Human papillomavirus type 6 virus-like particles present overlapping yet distinct conformational epitopes

1 Merck Research Laboratories, PO Box 4, West Point, PA 19486, USA 2 The Jake Gittlen Cancer Research Institute, Department of Pathology, Penn State University, Milton S. Hershey Medical Center, 500 University Drive, Hershey, PA 17033, USA Correspondence William McClements william_mcclements{at}merc...

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Bibliographic Details
Published in:Journal of general virology 2003-06, Vol.84 (6), p.1493-1497
Main Authors: Wang, Xin-Min, Cook, James C, Lee, Jessica C, Jansen, Kathrin U, Christensen, Neil D, Ludmerer, Steven W, McClements, William L
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Amino Acid Substitution
Antibodies, Monoclonal
Antigens, Viral - chemistry
Antigens, Viral - genetics
Cottontail rabbit papillomavirus
Cross Reactions
Epitope Mapping
Epitopes - chemistry
Epitopes - genetics
Human papillomavirus 6
Humans
Molecular Sequence Data
Mutagenesis, Site-Directed
Papillomaviridae - genetics
Papillomaviridae - immunology
Protein Conformation
Viral Proteins - chemistry
Viral Proteins - genetics
Viral Proteins - immunology
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Summary:1 Merck Research Laboratories, PO Box 4, West Point, PA 19486, USA 2 The Jake Gittlen Cancer Research Institute, Department of Pathology, Penn State University, Milton S. Hershey Medical Center, 500 University Drive, Hershey, PA 17033, USA Correspondence William McClements william_mcclements{at}merck.com The epitope for a human papillomavirus (HPV) type 6 conformation-dependent, neutralizing monoclonal antibody (mAb) was partially mapped using HPV L1 recombinant virus-like particles (VLPs). The mAb H6.J54 is cross-reactive with the closely related HPV types 6 and 11. By making HPV-6-like amino acid substitutions in the cottontail rabbit papillomavirus (CRPV) major capsid protein L1, we were able to transfer H6.J54 binding activity into a CRPV/HPV-6 hybrid L1 protein. Full binding activity was achieved with only nine amino acid changes and identified a region centred on the HPV-6 residues 49–54. This region has previously been shown to be a critical part of HPV-6 type-specific epitopes. Fine mapping of the region by scanning a series of alanine substitution mutations showed that in HPV-6 VLPs this type-common epitope overlaps HPV-6 type-specific epitopes.
ISSN:0022-1317
1465-2099
DOI:10.1099/vir.0.18872-0