Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Tracking immunoglobulin variable-gene expression in HIV infection.

M Zouali1

  • 1Institut National de la Santé et de la Recherche Médicale (INSERM), Paris, France.

Applied Biochemistry and Biotechnology
|May 29, 2000
PubMed
Summary

Human immunodeficiency virus 1 (HIV-1) gp120 protein acts as a superantigen, depleting protective V(H)3+ antibodies. This deficiency in V(H)3+ antibodies is linked to faster disease progression in HIV-1 patients.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Frontiers in clinical immunology 2008.

Scandinavian journal of immunology·2009
Same author

A novel tissue engineering-based assay for immunological infertility.

Scandinavian journal of immunology·2008
Same author

Cellular interactions and signalling defects in lupus (1).

Lupus·2008
Same author

Paraneoplastic autoimmunity.

Polish journal of veterinary sciences·2007
Same author

Silent antibodies.

Archives de l'Institut Pasteur de Tunis·2006
Same author

[Werner's syndrome and endocrine disorders].

Annales d'endocrinologie·2003

Area of Science:

  • Immunology
  • Virology
  • Structural Biology

Background:

  • B-cell superantigens (SAgs) activate B cells via non-specific immunoglobulin (Ig) interactions.
  • The major envelope protein of HIV-1, gp120, exhibits SAg-like properties, potentially causing B-cell apoptosis and loss.
  • This interaction differs from gp120 binding to specific antibodies, which requires Ig tertiary structure.

Purpose of the Study:

  • To investigate the role of V(H)3+ antibodies in HIV-1 infection.
  • To determine if V(H)3+ antibody deficiency is associated with disease progression.
  • To elucidate the structural basis of the interaction between HIV-1 gp120 and human V(H)3+ Igs.

Main Methods:

  • Longitudinal examination of V(H)3+ antibody levels in HIV-1-infected individuals over 7 years.

Related Experiment Videos

  • Quantification of V(H)3+ antibodies in serum samples from slow and rapid progressors.
  • Analysis of structural correlates for gp120 binding to V(H)3+ Igs.

    • Main Results:

    • V(H)3+ antibodies specific for the gp120 SAg-binding site were deficient in HIV-1-infected subjects.
    • Paucity of V(H)3+ antibodies correlated with rapid clinical decline and AIDS progression.
    • Anti-gp160 V(H)3+ antibody levels decreased over time in progressors, varying with viral load.
    • gp120 interacts with a subset of V(H)3+ Igs, with specific amino acid positions in the heavy-chain variable regions being critical for binding.

    Conclusions:

    • V(H)3+ antibodies play a crucial protective role in HIV-1 infection.
    • Underexpression of V(H)3+ antibodies may accelerate HIV-1 disease progression.
    • HIV-1 gp120 acts as a viral SAg, inducing humoral deficiency by depleting a key B-cell repertoire subset and promoting apoptosis.