Please use this identifier to cite or link to this item: http://hdl.handle.net/20.500.12779/3818
Title: HPLC immunoaffinity purification of rabies virus glycoprotein using immobilized antipeptide antibodies.
Authors: Santucci, Annalisa 
Rustici, M
Bracci, Luisa
Lozzi, Luisa
Soldani, Patrizia 
Neri, P.
Issue Date: 1990
Project: None 
Journal: JOURNAL OF IMMUNOLOGICAL METHODS
Abstract: 
It has been reported that the acetylcholine receptor may be used by the rabies virus to concentrate at sites in proximal to peripheral nerves. It has also been reported that the binding site for the receptor is located within the 190-203 region of the virus glycoprotein on the basis of its structural homology with the toxic center of snake neurotoxins, which are well known cholinergic ligands. We prepared monoclonal antibodies against the synthetic tetradecapeptide having the same sequence as the putative binding site of the rabies virus. One of three antibodies (clone 2PV 36-74) was able to recognize both the whole virus and its peplomeric glycoprotein and could bind acetylcholine. It was also able to inhibit the binding both of alpha-bungarotoxin and rabies virus glycoprotein to the acetylcholine receptor. We have covalently bound 2PV 36-74 to an HPLC affinity column and utilized it for specific purification of rabies virus glycoprotein. The immunoaffinity chromatographic method we describe is very sensitive and highly specific. Moreover this procedure does not denature the sample and is vary rapid and efficient
Description: 
56804
URI: http://hdl.handle.net/20.500.12779/3818
ISSN: 0022-1759
Appears in Collections:Publications

Show full item record

Page view(s)

1
Last Week
0
Last month
0
checked on May 17, 2021

Google ScholarTM

Check


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.