| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
Laboratoire de génétique des virus, CNRS, Avenue de la Terrasse, 91198 Gif-sur-Yvette Cédex, France
Nineteen yeast colonies secreting rabies virus glycoprotein (G) peptides immunoreactive with polyclonal anti-rabies virus sera were selected from a random expression library. The peptides, around 80 amino acids long, spanned amino acids 54–494 of the G protein. These peptides, together with two constructions including, respectively, immunodominant sites II and III, were analysed for their immunoreactivity with 40 anti-G protein monoclonal antibodies (MAbs) composed of 12 MAbs that reacted with SDS-treated protein in Western blot under reducing conditions (WB+) and 28 representative MAbs that did not react after denaturation (WB-). This last category represents 98% of anti-rabies virus G MAbs. None of the WB- MAbs bound peptides. Of the 12 WB+ MAbs, one bound two peptides situated before the transmembrane domain of the protein and six bound peptides overlapping a region situated between amino acids 223 and 276. These six MAbs define a new antigenic region that would be considered ‘immunodominant’ if the peptide strategy had been used to study the antigenicity of the protein; however, this region is only recognized by about 1% of our MAbs. Three of these WB+ MAbs had significant neutralizing activity; two were used for the selection of antigenic mutants (MAR mutants). Some mutants had a substitution within the region delimited by the peptides, confirming the pertinence of both the peptide and escape mutant approaches. However, a few mutants had a substitution outside the peptide-delimited region, suggesting that remote mutation(s) could affect epitope accessibility in the native protein.
* Author for correspondence. Fax +33 1 69 82 43 08.
Present address: Laboratoire de Virologie et Immunologie Moleculaires, Institut National de la Recherche Agronomique, F-78352 Jouy en Josas Cédex, France.
Received 14 July 1995;
accepted 28 September 1995.
This article has been cited by other articles:
|
|
 |
|
  S. Roche, F. A. Rey, Y. Gaudin, and S. Bressanelli Structure of the Prefusion Form of the Vesicular Stomatitis Virus Glycoprotein G Science, February 9, 2007; 315(5813): 843 - 848. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 L. Sissoeff, M. Mousli, P. England, and C. Tuffereau Stable trimerization of recombinant rabies virus glycoprotein ectodomain is required for interaction with the p75NTR receptor J. Gen. Virol., September 1, 2005; 86(9): 2543 - 2552. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
N. Johnson, K. L. Mansfield, and A. R. Fooks Canine vaccine recipients recognize an immunodominant region of the rabies virus glycoprotein J. Gen. Virol., November 1, 2002; 83(11): 2663 - 2669. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 C. Langevin and C. Tuffereau Mutations Conferring Resistance to Neutralization by a Soluble Form of the Neurotrophin Receptor (p75NTR) Map outside of the Known Antigenic Sites of the Rabies Virus Glycoprotein J. Virol., October 2, 2002; 76(21): 10756 - 10765. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
A. P. Maillard and Y. Gaudin Rabies virus glycoprotein can fold in two alternative, antigenically distinct conformations depending on membrane-anchor type J. Gen. Virol., June 1, 2002; 83(6): 1465 - 1476. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
H. Badrane and N. Tordo Host Switching in Lyssavirus History from the Chiroptera to the Carnivora Orders J. Virol., September 1, 2001; 75(17): 8096 - 8104. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
H. Badrane, C. Bahloul, P. Perrin, and N. Tordo Evidence of Two Lyssavirus Phylogroups with Distinct Pathogenicity and Immunogenicity J. Virol., April 1, 2001; 75(7): 3268 - 3276. [Abstract] [Full Text]
|
|
|
|
|
|
C. Jallet, Y. Jacob, C. Bahloul, A. Drings, E. Desmezieres, N. Tordo, and P. Perrin Chimeric Lyssavirus Glycoproteins with Increased Immunological Potential J. Virol., January 1, 1999; 73(1): 225 - 233. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
C. Tuffereau, J. Benejean, A.-M. R. Alfonso, A. Flamand, and M. C. Fishman Neuronal Cell Surface Molecules Mediate Specific Binding to Rabies Virus Glycoprotein Expressed by a Recombinant Baculovirus on the Surfaces of Lepidopteran Cells J. Virol., February 1, 1998; 72(2): 1085 - 1091. [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 | |
