Academic Journal

Investigation of the immunogenicity of Zika glycan loop

التفاصيل البيبلوغرافية
العنوان: Investigation of the immunogenicity of Zika glycan loop
المؤلفون: Elizabeth A. Henderson, Christina C. Tam, Luisa W. Cheng, Annie Elong Ngono, Anh-Viet Nguyen, Sujan Shresta, Matt McGee, Hal Padgett, Laurence K. Grill, Mikhail Martchenko Shilman
المصدر: Virology Journal, Vol 17, Iss 1, Pp 1-15 (2020)
بيانات النشر: BMC, 2020.
سنة النشر: 2020
المجموعة: LCC:Infectious and parasitic diseases
مصطلحات موضوعية: Zika, Envelope, Glycan loop, Neutralizing antibodies, Infectious and parasitic diseases, RC109-216
الوصف: Abstract Background Zika virus (ZIKV) is a major human pathogen and member of the Flavivirus genus. Previous studies have identified neutralizing antibodies from Zika patients that bind to quaternary epitopes across neighboring envelope (E) proteins, called E dimer epitopes (EDE). An asparagine-linked glycan on the “glycan loop” (GL) of the ZIKV envelope protein protects the functionally important “fusion loop” on the opposite E subunit in the dimer, and EDE antibodies have been shown to bind to both of these loops. Human EDE antibodies have been divided into two subclasses based on how they bind to the glycan loop region: EDE1 antibodies do not require glycosylation for binding, while EDE2 antibodies strongly rely on the glycan for binding. Methods ZIKV GL was expressed on tobacco mosaic virus nanoparticles. Mice were immunized with GL or full-length monomeric E and the immune response was analyzed by testing the ability of sera and monoclonal antibodies to bind to GL and to neutralize ZIKV in in vitro cellular assay. Results We report here the existence of ZIKV moderately neutralizing antibodies that bind to E monomers through epitopes that include the glycan loop. We show that sera from human Zika patients contain antibodies capable of binding to the unglycosylated glycan loop in the absence of the rest of the envelope protein. Furthermore, mice were inoculated with recombinant E monomers and produced neutralizing antibodies that either recognize unglycosylated glycan loop or require glycan for their binding to monomeric E. We demonstrate that both types of antibodies neutralize ZIKV to some extent in a cellular virus neutralization assay. Conclusions Analogous to the existing EDE antibody nomenclature, we propose a new classification for antibodies that bind to E monomer epitopes (EME): EME1 and EME2 for those that do not require and those that do require glycan for binding to E, respectively.
نوع الوثيقة: article
وصف الملف: electronic resource
اللغة: English
تدمد: 1743-422X
Relation: http://link.springer.com/article/10.1186/s12985-020-01313-1; https://doaj.org/toc/1743-422X
DOI: 10.1186/s12985-020-01313-1
URL الوصول: https://doaj.org/article/af3aec39c2b44a8c931ebf64741ed72b
رقم الانضمام: edsdoj.f3aec39c2b44a8c931ebf64741ed72b
قاعدة البيانات: Directory of Open Access Journals
الوصف
تدمد:1743422X
DOI:10.1186/s12985-020-01313-1