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 Concept Videos

You might also read

Related Articles

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

Sort by
Same author

Making Sense from Structure: What the Immune System Sees in Viral RNA.

Viruses·2026
Same author

Ribosome-induced mRNA pseudoknot interactions visualized by DMS MaP-Seq.

bioRxiv : the preprint server for biology·2025
Same author

Correction: Immunogenicity of differentially glycosylated Marburg virus glycoproteins expressed in mammalian and insect cells.

Virology journal·2025
Same author

DUSP11 is an Intracellular Innate Immune Checkpoint in Lung Adenocarcinoma.

Cancer immunology research·2025
Same author

Immunogenicity of differentially glycosylated Marburg virus glycoproteins expressed in mammalian and insect cells.

Virology journal·2025
Same author

Characterization of an mRNA-Encoded Antibody Against Henipavirus.

Current issues in molecular biology·2025
Same journal

Nanotechnology to Break the Antimicrobial Resistance.

ACS infectious diseases·2026
Same journal

Influenza A Virus Binding to α,2-3- and α,2-8-Linked Sialo-Gangliosides Reconstituted in Phase-Separated Vesicles.

ACS infectious diseases·2026
Same journal

<i>In Vivo</i> Activity of Antimicrobial Peptoid Oligomers against HSV-1 in a Mouse Model of Herpes Labialis.

ACS infectious diseases·2026
Same journal

Antimicrobial Peptides and Biofilms: From Molecular Interactions to Therapeutic Control.

ACS infectious diseases·2026
Same journal

Comparative Phenotypic Screening Identifies Protein Synthesis Inhibitors as Compounds That Enhance Early Acidification of <i>Mycobacterium tuberculosis</i> in Macrophages.

ACS infectious diseases·2026
Same journal

Correction to "<i>Treponema pallidum</i> Flagellin FlaB3 Activates Inflammation and Inhibits Autophagy in HMC3 Cells via the TLR4 Pathway".

ACS infectious diseases·2026
See all related articles

Related Experiment Video

Updated: Jun 20, 2025

Development of Cell-type specific anti-HIV gp120 aptamers for siRNA delivery
13:47

Development of Cell-type specific anti-HIV gp120 aptamers for siRNA delivery

Published on: June 23, 2011

19.6K

A Branched SELEX Approach Identifies RNA Aptamers That Bind Distinct HIV-1 Capsid Structural Components.

Paige R Gruenke1,2,3, Miles D Mayer2, Rachna Aneja1

  • 1Department of Molecular Microbiology and Immunology, University of Missouri, Columbia, Missouri 65212, United States.

ACS Infectious Diseases
|July 17, 2024
PubMed
Summary
This summary is machine-generated.

Researchers developed aptamers targeting specific structures of the HIV-1 capsid protein (CA). These aptamers enable purification of CA, offering new tools to study HIV-1 replication and host interactions.

More Related Videos

Nucleocapsid Annealing-Mediated Electrophoresis NAME Assay Allows the Rapid Identification of HIV-1 Nucleocapsid Inhibitors
08:33

Nucleocapsid Annealing-Mediated Electrophoresis NAME Assay Allows the Rapid Identification of HIV-1 Nucleocapsid Inhibitors

Published on: January 19, 2015

8.9K
Exploring Sequence Space to Identify Binding Sites for Regulatory RNA-Binding Proteins
11:34

Exploring Sequence Space to Identify Binding Sites for Regulatory RNA-Binding Proteins

Published on: August 9, 2019

6.6K

Related Experiment Videos

Last Updated: Jun 20, 2025

Development of Cell-type specific anti-HIV gp120 aptamers for siRNA delivery
13:47

Development of Cell-type specific anti-HIV gp120 aptamers for siRNA delivery

Published on: June 23, 2011

19.6K
Nucleocapsid Annealing-Mediated Electrophoresis NAME Assay Allows the Rapid Identification of HIV-1 Nucleocapsid Inhibitors
08:33

Nucleocapsid Annealing-Mediated Electrophoresis NAME Assay Allows the Rapid Identification of HIV-1 Nucleocapsid Inhibitors

Published on: January 19, 2015

8.9K
Exploring Sequence Space to Identify Binding Sites for Regulatory RNA-Binding Proteins
11:34

Exploring Sequence Space to Identify Binding Sites for Regulatory RNA-Binding Proteins

Published on: August 9, 2019

6.6K

Area of Science:

  • Virology
  • Molecular Biology
  • Biochemistry

Background:

  • The HIV-1 capsid protein (CA) exists in multiple structures during replication, influencing its function and interactions.
  • Understanding the role of distinct CA structures is crucial for HIV-1 research but technically challenging.

Purpose of the Study:

  • To develop novel tools for studying HIV-1 CA structural forms.
  • To identify aptamers with specificity for different CA conformations.

Main Methods:

  • Utilized a branched SELEX approach to select aptamers targeting HIV-1 CA.
  • Evaluated aptamer binding specificities to CA lattice and hexamer forms.
  • Demonstrated aptamer-mediated affinity purification of CA from cell lysates.

Main Results:

  • Identified aptamers with varying specificities for HIV-1 CA structural forms.
  • Characterized aptamer binding regions and structural features.
  • Successfully purified biologically relevant CA forms using aptamers.

Conclusions:

  • Structural form-specific aptamers are valuable tools for studying HIV-1 CA.
  • Aptamer-mediated purification facilitates research without altering virus or host components.