scholarly journals Solution Structure and Antibody Binding Studies of the Envelope Protein Domain III from the New York Strain of West Nile Virus

2004 ◽  
Vol 279 (37) ◽  
pp. 38755-38761 ◽  
Author(s):  
David E. Volk ◽  
David W. C. Beasley ◽  
Deborah A. Kallick ◽  
Michael R. Holbrook ◽  
Alan D. T. Barrett ◽  
...  
Keyword(s):  
New York ◽  
West Nile Virus ◽  
Envelope Protein ◽  
Solution Structure ◽  
Antibody Binding ◽  
Protein Domain ◽  
Binding Studies ◽  
West Nile ◽  
Domain Iii

scholarly journals Solution structure and neutralizing antibody binding studies of domain III of the dengue‐2 virus envelope protein

2008 ◽  
Vol 70 (3) ◽  
pp. 1116-1119 ◽  
Author(s):  
Kuo‐Chun Huang ◽  
Ming‐Che Lee ◽  
Chih‐Wei Wu ◽  
Kao‐Jean Huang ◽  
Huan‐Yao Lei ◽  
...  
Keyword(s):  
Envelope Protein ◽  
Solution Structure ◽  
Neutralizing Antibody ◽  
Antibody Binding ◽  
Binding Studies ◽  
Virus Envelope ◽  
Virus Envelope Protein ◽  
Domain Iii

scholarly journals Structural basis for Zika envelope domain III recognition by a germline version of a recurrent neutralizing antibody

2020 ◽  
Vol 117 (18) ◽  
pp. 9865-9875
Author(s):  
Shannon R. Esswein ◽  
Harry B. Gristick ◽  
Andrea Jurado ◽  
Avery Peace ◽  
Jennifer R. Keeffe ◽  
...  
Keyword(s):  
West Nile Virus ◽  
Envelope Protein ◽  
Yellow Fever Virus ◽  
Cross Reactivity ◽  
Affinity Maturation ◽  
Protein Domain ◽  
Structural Basis ◽  
Maturation Process ◽  
West Nile ◽  
Domain Iii

Recent epidemics demonstrate the global threat of Zika virus (ZIKV), a flavivirus transmitted by mosquitoes. Although infection is usually asymptomatic or mild, newborns of infected mothers can display severe symptoms, including neurodevelopmental abnormalities and microcephaly. Given the large-scale spread, symptom severity, and lack of treatment or prophylaxis, a safe and effective ZIKV vaccine is urgently needed. However, vaccine design is complicated by concern that elicited antibodies (Abs) may cross-react with other flaviviruses that share a similar envelope protein, such as dengue virus, West Nile virus, and yellow fever virus. This cross-reactivity may worsen symptoms of a subsequent infection through Ab-dependent enhancement. To better understand the neutralizing Ab response and risk of Ab-dependent enhancement, further information on germline Ab binding to ZIKV and the maturation process that gives rise to potently neutralizing Abs is needed. Here we use binding and structural studies to compare mature and inferred-germline Ab binding to envelope protein domain III of ZIKV and other flaviviruses. We show that affinity maturation of the light-chain variable domain is important for strong binding of the recurrent VH3-23/VK1-5 neutralizing Abs to ZIKV envelope protein domain III, and identify interacting residues that contribute to weak, cross-reactive binding to West Nile virus. These findings provide insight into the affinity maturation process and potential cross-reactivity of VH3-23/VK1-5 neutralizing Abs, informing precautions for protein-based vaccines designed to elicit germline versions of neutralizing Abs.

scholarly journals Long Range Communication in the Envelope Protein Domain III and Its Effect on the Resistance of West Nile Virus to Antibody-mediated Neutralization

2007 ◽  
Vol 283 (1) ◽  
pp. 613-622 ◽  
Author(s):  
Rodrigo A. Maillard ◽  
Matthew Jordan ◽  
David W. C. Beasley ◽  
Alan D. T. Barrett ◽  
J. Ching Lee
Keyword(s):  
West Nile Virus ◽  
Long Range ◽  
Envelope Protein ◽  
Protein Domain ◽  
West Nile ◽  
Domain Iii ◽  
Long Range Communication

scholarly journals Plasticity of a critical antigenic determinant in the West Nile virus NY99 envelope protein domain III

