation for the quick exocytosis of their contents in response to a stimulus. The fusion process is mainly carried out by a SNAP Receptor or SNARE complex, consisting of synaptobrevin, syntaxin-1, and SNAP-25.
In 1993, Jim Rothman proposed that the antiparallel pairing of vesicular and transmembrane SNAREs, or...
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SNAREs and Membrane Fusion01:43

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Once a transport vesicle has recognized its target organelle, the vesicular membrane needs to fuse with the target membrane to unload the cargo. Transmembrane proteins called SNAREs present on organelle membranes and their vesicles, mediate vesicle fusion.
SNAREs exist in pairs that symmetrically interact and catalyze the fusion of the lipid bilayers in vesicle and target organelle. v-SNARE in the vesicle membrane are single polypeptide chains that bind to a complementary t-SNARE, composed of 2...
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Clathrin Coated Vesicles01:12

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Clathrin-coated vesicles use endocytosis to transport receptors and lysosomal hydrolases from the Golgi to the lysosome in the late secretory pathway. Clathrin-mediated endocytosis was the first described endocytic process, and Clathrin-coated vesicles remain one of the most well-studied transport vesicles. The molecular machinery that generates clathrin-coated vesicles comprises over 50 proteins that precisely coordinate vesicle formation. Cell surface receptors concentrated in indented sites...
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Mechanisms of Membrane Domain Formation00:59

Mechanisms of Membrane Domain Formation

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Different physical properties of lipids and proteins allow them to localize and form distinct islands or domains in the membrane. Some membrane domains are formed due to protein-protein interactions, whereas others are formed due to the presence of specific lipids such as sphingolipids and sterols—for example, large proteins, such as bacteriorhodopsin, aggregate and create distinct domains.
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Vesicular Tubular Clusters01:45

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After budding out from the ER membrane, some COPII vesicles lose their coat and fuse with one another to form larger vesicles and interconnected tubules called vesicular tubular clusters or VTCs. These clusters constitute a compartment at the ER-Golgi interface known as ERGIC (Endoplasmic Reticulum Golgi Intermediate Compartment). The ERGIC is a mobile membrane-bound cargo transport system that sorts proteins secreted from ER and delivers them to the Golgi.
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Intralumenal Vesicles and Multivesicular Bodies01:38

Intralumenal Vesicles and Multivesicular Bodies

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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...
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Related Experiment Video

Updated: Mar 17, 2026

Method for Measurement of Viral Fusion Kinetics at the Single Particle Level
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Method for Measurement of Viral Fusion Kinetics at the Single Particle Level

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Membrane fusion during poxvirus entry.

Bernard Moss1

  • 1Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA.

Seminars in Cell & Developmental Biology
|July 18, 2016
PubMed
Summary
This summary is machine-generated.

Poxviruses use an eleven-protein Entry Fusion Complex (EFC) for cell entry, requiring specific pH activation and multiple proteins for fusion and viral DNA delivery into the host cytoplasm.

Keywords:
EndocytosisHemifusionMembrane fusionVaccinia virusVirus entry

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Area of Science:

  • Virology
  • Molecular Biology
  • Cell Biology

Background:

  • Poxviruses are large, enveloped DNA viruses with cytoplasmic replication.
  • They possess unique mechanisms for cell entry, differing from most DNA viruses.
  • Vaccinia virus serves as a model for studying poxvirus entry.

Purpose of the Study:

  • To elucidate the mechanism of poxvirus entry into host cells.
  • To detail the roles of proteins involved in the Entry Fusion Complex (EFC).
  • To understand the regulation of viral fusion and entry processes.

Main Methods:

  • Analysis of poxvirus Entry Fusion Complex (EFC) protein composition and interactions.
  • Investigation of the stages of viral entry: attachment, hemifusion, and core entry.
  • Examination of the role of pH and fusion repressors in viral entry.

Main Results:

  • The Entry Fusion Complex (EFC) comprises eleven proteins, conserved across poxviruses.
  • Nine EFC proteins are essential for complex stability, with at least eight required for hemifusion.
  • All eleven EFC proteins are necessary for core entry into the host cell.
  • Low pH activates fusion by removing repressors, and additional repressors prevent secondary infections.

Conclusions:

  • Poxvirus entry is a complex, multi-step process mediated by the EFC.
  • The EFC's structure and function are critical for viral infection.
  • Lack of structural data for most EFC proteins hinders a complete understanding of the fusion mechanism.