A glycosylated peptide in the West Nile virus envelope protein is immunogenic during equine infection

Hobson-Peters, Jody, Toye, Philip, Sanchez, Melissa D., Bossart, Katharine N., Wang, Lin-Fa, Clark, David C., Cheah, Wai Yuen and Hall, Roy A. (2008) A glycosylated peptide in the West Nile virus envelope protein is immunogenic during equine infection. Journal of General Virology, 89 12: 3063-3072. doi:10.1099/vir.0.2008/003731-0


Author Hobson-Peters, Jody
Toye, Philip
Sanchez, Melissa D.
Bossart, Katharine N.
Wang, Lin-Fa
Clark, David C.
Cheah, Wai Yuen
Hall, Roy A.
Title A glycosylated peptide in the West Nile virus envelope protein is immunogenic during equine infection
Journal name Journal of General Virology   Check publisher's open access policy
ISSN 0022-1317
Publication date 2008-12-01
Sub-type Article (original research)
DOI 10.1099/vir.0.2008/003731-0
Open Access Status Not Open Access
Volume 89
Issue 12
Start page 3063
End page 3072
Total pages 10
Place of publication Basingstoke, United Kingdom
Publisher Society for General Microbiolgoy
Language eng
Subject C1
110804 Medical Virology
070705 Veterinary Immunology
070712 Veterinary Virology
Abstract Using a monoclonal antibody directed to domain I of the West Nile virus (WNV) envelope (E) protein, we identified a continuous (linear) epitope that was immunogenic during WNV infection of horses. Using synthetic peptides, this epitope was mapped to a 19 aa sequence (WN19: E147-165) encompassing the WNV NY99 E protein glycosylation site at position 154. The inability of WNV-positive horse and mouse sera to bind the synthetic peptides indicated that glycosylation was required for recognition of peptide WN19 by WNV-specific antibodies in sera. N-linked glycosylation of WN19 was achieved through expression of the peptide as a C-terminal fusion protein in mammalian cells and specific reactivity of WNV-positive horse sera to the glycosylated WN19 fusion protein was shown by Western blot. Additional sera collected from horses infected with Murray Valley encephalitis virus (MVEV), which is similarly glycosylated at position Ell 54 and exhibits high sequence identity to WNV NY99 in this region, also recognized the recombinant peptide. Failure of most WNV- and MVEV-positive horse sera to recognize the epitope as a deglycosylated fusion protein confirmed that the N-linked glycan was important for antibody recognition of the peptide. Together, these results suggest that the induction of antibodies to the WN19 epitope during WNV infection of horses is generally associated with E protein glycosylation of the infecting viral strain.
Keyword Murray Valley Encephalitis
Recombinant Antigen
Yellow-fever Virus
Kunjin Virus
Microsphere Immunoassay
Monoclonal-antibodies
Diagnosis
Dna Vaccine
Ns1 Protein
Q-Index Code C1
Q-Index Status Confirmed Code

Document type: Journal Article
Sub-type: Article (original research)
Collections: 2009 Higher Education Research Data Collection
School of Chemistry and Molecular Biosciences
 
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Created: Tue, 31 Mar 2009, 00:36:51 EST by Jennifer Falknau on behalf of School of Chemistry & Molecular Biosciences