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Related Concept Videos

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.
Fusion of Secretory Vesicles with the Plasma Membrane01:26

Fusion of Secretory Vesicles with the Plasma Membrane

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...
SNAREs and Membrane Fusion01:43

SNAREs and Membrane Fusion

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...
Vesicular Tubular Clusters01:45

Vesicular Tubular Clusters

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.
With the help of motor proteins such...
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...
Introduction to Virus01:28

Introduction to Virus

Viruses are unique biological entities that blur the boundary between living and non-living systems. Although they lack cellular structure and metabolic processes, they can exhibit characteristics of life when infecting a host. Their defining feature is a nucleic acid core, composed of either DNA or RNA, encapsulated within a protein coat called a capsid. This simple structure allows them to invade host cells and use their machinery for replication efficiently.Viral Structure and...

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Related Experiment Video

Updated: May 27, 2026

Methodology for the Efficient Generation of Fluorescently Tagged Vaccinia Virus Proteins
09:27

Methodology for the Efficient Generation of Fluorescently Tagged Vaccinia Virus Proteins

Published on: January 17, 2014

Structural Syntax of the Vaccinia Virus Entry-Fusion Complex.

Joshua N Sargeant1, Paul D Gershon1

  • 1Department of Molecular Biology and Biochemistry, University of California Irvine, Irvine, California, USA.

Proteomics
|May 26, 2026
PubMed
Summary
This summary is machine-generated.

Poxvirus cell entry involves an 11-chain entry-fusion complex (EFC). Computational modeling revealed its structure, including novel transmembrane bundles and a pseudo beta helical connector (PBHC), aiding in understanding virus-host interactions.

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Methodology for the Efficient Generation of Fluorescently Tagged Vaccinia Virus Proteins
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Area of Science:

  • Virology
  • Structural Biology
  • Computational Biology

Background:

  • Poxviruses utilize a unique, uncharacterized mechanism for cell entry.
  • This process involves an 11-chain entry-fusion complex (EFC) anchored to the viral envelope.

Purpose of the Study:

  • To computationally model the structure of the complete 11-chain entry-fusion complex (holoEFC).
  • To elucidate the structural organization and potential assembly pathways of the EFC.
  • To investigate the interaction of fusion inhibitor A26 with the EFC.

Main Methods:

  • Utilized AlphaFold for computational modeling of the holoEFC.
  • Integrated crosslinking mass spectrometry (XLMS) and monolink data for model validation.
  • Employed pDockQ, dG_separated, and dSASA for assessing subunit interface authenticity.
  • Applied quantitative protein mass spectrometry to determine subunit stoichiometry.

Main Results:

  • A computationally confident model of the holoEFC containing all 11 chains was generated.
  • Identified novel structural features: an 11-chain transmembrane bundle and a pseudo beta helical connector (PBHC).
  • The holoEFC model revealed two distinct subregions with mobility around the PBHC, and a potential assembly pathway for the subregion 2 hexamer.
  • Fusion inhibitor A26 was modeled in complex with EFC subcomplex A28:H2:A16:G9, primarily interacting with G9.
  • Subunits F9 and J5 were found to be sub-stoichiometric in mature Vaccinia virus preparations.

Conclusions:

  • The study provides a high-resolution computational model of the poxvirus EFC, offering insights into its unique cell entry mechanism.
  • The identified structural elements, including the PBHC, are critical for understanding EFC function and viral entry.
  • The findings lay the groundwork for developing novel antiviral strategies targeting poxvirus entry.