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Identification of epitopes in the nucleocapsid protein of Nipah virus using a linear phage‐displayed random peptide library
Author(s) -
Eshaghi Majid,
Tan Wen Siang,
Yusoff Khatijah
Publication year - 2005
Publication title -
journal of medical virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 121
eISSN - 1096-9071
pISSN - 0146-6615
DOI - 10.1002/jmv.20249
Subject(s) - epitope , virology , biology , clone (java method) , virus , bacteriophage , antiserum , phage display , peptide library , antigen , antibody , linear epitope , peptide sequence , monoclonal antibody , microbiology and biotechnology , peptide , escherichia coli , gene , genetics , biochemistry
Abstract A random peptide library of heptamers displayed on the surface of M13 bacteriophage was used to identify specific epitopes of antibodies in pooled sera of swine naturally infected by Nipah virus. The selected heptapeptides were aligned with protein sequences of Nipah virus and several putative epitopes were identified within the nucleocapsid protein. A total of 41 of 60 (68%) selected phage clones had inserts resembling a region with the sequence SNRTQGE, located at the C‐terminal end (amino acids 503–509) of the nucleocapsid protein. The binding of antibodies in the swine and human antisera to the phage clone was inhibited by a synthetic peptide corresponding to this region. Epitopes identified by phage display are consistent with the predicted antigenic sites for the Nipah virus nucleocapsid protein. The selected phage clone used as a coating antigen discriminated swine and human Nipah virus sera‐positive from sera‐negative samples exhibiting characteristics, which might be attractive for diagnostic tests. J. Med. Virol. 75:147–152, 2005. © 2005 Wiley‐Liss, Inc.