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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.
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...
Antibody Structure01:10

Antibody Structure

Overview
Antibodies, also known as immunoglobulins (Ig), are essential players of the adaptive immune system. These antigen-binding proteins are produced by B cells and make up 20 percent of the total blood plasma by weight. In mammals, antibodies fall into five different classes, which each elicits a different biological response upon antigen binding.
The Y-Shaped Structure of Antibodies Consists of Four Polypeptide Chains
Antibodies consist of four polypeptide chains: two identical heavy...
Size and Structure of Viral Genomes01:26

Size and Structure of Viral Genomes

Viral genomes exhibit remarkable diversity in size, structure, and composition, influencing their replication strategies and interactions with host cells. These genomes consist of either DNA or RNA and may be linear or circular. Additionally, they can be single-stranded or double-stranded, with each configuration affecting how the virus propagates within a host. RNA viruses, for instance, generally have smaller genomes than DNA viruses, a factor that contributes to their high mutation rates and...

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Related Experiment Video

Updated: Jun 17, 2026

Assessment of Immunologically Relevant Dynamic Tertiary Structural Features of the HIV-1 V3 Loop Crown R2 Sequence by ab initio Folding
10:50

Assessment of Immunologically Relevant Dynamic Tertiary Structural Features of the HIV-1 V3 Loop Crown R2 Sequence by ab initio Folding

Published on: September 15, 2010

Challenges for structure-based HIV vaccine design.

William R Schief1, Yih-En Andrew Ban, Leonidas Stamatatos

  • 1Department of Biochemistry, University of Washington, Seattle, USA. schief@u.washington.edu

Current Opinion in HIV and AIDS
|January 6, 2010
PubMed
Summary
This summary is machine-generated.

Designing effective HIV vaccines remains challenging. New structural insights into the HIV envelope trimer and broadly neutralizing antibodies offer guidance for developing improved immunogens to elicit potent immune responses.

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Production of E. coli-expressed Self-Assembling Protein Nanoparticles for Vaccines Requiring Trimeric Epitope Presentation

Published on: August 21, 2019

Area of Science:

  • Structural biology
  • Immunology
  • Virology

Background:

  • The human immunodeficiency virus (HIV) envelope trimer is the primary target for neutralizing antibodies.
  • Broadly neutralizing antibodies (bNAbs) can neutralize diverse HIV strains by targeting conserved epitopes.
  • Previous attempts to elicit bNAbs through immunization have been unsuccessful.

Purpose of the Study:

  • To review structural information on the native HIV envelope trimer.
  • To analyze known epitopes for bNAbs.
  • To guide the design of more effective immunogens for HIV vaccine development.

Main Methods:

  • Cryo-electron tomography was used to determine the low-resolution structure of the native HIV-1 envelope trimer on virions.
  • High-resolution crystal structures of monomeric gp120 complexed with neutralizing ligands were fitted into cryo-electron density maps.
  • Epitope mapping of HIV-positive sera was performed to identify targets of bNAb responses.

Main Results:

  • The immune system can mount potent bNAb responses against conserved HIV envelope elements.
  • Structural models of the native virion trimer and neutralization mechanisms were generated.
  • Steric and geometric constraints faced by antibodies targeting conserved HIV epitopes were clarified.

Conclusions:

  • Despite the ability of the immune system to generate bNAbs, all immunization strategies to date have failed to elicit them.
  • Structural insights into the HIV envelope trimer and bNAb-epitope interactions provide critical information for future vaccine design.
  • Understanding these constraints is crucial for developing successful HIV vaccines.