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Related Concept Videos

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Tail-anchoring of Proteins in the ER Membrane

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Related Experiment Video

Updated: Jun 8, 2026

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Specific Interactions between HIV-1 Env Cytoplasmic Tail and Gag Matrix Domain Probed by NMR.

Manish Chaubey1, Hailong Gao2,3, Christy L Lavine4

  • 1Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115, United States.

Journal of the American Chemical Society
|May 14, 2025
PubMed
Summary

The HIV-1 envelope glycoprotein (Env) interacts with the Gag matrix protein (MA) at the plasma membrane. This interaction, mediated by Env's cytoplasmic tail, is crucial for recruiting Env during viral assembly and ensuring infectivity.

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Area of Science:

  • Virology
  • Structural Biology
  • Biochemistry

Background:

  • HIV-1 envelope glycoprotein (Env) mediates viral entry and requires proper incorporation during assembly for infectivity.
  • The interaction between Env and the Gag matrix protein (MA) has been hypothesized to facilitate Env recruitment to the plasma membrane, but direct evidence is lacking.

Purpose of the Study:

  • To provide direct biochemical and structural evidence for the interaction between HIV-1 Env and MA in a membrane-like environment.
  • To elucidate the specific structural contacts and interaction mechanisms between Env's cytoplasmic tail (CT) and MA during viral assembly.

Main Methods:

  • Nuclear Magnetic Resonance (NMR) chemical shift perturbation
  • Intermolecular paramagnetic relaxation enhancements
  • Microscale thermophoresis
  • Utilized bicelles to mimic a lipid bilayer environment

Main Results:

  • Specific structural contacts were identified between the trimeric Env CT and trimeric MA in bicelles.
  • The interaction is primarily electrostatic, involving acidic residues in the Env CT and positively charged patches on MA.
  • Mutating these acidic residues in Env significantly reduced viral infectivity.

Conclusions:

  • The cytoplasmic tail of HIV-1 Env directly interacts with the MA domain of Gag in a membrane-like environment.
  • This specific CT-MA interaction plays a critical structural role in recruiting Env during HIV-1 assembly.
  • The findings provide a mechanistic understanding of Env incorporation essential for viral infectivity.