scholarly journals A broadly neutralizing germline-like human monoclonal antibody against dengue virus envelope domain III

2019 ◽  
Vol 15 (6) ◽  
pp. e1007836 ◽  
Author(s):  
Dan Hu ◽  
Zhongyu Zhu ◽  
Shun Li ◽  
Yongqiang Deng ◽  
Yanling Wu ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Dengue Virus ◽  
Human Monoclonal Antibody ◽  
Virus Envelope ◽  
Domain Iii

scholarly journals Residues in domain III of the dengue virus envelope glycoprotein involved in cell-surface glycosaminoglycan binding

2012 ◽  
Vol 93 (1) ◽  
pp. 72-82 ◽  
Author(s):  
Daniel Watterson ◽  
Bostjan Kobe ◽  
Paul R. Young
Keyword(s):  
Cell Surface ◽  
Dengue Virus ◽  
Site Directed Mutagenesis ◽  
Cell Surface Receptor ◽  
Protein Fusion ◽  
Virus Envelope ◽  
Putative Receptor ◽  
E Protein ◽  
Surface Receptor ◽  
Domain Iii

The dengue virus (DENV) envelope (E) protein mediates virus entry into cells via interaction with a range of cell-surface receptor molecules. Cell-surface glycosaminoglycans (GAGs) have been shown to play an early role in this interaction, and charged oligosaccharides such as heparin bind to the E protein. We have examined this interaction using site-directed mutagenesis of a recombinant form of the putative receptor-binding domain III of the DENV-2E protein expressed as an MBP (maltose-binding protein)-fusion protein. Using an ELISA-based GAG-binding assay, cell-based binding analysis and antiviral-activity assays, we have identified two critical residues, K291 and K295, that are involved in GAG interactions. These studies have also demonstrated differential binding between mosquito and human cells.

scholarly journals Immunogenicity and Efficacy of Zika Virus Envelope Domain III in DNA, Protein, and ChAdOx1 Adenoviral-Vectored Vaccines

Vaccines ◽  
2020 ◽  
Vol 8 (2) ◽  
pp. 307 ◽  
Author(s):  
César López-Camacho ◽  
Giuditta De Lorenzo ◽  
Jose Luis Slon-Campos ◽  
Stuart Dowall ◽  
Peter Abbink ◽  
...  
Keyword(s):  
Immune Responses ◽  
Dengue Virus ◽  
Zika Virus ◽  
Neutralizing Antibodies ◽  
Vaccine Candidate ◽  
Protein Domain ◽  
Virus Envelope ◽  
Zikv Infection ◽  
Domain Iii ◽  
Open Question

The flavivirus envelope protein domain III (EDIII) was an effective immunogen against dengue virus (DENV) and other related flaviviruses. Whether this can be applied to the Zika virus (ZIKV) vaccinology remains an open question. Here, we tested the efficacy of ZIKV-EDIII against ZIKV infection, using several vaccine platforms that present the antigen in various ways. We provide data demonstrating that mice vaccinated with a ZIKV-EDIII as DNA or protein-based vaccines failed to raise fully neutralizing antibodies and did not control viremia, following a ZIKV challenge, despite eliciting robust antibody responses. Furthermore, we showed that ZIKV-EDIII encoded in replication-deficient Chimpanzee adenovirus (ChAdOx1-EDIII) elicited anti-ZIKV envelope antibodies in vaccinated mice but also provided limited protection against ZIKV in two physiologically different mouse challenge models. Taken together, our data indicate that contrary to what was shown for other flaviviruses like the dengue virus, which has close similarities with ZIKV-EDIII, this antigen might not be a suitable vaccine candidate for the correct induction of protective immune responses against ZIKV.

