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Heparan sulfate proteoglycans interact exclusively with conformationally intact HPV L1 assemblies: Basis for a virus-like particle ELISA

Rommel, O; Dillner, Joakim LU ; Fligge, C; Bergsdorf, C; Wang, Xiaohong LU ; Selinka, HC and Sapp, M (2005) In Journal of Medical Virology 75(1). p.114-121
Abstract
In this article, we demonstrate that interaction of human papillomavirus-like particles (HPV-VLPs) with the putative glucosaminoglycan binding receptor is strictly dependent on conformational integrity. Such conformations are present on VLPs and capsomeres but not on monomers of the major capsid protein, L1, confirming reports that capsomeres can induce virus-neutralizing antibodies. Furthermore, we show the suitability of this specific interaction for development of VLP-based enzyme-linked immunosorbent assays (ELISAs), using heparin for indirect coupling of VLPs to microtiter plates, which may add an intrinsic quality control. This avoids presentation of linear, often highly cross-reactive epitopes of L1. In addition, heparin... (More)
In this article, we demonstrate that interaction of human papillomavirus-like particles (HPV-VLPs) with the putative glucosaminoglycan binding receptor is strictly dependent on conformational integrity. Such conformations are present on VLPs and capsomeres but not on monomers of the major capsid protein, L1, confirming reports that capsomeres can induce virus-neutralizing antibodies. Furthermore, we show the suitability of this specific interaction for development of VLP-based enzyme-linked immunosorbent assays (ELISAs), using heparin for indirect coupling of VLPs to microtiter plates, which may add an intrinsic quality control. This avoids presentation of linear, often highly cross-reactive epitopes of L1. In addition, heparin specifically interacts with a wide variety of HPV types, making it a prime candidate for a universal capture molecule. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
epidemiology, VLPs, conformational epitope, papillomavirus, receptor binding
in
Journal of Medical Virology
volume
75
issue
1
pages
114 - 121
publisher
John Wiley & Sons
external identifiers
  • pmid:15543569
  • wos:000225408900017
  • scopus:9644302502
ISSN
1096-9071
DOI
10.1002/jmv.20245
language
English
LU publication?
yes
id
d5bbca3a-1ab6-405a-840e-a3206234808a (old id 259591)
date added to LUP
2007-08-14 15:26:04
date last changed
2017-08-06 03:30:32
@article{d5bbca3a-1ab6-405a-840e-a3206234808a,
  abstract     = {In this article, we demonstrate that interaction of human papillomavirus-like particles (HPV-VLPs) with the putative glucosaminoglycan binding receptor is strictly dependent on conformational integrity. Such conformations are present on VLPs and capsomeres but not on monomers of the major capsid protein, L1, confirming reports that capsomeres can induce virus-neutralizing antibodies. Furthermore, we show the suitability of this specific interaction for development of VLP-based enzyme-linked immunosorbent assays (ELISAs), using heparin for indirect coupling of VLPs to microtiter plates, which may add an intrinsic quality control. This avoids presentation of linear, often highly cross-reactive epitopes of L1. In addition, heparin specifically interacts with a wide variety of HPV types, making it a prime candidate for a universal capture molecule.},
  author       = {Rommel, O and Dillner, Joakim and Fligge, C and Bergsdorf, C and Wang, Xiaohong and Selinka, HC and Sapp, M},
  issn         = {1096-9071},
  keyword      = {epidemiology,VLPs,conformational epitope,papillomavirus,receptor binding},
  language     = {eng},
  number       = {1},
  pages        = {114--121},
  publisher    = {John Wiley & Sons},
  series       = {Journal of Medical Virology},
  title        = {Heparan sulfate proteoglycans interact exclusively with conformationally intact HPV L1 assemblies: Basis for a virus-like particle ELISA},
  url          = {http://dx.doi.org/10.1002/jmv.20245},
  volume       = {75},
  year         = {2005},
}