Related Experiment Videos
Human papillomavirus type 6 virus-like particles present overlapping yet distinct conformational epitopes
Xin-Min Wang1, James C Cook1, Jessica C Lee1
1Merck Research Laboratories, PO Box 4, West Point, PA 19486, USA.
The Journal of General Virology
|May 29, 2003
Summary
Researchers mapped a human papillomavirus (HPV) type 6 neutralizing antibody epitope using virus-like particles (VLPs). Nine amino acid changes in a hybrid protein transferred antibody binding, pinpointing a key epitope region.
Area of Science:
- Virology
- Immunology
- Structural Biology
Background:
- Human papillomavirus (HPV) type 6 is a common oncogenic virus.
- Neutralizing monoclonal antibodies (mAbs) are crucial for HPV therapeutic and diagnostic development.
- Understanding HPV epitopes is key to vaccine and drug design.
Purpose of the Study:
- To map the epitope recognized by a neutralizing monoclonal antibody (mAb) H6.J54 targeting human papillomavirus (HPV) type 6.
- To identify specific amino acid residues responsible for mAb binding and cross-reactivity with HPV type 11.
Main Methods:
- Utilized HPV L1 recombinant virus-like particles (VLPs) for epitope mapping.
- Constructed hybrid L1 proteins with cottontail rabbit papillomavirus (CRPV) and HPV-6 amino acid substitutions.
- Employed alanine scanning mutagenesis to fine-map the epitope region.
Main Results:
- Transferred mAb H6.J54 binding activity to a CRPV/HPV-6 hybrid L1 protein with nine amino acid substitutions.
- Identified an epitope region centered on HPV-6 residues 49-54.
- Demonstrated that this type-common epitope overlaps with HPV-6 type-specific epitopes.
Conclusions:
- The study successfully mapped a conformational epitope for a neutralizing HPV-6 mAb.
- Residues 49-54 in HPV-6 L1 are critical for mAb H6.J54 binding and contribute to type-common epitopes.
- Findings advance the understanding of HPV-antibody interactions and epitope structure.