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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...
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Stabilizing the HIV-1 envelope glycoprotein State 2A conformation.

Dani Vézina1,2, Shang Yu Gong1,3, William D Tolbert4

  • 1Centre de Recherche du CHUM, Montreal, QC, Canada.

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|December 10, 2020
PubMed
Summary

Stabilizing the HIV-1 Env State 2A conformation, which makes infected cells vulnerable to antibody-dependent cellular cytotoxicity (ADCC), requires all three gp120 subunits to bind soluble CD4 (sCD4) or CD4 mimetics (CD4mc) and anti-coreceptor binding site (CoRBS) antibodies.

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Area of Science:

  • Virology
  • Immunology
  • Structural Biology

Background:

  • The HIV-1 envelope glycoprotein (Env) trimer exists in a metastable state, sampling various conformations.
  • Env transitions from an antibody-resistant closed state (State 1) to more open states upon CD4 binding.
  • Specific antibody binding can stabilize an antibody-vulnerable conformation (State 2A), enabling antibody-dependent cellular cytotoxicity (ADCC).

Purpose of the Study:

  • To determine the precise stoichiometry of components required for stabilizing the HIV-1 Env State 2A conformation.
  • To elucidate the sequential binding events leading to the stabilization of Env State 2A.

Main Methods:

  • Utilized a cell-based ELISA (CBE) assay.
  • Employed a "trimer mixing" approach combining wild-type and functionally impaired Env subunits.
  • Evaluated the individual contributions of CD4 mimetics (CD4mc), soluble CD4 (sCD4), anti-coreceptor binding site (CoRBS) antibodies, and anti-cluster A antibodies.

Main Results:

  • Optimal stabilization of Env State 2A necessitates binding of all three gp120 subunits by both sCD4/CD4mc and anti-CoRBS antibodies.
  • Subsequent binding of anti-cluster A antibodies to two of these subunits further stabilizes the conformation.
  • Demonstrated that simultaneous engagement of all three gp120 subunits by CD4-binding agents and anti-CoRBS antibodies is critical.

Conclusions:

  • The study provides a detailed understanding of the molecular requirements for stabilizing the antibody-vulnerable HIV-1 Env State 2A conformation.
  • Stabilizing Env State 2A enhances susceptibility to ADCC, suggesting potential therapeutic strategies.
  • Findings offer insights into optimizing therapeutic cocktails for HIV-1 treatment by targeting specific Env conformations.