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Related Concept Videos

Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

14.7K
The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
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Coat Assembly and GTPases01:33

Coat Assembly and GTPases

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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...
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Protein Complex Assembly02:41

Protein Complex Assembly

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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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Bacterial Protein Maturation01:26

Bacterial Protein Maturation

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Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...
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Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

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After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...
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Related Experiment Video

Updated: Apr 27, 2026

Studies of Chaperone-Cochaperone Interactions using Homogenous Bead-Based Assay
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Studies of Chaperone-Cochaperone Interactions using Homogenous Bead-Based Assay

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Hsp90: a chaperone for HIV-1.

Jun Siong Low1, Ariberto Fassati1

  • 1The Wohl Virion Centre, MRC Centre for Medical Molecular Virology,Division of Infection & Immunity, UCL, Cruciform Building, 90 Gower Street, London WC1E 6BT,UK.

Parasitology
|July 10, 2014
PubMed
Summary

Heat shock protein 90 (Hsp90) significantly aids human immunodeficiency virus type 1 (HIV-1) replication by promoting gene expression and viral transcription. Hsp90 inhibitors, tested for cancer, may offer new HIV-1 treatment strategies.

Area of Science:

  • Molecular Biology
  • Virology
  • Immunology

Background:

  • Heat shock protein 90 (Hsp90) is a crucial chaperone protein involved in cellular homeostasis.
  • Recent research highlights Hsp90's emerging role in human immunodeficiency virus type 1 (HIV-1) infection.
  • Understanding host-pathogen interactions is key to developing novel therapeutic strategies.

Purpose of the Study:

  • To elucidate the multifaceted roles of Hsp90 in the HIV-1 life cycle.
  • To explore the potential of Hsp90 as a therapeutic target for HIV-1 infection.

Main Methods:

  • Review of existing literature on Hsp90 function and its involvement in HIV-1 replication.
  • Analysis of Hsp90's molecular mechanisms, including gene expression, promoter localization, and complex activation.

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Author Spotlight: Exploring the Role of Unfolded Protein Response in HIV-1 Replication and Infectivity
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Related Experiment Videos

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  • Consideration of Hsp90's role in viral mutation buffering and immune response modulation.

    • Main Results:

    • Hsp90 promotes HIV-1 gene expression in infected cells and localizes to the viral promoter DNA.
    • Hsp90 enhances HIV-1 replication under hyperthermia and activates the essential P-TEFb transcription complex.
    • Hsp90 influences viral core stability and modulates innate and acquired immune responses to HIV-1.

    Conclusions:

    • Hsp90 is a critical host factor supporting multiple stages of the HIV-1 life cycle.
    • Hsp90 inhibitors, currently in clinical trials for cancer, show promise for inhibiting HIV-1 infection.
    • Targeting Hsp90 offers a potential multi-pronged strategy for combating HIV-1.