Role of BC loop residues in structure, function and antigenicity of the West Nile virus envelope protein receptor-binding domain III

Shuliu Zhang; Evgeniy I. Bovshik; Rodrigo Maillard; Gregory D. Gromowski; David E. Volk; Catherine H. Schein; Claire Y.H. Huang; David G. Gorenstein; James Lee; Alan D.T. Barrett; David W.C. Beasley

doi:10.1016/j.virol.2010.03.038

Role of BC loop residues in structure, function and antigenicity of the West Nile virus envelope protein receptor-binding domain III

Shuliu Zhang, Evgeniy I. Bovshik, Rodrigo Maillard, Gregory D. Gromowski, David E. Volk, Catherine H. Schein, Claire Y.H. Huang, David G. Gorenstein, James Lee, Alan D.T. Barrett, David W.C. Beasley

Research output: Contribution to journal › Article › peer-review

25 Scopus citations

Abstract

Site-directed mutagenesis of residues in the BC loop (residues 329-333) of the envelope (E) protein domain III in a West Nile virus (WNV) infectious clone and in plasmids encoding recombinant WNV and dengue type 2 virus domain III proteins demonstrated a critical role for residues in this loop in the function and antigenicity of the E protein. This included a strict requirement for the tyrosine at residue 329 of WNV for virus viability and E domain III folding. The absence of an equivalent residue in this region of yellow fever group viruses and most tick-borne flavivirus suggests there is an evolutionary divergence in the molecular mechanisms of domain III folding employed by different flaviviruses.

Original language	English (US)
Pages (from-to)	85-91
Number of pages	7
Journal	Virology
Volume	403
Issue number	1
DOIs	https://doi.org/10.1016/j.virol.2010.03.038
State	Published - Jul 2010

Keywords

Attenuation
Envelope protein
Flavivirus
Neutralization
Receptor binding domain
West Nile virus

ASJC Scopus subject areas

Virology

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10.1016/j.virol.2010.03.038

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Zhang, S., Bovshik, E. I., Maillard, R., Gromowski, G. D., Volk, D. E., Schein, C. H., Huang, C. Y. H., Gorenstein, D. G., Lee, J., Barrett, A. D. T., & Beasley, D. W. C. (2010). Role of BC loop residues in structure, function and antigenicity of the West Nile virus envelope protein receptor-binding domain III. Virology, 403(1), 85-91. https://doi.org/10.1016/j.virol.2010.03.038

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title = "Role of BC loop residues in structure, function and antigenicity of the West Nile virus envelope protein receptor-binding domain III",

abstract = "Site-directed mutagenesis of residues in the BC loop (residues 329-333) of the envelope (E) protein domain III in a West Nile virus (WNV) infectious clone and in plasmids encoding recombinant WNV and dengue type 2 virus domain III proteins demonstrated a critical role for residues in this loop in the function and antigenicity of the E protein. This included a strict requirement for the tyrosine at residue 329 of WNV for virus viability and E domain III folding. The absence of an equivalent residue in this region of yellow fever group viruses and most tick-borne flavivirus suggests there is an evolutionary divergence in the molecular mechanisms of domain III folding employed by different flaviviruses.",

keywords = "Attenuation, Envelope protein, Flavivirus, Neutralization, Receptor binding domain, West Nile virus",

author = "Shuliu Zhang and Bovshik, {Evgeniy I.} and Rodrigo Maillard and Gromowski, {Gregory D.} and Volk, {David E.} and Schein, {Catherine H.} and Huang, {Claire Y.H.} and Gorenstein, {David G.} and James Lee and Barrett, {Alan D.T.} and Beasley, {David W.C.}",

note = "Funding Information: This work was supported by NIH ( R21 AI063468 to D.W.C.B.) and by the Pediatric Dengue Vaccine Initiative (to A.D.T.B.). We thank Drs. Rich Kinney (CDC) and Alexey Gribenko (UTMB) for helpful advice and review of the manuscript. ",

year = "2010",

month = jul,

doi = "10.1016/j.virol.2010.03.038",

language = "English (US)",

volume = "403",

pages = "85--91",

journal = "Virology",

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AU - Zhang, Shuliu

AU - Bovshik, Evgeniy I.

AU - Maillard, Rodrigo

AU - Gromowski, Gregory D.

AU - Volk, David E.

AU - Schein, Catherine H.

AU - Huang, Claire Y.H.

AU - Gorenstein, David G.

AU - Lee, James

AU - Barrett, Alan D.T.

AU - Beasley, David W.C.

N1 - Funding Information: This work was supported by NIH ( R21 AI063468 to D.W.C.B.) and by the Pediatric Dengue Vaccine Initiative (to A.D.T.B.). We thank Drs. Rich Kinney (CDC) and Alexey Gribenko (UTMB) for helpful advice and review of the manuscript.

PY - 2010/7

Y1 - 2010/7

N2 - Site-directed mutagenesis of residues in the BC loop (residues 329-333) of the envelope (E) protein domain III in a West Nile virus (WNV) infectious clone and in plasmids encoding recombinant WNV and dengue type 2 virus domain III proteins demonstrated a critical role for residues in this loop in the function and antigenicity of the E protein. This included a strict requirement for the tyrosine at residue 329 of WNV for virus viability and E domain III folding. The absence of an equivalent residue in this region of yellow fever group viruses and most tick-borne flavivirus suggests there is an evolutionary divergence in the molecular mechanisms of domain III folding employed by different flaviviruses.

AB - Site-directed mutagenesis of residues in the BC loop (residues 329-333) of the envelope (E) protein domain III in a West Nile virus (WNV) infectious clone and in plasmids encoding recombinant WNV and dengue type 2 virus domain III proteins demonstrated a critical role for residues in this loop in the function and antigenicity of the E protein. This included a strict requirement for the tyrosine at residue 329 of WNV for virus viability and E domain III folding. The absence of an equivalent residue in this region of yellow fever group viruses and most tick-borne flavivirus suggests there is an evolutionary divergence in the molecular mechanisms of domain III folding employed by different flaviviruses.

KW - Attenuation

KW - Envelope protein

KW - Flavivirus

KW - Neutralization

KW - Receptor binding domain

KW - West Nile virus

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Role of BC loop residues in structure, function and antigenicity of the West Nile virus envelope protein receptor-binding domain III

Abstract

Keywords

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