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Related Experiment Video

Updated: Mar 2, 2026

A Flow Cytometry-based Assay to Identify Compounds That Disrupt Binding of Fluorescently-labeled CXC Chemokine Ligand 12 to CXC Chemokine Receptor 4
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Study on CCR5 analogs and affinity peptides.

Yingping Wu1, Riqiang Deng, Wenyan Wu

  • 1Biopharmaceutical Centre, State Key Laboratory of Biocontrol, College of Life Sciences, Sun Yat-Sen University, Guangdong 510275, China.

Protein Engineering, Design & Selection : PEDS
|January 13, 2012
PubMed
Summary
This summary is machine-generated.

Researchers developed novel CCR5 analogs and high-affinity peptides to block HIV-1 entry. These tools target the chemokine receptor 5 (CCR5), a key player in HIV infection, offering potential for new antiviral therapies.

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Area of Science:

  • Molecular Biology
  • Virology
  • Immunology

Background:

  • The human chemokine receptor 5 (CCR5) is crucial for HIV-1 entry into host cells, binding to the viral glycoprotein gp120.
  • Naturally occurring CCR5 mutations, like CCR5 delta-32, highlight its potential as an HIV intervention target.
  • Developing high-affinity blocking peptides requires CCR5 analogs with similar conformations.

Purpose of the Study:

  • To create high-affinity peptides capable of blocking CCR5 interactions.
  • To generate and characterize recombinant CCR5 analogs for potential use as HIV antagonists.
  • To identify novel peptide antagonists for CCR5.

Main Methods:

  • Cloning of CCR5 N-terminal, extracellular loop 1, and extracellular loop 2 fragments into recombinant proteins (CCR5 N-Linker-E2, CCR5 mN-E1-E2).
  • High-yield expression and purification of CCR5 analogs in Escherichia coli using intein self-cleavage technology.
  • Epitope activity validation via immunoprecipitation and ELISA; screening of a phage random-peptide library.

Main Results:

  • Successful production of recombinant CCR5 analogs with confirmed epitope activity similar to natural CCR5.
  • Demonstrated applicability of CCR5 analogs as antagonists for chemokine ligands.
  • Identification of nine high-affinity polypeptides from a phage library acting as CCR5 peptide antagonists.

Conclusions:

  • The developed recombinant CCR5 analogs serve as valuable tools for studying CCR5 function and developing antagonists.
  • The identified affinity peptides represent promising candidates for blocking CCR5 and inhibiting HIV-1 infection.
  • This research provides a foundation for further investigation into mechanisms of HIV-1 inhibition via CCR5 antagonism.