scholarly journals Characterization of Dengue Virus Complex-Specific Neutralizing Epitopes on Envelope Protein Domain III of Dengue 2 Virus

2008 ◽  
Vol 82 (17) ◽  
pp. 8828-8837 ◽  
Author(s):  
Gregory D. Gromowski ◽  
Nicholas D. Barrett ◽  
Alan D. T. Barrett
Keyword(s):  
Dengue Virus ◽  
Critical Role ◽  
Antigenic Site ◽  
Protein Domain ◽  
Virus Infectivity ◽  
E Proteins ◽  
Mutant Proteins ◽  
Virus Complex ◽  
Domain Iii

ABSTRACT The surface of the mature dengue virus (DENV) particle is covered with 180 envelope (E) proteins arranged as homodimers that lie relatively flat on the virion surface. Each monomer consists of three domains (ED1, ED2, and ED3), of which ED3 contains the critical neutralization determinant(s). In this study, a large panel of DENV-2 recombinant ED3 mutant proteins was used to physically and biologically map the epitopes of five DENV complex-specific monoclonal antibodies (MAbs). All five MAbs recognized a single antigenic site that includes residues K310, I312, P332, L389, and W391. The DENV complex antigenic site was located on an upper lateral surface of ED3 that was distinct but overlapped with a previously described DENV-2 type-specific antigenic site on ED3. The DENV complex-specific MAbs required significantly higher occupancy levels of available ED3 binding sites on the virion, compared to DENV-2 type-specific MAbs, in order to neutralize virus infectivity. Additionally, there was a great deal of variability in the neutralization efficacy of the DENV complex-specific MAbs with representative strains of the four DENVs. Overall, the differences in physical binding and potency of neutralization observed between DENV complex- and type-specific MAbs in this study demonstrate the critical role of the DENV type-specific antibodies in the neutralization of virus infectivity.

Paradoxical Role of Dengue Virus Envelope Protein Domain III Antibodies in Dengue Virus Infection

2020 ◽  
Vol 30 (3) ◽  
pp. 199-206
Author(s):  
Sheeza Ali ◽  
Samia Afzal ◽  
Muhammad Zubair Yousaf ◽  
Muhammad Shahid ◽  
Iram Amin ◽  
...  
Keyword(s):  
Virus Infection ◽  
Dengue Virus ◽  
Envelope Protein ◽  
Protein Domain ◽  
Virus Envelope ◽  
Dengue Virus Infection ◽  
Virus Envelope Protein ◽  
Domain Iii

scholarly journals Dengue virus neutralization by human immune sera: Role of envelope protein domain III-reactive antibody

Virology ◽  
2009 ◽  
Vol 392 (1) ◽  
pp. 103-113 ◽  
Author(s):  
W.M.P.B. Wahala ◽  
Annette A. Kraus ◽  
Laura B. Haymore ◽  
Mary Ann Accavitti-Loper ◽  
Aravinda M. de Silva
Keyword(s):  
Dengue Virus ◽  
Envelope Protein ◽  
Protein Domain ◽  
Virus Neutralization ◽  
Human Immune ◽  
Domain Iii ◽  
Reactive Antibody

scholarly journals Critical role of Dengue Virus NS1 protein in viral replication

2014 ◽  
Vol 29 (3) ◽  
pp. 162-169 ◽  
Author(s):  
Jingjing Fan ◽  
Yi Liu ◽  
Zhiming Yuan
Keyword(s):  
Dengue Virus ◽  
Viral Replication ◽  
Critical Role ◽  
Ns1 Protein

scholarly journals Albino mutants of Streptomyces glaucescens tyrosinase

1991 ◽  
Vol 274 (3) ◽  
pp. 707-713 ◽  
Author(s):  
M P Jackman ◽  
A Hajnal ◽  
K Lerch
Keyword(s):  
Active Site ◽  
Critical Role ◽  
Site Directed Mutagenesis ◽  
Mutant Proteins ◽  
Carbonyl Derivatives ◽  
Hydrogen Bonding Interactions ◽  
Albino Phenotype ◽  
Derivatives Of ◽  
Streptomyces Glaucescens

Site-directed mutagenesis was used to determine the functional role of several residues of Streptomyces glaucescens tyrosinase. Replacement of His-37, -53, -193 or -215 by glutamine yields albino phenotypes, as determined by expression on melanin-indicator plates. The purified mutant proteins display no detectable oxy-enzyme and increased Cu lability at the binuclear active site. The carbonyl derivatives of H189Q and H193Q luminesce, with lambda max. displaced more than 25 nm to a longer wavelength compared with native tyrosinase. The remaining histidine mutants display no detectable luminescence. The results are consistent with these histidine residues (together with His-62 and His-189 reported earlier) acting as Cu ligands in the Streptomyces glaucescens enzyme. Conservative substitution of the invariant Asn-190 by glutamine also gives an albino phenotype, no detectable oxy-enzyme and labilization of active-site Cu. The luminescence spectrum of carbonyl-N190Q, however, closely resembles that of the native enzyme under conditions promoting double Cu occupancy of the catalytic site. A critical role for Asn-190 in active-site hydrogen-bonding interactions is proposed.

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 Humoral Immune Response in a Mouse Model Induced With Dengue Virus-like Particles Serotypes 1 and 4 Produced in Silkworm Larvae

2021 ◽  
Author(s):  
Doddy Irawan ◽  
Sabar Pambudi ◽  
Enoch Y. Park
Keyword(s):  
Immune Response ◽  
Dengue Virus ◽  
Protein Domain ◽  
Titration Calorimetry ◽  
Heparin Binding ◽  
Global Public Health ◽  
Silkworm Larvae ◽  
Virus Like Particles ◽  
Humoral Immune ◽  
Domain Iii

Abstract Dengue is an arboviral disease, which threatens almost half the global population, and has emerged as the most significant of current global public health challenges. In this study, we prepared dengue virus-like particles (DENV-LPs) consisting of Capsid-Premembrane-Envelope (CprM/E) and Premembrane-Envelope (prM/E) polypeptides from serotype 1 and 4, which were expressed in the silkworms using Bombyx mori nucleopolyhedrovirus (BmNPV) bacmid. 1CprME, 1prME, 4CprME, and 4prME expressed proteins in hemolymph and molecular weight of the purified proteins were 55 kDa, respectively. The purified polypeptides formed spherical Dengue virus-like particles (DENV-LPs) with approximately 30–55 nm in diameter. The immunoelectron microscopy (IEM) images revealed antigens to the surface of a lipid bilayer of DENV-LPs. The heparin-binding assay shows a positive relationship between absorbance and the quantity of E protein domain III (EDIII), which was supported by the isothermal titration calorimetry assay, showing a moderate binding affinity between heparin and DENV-LP. The high correlation between patient sera and DENV-LP reactivities revealed that these DENV-LPs shared similar epitopes with the natural dengue virus. IgG elicitation studies in mice have demonstrated that DENV-LP/CPrMEs elicits a stronger immune response than DENV-LP/prMEs, which lends credence to this claim.

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