| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
1 Department of Genome Modifications and Cancer, Infection and Cancer Program, German Cancer Research Center (DKFZ), Im Neuenheimer Feld 242, 69120 Heidelberg, Germany
2 Departments of Pathology and Microbiology and Immunology, The Jake Gittlen Cancer Research Foundation, College of Medicine, Pennsylvania State University, Hershey, PA 17033, USA
Correspondence
Michael Pawlita
M.Pawlita{at}dkfz.de
Most anti-human papillomavirus (HPV) capsid antibody assays are based on virus-like particles (VLP). We evaluated glutathione S-transferase (GST)–L1 fusion proteins as ELISA antigens for determining type specificity and cross-reactivity of 92 VLP-specific monoclonal antibodies (mAb) generated against nine mucosal alpha papillomavirus types of species 7, 9 and 10. The antibody panel included 25 new mAb, and 24 previously published mAb are further characterized. We determined the cross-reactivity patterns with 15 different HPV types representing 6 species (alpha1, 2, 4, 7, 9 and 10) and neutralization and cross-neutralization properties with HPV types 6, 11, 16, 18 and 45. Eighty-nine (97 %) of the antibodies including 34, 71 and 14 recognizing neutralizing, conformational and linear epitopes, respectively, reacted with the GST–L1 protein of the HPV type used as immunogen, with log titres ranging from 2.0 to 7.3. Of these 89 antibodies, 52 % were monotypic, 20 % showed intra-species and 28 % inter-species cross-reactivity. Log neutralization titres to the immunogen HPV ranged from 1.7 to 5.6. A single cross-neutralizing mAb (H6.L12) was found. ELISA titres were always higher than neutralization titres. All neutralizing epitopes were conformational and mostly type-specific. Our data show that bacterially expressed, affinity-purified GST–L1 fusion proteins display a broad variety of epitopes and thus are well suited for detection of HPV antibodies. Cross-reactivity is associated with linear as well as conformational epitopes. Distantly related mucosal and skin alpha papillomaviruses share some conformational epitopes and the phylogenetic L1-based species definition may not define a serological unit since no species-specific epitope was found.
Present address: Joint DKFZ-EMBL Chemical Biology Core Facility, European Molecular Biology Laboratory (EMBL), Meyerhofstr. 1, 69117 Heidelberg, Germany.
This article has been cited by other articles:
|
|
 |
|
  L. Schadlich, T. Senger, B. Gerlach, N. Mucke, C. Klein, I. G. Bravo, M. Muller, and L. Gissmann Analysis of Modified Human Papillomavirus Type 16 L1 Capsomeres: the Ability To Assemble into Larger Particles Correlates with Higher Immunogenicity J. Virol., August 1, 2009; 83(15): 7690 - 7705. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 P. Randhawa, R. Viscidi, J. J. Carter, D. A. Galloway, T. D. Culp, C. Huang, B. Ramaswami, and N. D. Christensen Identification of species-specific and cross-reactive epitopes in human polyomavirus capsids using monoclonal antibodies J. Gen. Virol., March 1, 2009; 90(3): 634 - 639. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
N. Thones, A. Herreiner, L. Schadlich, K. Piuko, and M. Muller A Direct Comparison of Human Papillomavirus Type 16 L1 Particles Reveals a Lower Immunogenicity of Capsomeres than Viruslike Particles with Respect to the Induced Antibody Response J. Virol., June 1, 2008; 82(11): 5472 - 5485. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| INT J SYST EVOL MICROBIOL | MICROBIOLOGY | J GEN VIROL |
| J MED MICROBIOL | ALL SGM JOURNALS | |
