PMID: 8588324May 1, 1995Paper

Spot synthesis of overlapping peptides on paper membrane supports enables the identification of linear monoclonal antibody binding determinants on morbillivirus phosphoproteins

Veterinary Microbiology
W MartensB Liess

Abstract

In order to map antigenic domains on the P-protein of morbillivirus, a series of overlapping peptides, representing the P-protein sequences of phocid distemper virus strain 2558/Han88 and canine distemper virus strain Onderstepoort, were synthesized on a paper support by the spot-technique. The reactivity of six monoclonal antibodies with the peptides was tested in an enzyme immunoassay and compared to their reactivity in Western blots and in an ELISA using detergent extracts from virus-infected cells. Three linear determinants could be localized on the P-protein. Two antibody-binding sites were delineated within the C-terminal (between amino acids 307-322 and 382-400, respectively), and a third one was located on the N-terminal part (amino acids 13-31) of the protein. Fine mapping of this binding site revealed that this was a part of an antigenic domain. In Western blots, the monoclonal antibodies reacting with this domain also reacted with a second protein which was possibly the V-protein.

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Citations

Sep 19, 2002·Protein Science : a Publication of the Protein Society·Xavier EspanelRob Hooft van Huijsduijnen
Apr 22, 1999·Protein Science : a Publication of the Protein Society·M ValleJ P Albar
Jun 20, 2001·Journal of Virology·V von MesslingR Cattaneo
Dec 19, 2009·Biochimica Et Biophysica Acta·Christian K NicklWolfgang R Dostmann
Dec 7, 2007·Biotechnology & Genetic Engineering Reviews·Kai HilperRobert E W Hancock
Jan 1, 2015·Microarrays·Sarah Picaud, Panagis Filippakopoulos

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