Virology ◽  
2016 ◽  
Vol 496 ◽  
pp. 97-105 ◽  
Author(s):  
Jessica A. Plante ◽  
Maricela Torres ◽  
Claire Y.-H. Huang ◽  
David W.C. Beasley
Keyword(s):  
West Nile Virus ◽  
Envelope Protein ◽  
Antigenic Determinant ◽  
Protein Domain ◽  
The West ◽  
West Nile ◽  
Domain Iii

scholarly journals Identification of Neutralizing Epitopes within Structural Domain III of the West Nile Virus Envelope Protein

2002 ◽  
Vol 76 (24) ◽  
pp. 13097-13100 ◽  
Author(s):  
David W. C. Beasley ◽  
Alan D. T. Barrett
Keyword(s):  
New York ◽  
Monoclonal Antibodies ◽  
West Nile Virus ◽  
Envelope Protein ◽  
Structural Domain ◽  
Virus Envelope ◽  
West Nile ◽  
Virus Envelope Protein ◽  
Domain Iii ◽  
Virus Strains

ABSTRACT Using a panel of neutralizing monoclonal antibodies, we have mapped epitopes in domain III of the envelope protein of the New York strain of West Nile virus. The ability of monoclonal antibodies that recognize these epitopes to neutralize virus appeared to differ between lineage I and II West Nile virus strains, and epitopes were located on the upper surface of domain III at residues E307, E330, and E332.

scholarly journals A Plant-Produced Virus-Like Particle Displaying Envelope Protein Domain III Elicits an Immune Response Against West Nile Virus in Mice

2021 ◽  
Vol 12 ◽  
Author(s):  
Jennifer Stander ◽  
Aleyo Chabeda ◽  
Edward P. Rybicki ◽  
Ann E. Meyers
Keyword(s):  
West Nile Virus ◽  
Envelope Protein ◽  
One Health ◽  
Vaccine Candidate ◽  
Protein Domain ◽  
West Nile ◽  
Health Initiative ◽  
Virus Like Particle ◽  
The One ◽  
Domain Iii

West Nile virus (WNV) is a globally disseminated Flavivirus that is associated with encephalitis outbreaks in humans and horses. The continuous global outbreaks of West Nile disease in the bird, human, and horse populations, with no preventative measures for humans, pose a major public health threat. The development of a vaccine that contributes to the “One Health” Initiative could be the answer to prevent the spread of the virus and control human and animal disease. The current commercially available veterinary vaccines are generally costly and most require high levels of biosafety for their manufacture. Consequently, we explored making a particulate vaccine candidate made transiently in plants as a more cost-effective and safer means of production. A WNV virus-like particle-display-based vaccine candidate was generated by the use of the SpyTag/SpyCatcher (ST/SC) conjugation system. The WNV envelope protein domain III (EDIII), which contains WNV-specific epitopes, was fused to and displayed on AP205 phage virus-like particles (VLPs) following the production of both separately in Nicotiana benthamiana. Co-purification of AP205 and EDIII genetically fused to ST and SC, respectively, resulted in the conjugated VLPs displaying EDIII with an average coupling efficiency of 51%. Subcutaneous immunisation of mice with 5 μg of purified AP205: EDIII VLPs elicited a potent IgG response to WNV EDIII. This study presents the potential plants being used as biofactories for making significant pharmaceutical products for the “One Health” Initiative and could be used to address the need for their local production in low- and middle-income countries (LMICs).

The DE loop of the domain III of the envelope protein appears to be associated with West Nile virus neutralization

2007 ◽  
Vol 123 (2) ◽  
pp. 216-218 ◽  
Author(s):  
Kang-Seuk Choi ◽  
Jin-Ju Nah ◽  
Young-Joon Ko ◽  
Yong-Joo Kim ◽  
Yi-Seok Joo
Keyword(s):  
West Nile Virus ◽  
Envelope Protein ◽  
Virus Neutralization ◽  
West Nile ◽  
Domain Iii
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