The DE loop of the domain III of the envelope protein appears to be associated with West Nile virus neutralization.
The envelope (E) protein of WNV plays an important role in the virus neutralization. Using a mAb 5E8, a neutralizing epitope on the domain III of the E of the New York strain of WN virus was characterized. Results from neutralization-escape mutants and site-directed mutagenesis revealed that the 5E8 epitope is a highly conformation dependent epitope consisting of at least residues E330, E332 and E367 on the domain III. Besides known critical neutralizing epitopes E330 and E332, our results indicate that residue E367, a component of DE loop on the domain III, appeared to be associated with neutralization but little with neuroinvasion of the virus, as reported previously (Beasley et al., 2002).
Choi
Kang-Seuk
KS
Foreign Animal Disease Division, National Veterinary Research and Quarantine Service, 480 Anyang-6 Dong, Anyang, Gyeonggi 430-824, Republic of Korea. choiks@nvrqs.go.kr
Nah
Jin-Ju
JJ
Ko
Young-Joon
YJ
Kim
Yong-Joo
YJ
Joo
Yi-Seok
YS
D016056:Immunodominant Epitopes / Q000276:immunology*; D008958:Models, Molecular; D009500:Neutralization Tests; D017434:Protein Structure, Tertiary / Q000502:physiology; D014759:Viral Envelope Proteins / Q000737:chemistry / Q000276:immunology*; D014902:West Nile virus / Q000276:immunology*
D016056:Immunodominant Epitopes; D014759:Viral Envelope Proteins