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Related Concept Videos

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...
Subviral Agents01:29

Subviral Agents

Subviral agents are infectious entities that resemble viruses but lack one or more viral components, such as a capsid or essential replication machinery. These agents include viroids, prions, and satellites, each possessing distinct structural and functional characteristics that influence their mode of infection and replication.Viroids are the simplest subviral agents, consisting of circular, single-stranded RNA molecules without a protein coat. They exclusively infect plants, relying entirely...
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...
Initiation of Translation02:33

Initiation of Translation

Initiating translation is complex because it involves multiple molecules. Initiator tRNA, ribosomal subunits, and eukaryotic initiation factors (eIFs) are all required to assemble on the initiation codon of mRNA. This process consists of several steps that are mediated by different eIFs.
First, the initiator tRNA must be selected from the pool of elongator tRNAs by eukaryotic initiation factor 2 (eIF2). The initiator tRNA (Met-tRNAi) has conserved sequence elements including modified bases at...
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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In situ Subcellular Fractionation of Adherent and Non-adherent Mammalian Cells
09:20

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Published on: July 23, 2010

Subunit interactions in bovine papillomavirus.

Matthias Wolf1, Robert L Garcea, Nikolaus Grigorieff

  • 1Jack and Eileen Connors Structural Biology Laboratory, Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, 250 Longwood Avenue, Boston, MA 02115, USA.

Proceedings of the National Academy of Sciences of the United States of America
|March 24, 2010
PubMed
Summary

Researchers determined the bovine papillomavirus capsid structure using cryo-electron microscopy. This reveals critical L1 protein arm interactions essential for viral assembly and infection.

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Area of Science:

  • Structural biology
  • Virology
  • Biophysics

Background:

  • Papillomaviruses are dsDNA viruses linked to epithelial growths and tumors.
  • Their capsids are composed of 72 L1 protein pentamers.

Purpose of the Study:

  • To determine the high-resolution structure of the bovine papillomavirus (BPV) capsid.
  • To elucidate the molecular interactions governing BPV capsid assembly and viral entry.

Main Methods:

  • Single-particle cryo-electron microscopy (cryoEM) was employed.
  • Analysis of approximately 4,000 particle images yielded a 3.6 Å resolution density map.

Main Results:

  • The L1 polypeptide chain trace was resolved, detailing N- and C-terminal arm associations between pentamers.
  • Specific C-terminal arm contacts, including a disulfide bond, were identified, refining previous structural models.
  • The study provides insights into the assembly mechanisms and infectious entry pathways of papillomaviruses.

Conclusions:

  • The determined BPV structure clarifies L1 subunit interactions crucial for capsid formation.
  • This work has implications for understanding viral assembly and infection.
  • It suggests the feasibility of high-resolution cryoEM reconstructions for asymmetric particles.