Dengue virus envelope protein domain III-elicited antibodies mediate cross-protection against Zika virus in a mouse model

2020 ◽  
Vol 278 ◽  
pp. 197882
Author(s):  
Yongchao Zhou ◽  
Dong Chen ◽  
Lan Yang ◽  
Weiwei Zou ◽  
Zhiliang Duan ◽  
...  
Keyword(s):  
Mouse Model ◽  
Dengue Virus ◽  
Zika Virus ◽  
Envelope Protein ◽  
Cross Protection ◽  
Protein Domain ◽  
Virus Envelope ◽  
Virus Envelope Protein ◽  
Domain Iii

scholarly journals Suppressive effect of dengue virus envelope protein domain III on megakaryopoiesis

Virulence ◽  
2017 ◽  
Vol 8 (8) ◽  
pp. 1719-1731 ◽  
Author(s):  
Guan-Ling Lin ◽  
Hsin-Hou Chang ◽  
Te-Sheng Lien ◽  
Po-Kong Chen ◽  
Hao Chan ◽  
...  
Keyword(s):  
Dengue Virus ◽  
Envelope Protein ◽  
Suppressive Effect ◽  
Protein Domain ◽  
Virus Envelope ◽  
Virus Envelope Protein ◽  
Domain Iii

scholarly journals Comparison of Plaque- and Enzyme-Linked Immunospot-Based Assays To Measure the Neutralizing Activities of Monoclonal Antibodies Specific to Domain III of Dengue Virus Envelope Protein

2011 ◽  
Vol 19 (1) ◽  
pp. 73-78 ◽  
Author(s):  
Lidong Liu ◽  
Kun Wen ◽  
Jie Li ◽  
Dongmei Hu ◽  
Yanfen Huang ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Dengue Virus ◽  
Envelope Protein ◽  
Neutralizing Antibodies ◽  
Large Scale ◽  
Immunofluorescence Assay ◽  
Virus Envelope ◽  
Virus Envelope Protein ◽  
Domain Iii ◽  
Microneutralization Test

ABSTRACTThe plaque reduction neutralization test (PRNT) is used widely to measure the neutralization activity of anti-dengue virus (DENV) antibodies, but it is time-consuming and labor-intensive and has low sample throughput. For fast and convenient measurement of neutralizing antibodies, especially in evaluating the efficiency of the DENV vaccines on a large scale, a new method is needed to replace PRNT. In recent decades, several microneutralization assays have been developed to overcome the limitations of PRNT. In the present study, we evaluated one of these, the enzyme-linked immunospot microneutralization test (ELISPOT-MNT), in comparison with PRNT. ELISPOT-MNT is performed in 96-well format, and the plaques are developed after 2 to 4 days using an ELISA to transform them into spots, which are detected automatically with an ELISPOT instrument. The assay is faster than PRNT, has a high throughput, and is more objective. We used 10 monoclonal antibodies (MAbs) against domain III of the DENV envelope protein (EDIII) to evaluate the two assays; all of these MAbs cross-react with all four serotypes of DENV as measured by immunofluorescence assay. The two neutralization assays were performed simultaneously to measure the 50% inhibitory concentration (IC50) of these MAbs. Using PRNT as the reference and treating IC50values higher than 50 μg/ml of MAbs as negative, ELISPOT-MNT showed a sensitivity of 95.6% and specificity of 88.24% when 10 MAbs were tested against four DENV serotype strains. A good correlation (R2= 0.672;P= 0.000) was observed between the two assays, making ELISPOT-MNT a potentially valuable method for measure of neutralizing antibodies against DENV.

Expression, purification and characterization of in vivo biotinylated dengue virus envelope domain III based tetravalent antigen

2010 ◽  
Vol 74 (1) ◽  
pp. 99-105 ◽  
Author(s):  
Gaurav Batra ◽  
Sheikh Mohd. Talha ◽  
Satish Kumar Nemani ◽  
Nisha Dhar ◽  
Sathyamangalam Swaminathan ◽  
...  
Keyword(s):  
Dengue Virus ◽  
Purification And Characterization ◽  
Virus Envelope ◽  
Domain Iii
Sign in / Sign up

Export Citation Format

Share Document