Backbone 1H, 15N, and 13C resonance assignments of the non-structural protein NS2B of Zika virus

2021 ◽  
Author(s):  
Beatriz Rosa Penna ◽  
Danielle Maria P. de Oliveira ◽  
Cristiane Dinis Anobom ◽  
Ana Paula Valente
Keyword(s):  
Zika Virus ◽  
Resonance Assignments ◽  
Structural Protein

scholarly journals A Label and Probe-Free Zika Virus Immunosensor Prussian Blue@carbon Nanotube-Based for Amperometric Detection of the NS2B Protein

Biosensors ◽  
2021 ◽  
Vol 11 (5) ◽  
pp. 157
Author(s):  
Bárbara V. M. Silva ◽  
Marli T. Cordeiro ◽  
Marco A. B. Rodrigues ◽  
Ernesto T. A. Marques ◽  
Rosa F. Dutra
Keyword(s):  
Carbon Nanotube ◽  
Prussian Blue ◽  
Zika Virus ◽  
Point Of Care ◽  
Amperometric Detection ◽  
Cross Reactivity ◽  
Structural Protein ◽  
Serum Samples ◽  
Polypyrrole Composite ◽  
Congenital Disabilities

Zika virus (ZIKV) is a mosquito-borne infection, predominant in tropical and subtropical regions causing international concern due to the ZIKV disease having been associated with congenital disabilities, especially microcephaly and other congenital abnormalities in the fetus and newborns. Development of strategies that minimize the devastating impact by monitoring and preventing ZIKV transmission through sexual intercourse, especially in pregnant women, since no vaccine is yet available for the prevention or treatment, is critically important. ZIKV infection is generally asymptomatic and cross-reactivity with dengue virus (DENV) is a global concern. An innovative screen-printed electrode (SPE) was developed for amperometric detection of the non-structural protein (NS2B) of ZIKV by exploring the intrinsic redox catalytic activity of Prussian blue (PB), incorporated into a carbon nanotube–polypyrrole composite. Thus, this immunosensor has the advantage of electrochemical detection without adding any redox-probe solution (probe-less detection), allowing a point-of-care diagnosis. It was responsive to serum samples of only ZIKV positive patients and non-responsive to negative ZIKV patients, even if the sample was DENV positive, indicating a possible differential diagnosis between them by NS2B. All samples used here were confirmed by CDC protocols, and immunosensor responses were also checked in the supernatant of C6/36 and in Vero cell cultures infected with ZIKV.

scholarly journals Site-specific N-glycosylation analysis of animal cell culture-derived Zika virus proteins

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Alexander Pralow ◽  
Alexander Nikolay ◽  
Arnaud Leon ◽  
Yvonne Genzel ◽  
Erdmann Rapp ◽  
...  
Keyword(s):  
Zika Virus ◽  
Animal Cell ◽  
Gradient Centrifugation ◽  
Viral Envelope ◽  
Protein Glycosylation ◽  
High Yield ◽  
Structural Protein ◽  
Site Specific ◽  
E Protein ◽  
The Impact

AbstractHere, we present for the first time, a site-specific N-glycosylation analysis of proteins from a Brazilian Zika virus (ZIKV) strain. The virus was propagated with high yield in an embryo-derived stem cell line (EB66, Valneva SE), and concentrated by g-force step-gradient centrifugation. Subsequently, the sample was proteolytically digested with different enzymes, measured via a LC–MS/MS-based workflow, and analyzed in a semi-automated way using the in-house developed glyXtoolMS software. The viral non-structural protein 1 (NS1) was glycosylated exclusively with high-mannose structures on both potential N-glycosylation sites. In case of the viral envelope (E) protein, no specific N-glycans could be identified with this method. Nevertheless, N-glycosylation could be proved by enzymatic de-N-glycosylation with PNGase F, resulting in a strong MS-signal of the former glycopeptide with deamidated asparagine at the potential N-glycosylation site N444. This confirmed that this site of the ZIKV E protein is highly N-glycosylated but with very high micro-heterogeneity. Our study clearly demonstrates the progress made towards site-specific N-glycosylation analysis of viral proteins, i.e. for Brazilian ZIKV. It allows to better characterize viral isolates, and to monitor glycosylation of major antigens. The method established can be applied for detailed studies regarding the impact of protein glycosylation on antigenicity and human pathogenicity of many viruses including influenza virus, HIV and corona virus.

scholarly journals Temperature-dependent secretion of Zika virus envelope and non-structural protein 1 in mammalian cells for clinical applications

2021 ◽  
pp. 114175
Author(s):  
Young Chan Kim ◽  
Joanne E. Nettleship ◽  
Nallely García-Larragoiti ◽  
Mar Maria Antonieta ◽  
Ariadna Lorena Mondragón-García ◽  
...  
Keyword(s):  
Zika Virus ◽  
Mammalian Cells ◽  
Clinical Applications ◽  
Structural Protein ◽  
Temperature Dependent ◽  
Virus Envelope

scholarly journals A GFP Reporter MR766-Based Flow Cytometry Neutralization Test for Rapid Detection of Zika Virus-Neutralizing Antibodies in Serum Specimens

Vaccines ◽  
2019 ◽  
Vol 7 (3) ◽  
pp. 66 ◽  
Author(s):  
Frumence ◽  
Viranaicken ◽  
Gadea ◽  
Desprès
Keyword(s):  
Flow Cytometry ◽  
Zika Virus ◽  
Neutralizing Antibodies ◽  
Neutralization Test ◽  
Health Concern ◽  
Structural Protein ◽  
Adult Mice ◽  
Gfp Reporter ◽  
Infected Cells ◽  
High Level

Zika virus (ZIKV) is an emerging arthropod-borne virus of major public health concern. ZIKV infection is responsible for congenital Zika disease and other neurological defects. Antibody-mediated virus neutralization is an essential component of protective antiviral immunity against ZIKV. In the present study, we assessed whether our GFP reporter ZIKV derived from African viral strain MR766 could be useful for the development of a flow cytometry neutralization test (FNT), as an alternative to the conventional plaque-reduction neutralization test (PRNT). To improve the efficacy of GFP-expressing MR766, we selected virus variant MR766GFP showing a high level of GFP signal in infected cells. A MR766GFP-based FNT was assayed with immune sera from adult mice that received ZIKBeHMR-2. The chimeric ZIKV clone ZIKBeHMR-2 comprises the structural protein region of epidemic strain BeH819015 into MR766 backbone. We reported that adult mice inoculated with ZIKBeHMR-2 developed high levels of neutralizing anti-ZIKV antibodies. Comparative analysis between MR766GFP-based FNT and conventional PRNT was performed using mouse anti-ZIKBeHMR-2 immune sera. Indistinguishable neutralization patterns were observed when compared with PRNT50 and FNT50. We consider that the newly developed MR766GFP-based FNT is a valid format for measuring ZIKV-neutralizing antibodies in serum specimens.

scholarly journals Construction and Identification of Recombinant HEK293T Cell Lines Expressing Non-structural Protein 1 of Zika Virus

2017 ◽  
Vol 14 (11) ◽  
pp. 1072-1079 ◽  
Author(s):  
Jun Liu ◽  
Pengfei Wan ◽  
Qingqing Li ◽  
Xiaoxin Li ◽  
Andrew Li ◽  
...  
Keyword(s):  
Cell Lines ◽  
Zika Virus ◽  
Hek293t Cell ◽  
Structural Protein

scholarly journals RIG-I Plays a Dominant Role in the Induction of Transcriptional Changes in Zika Virus-Infected Cells, which Protect from Virus-Induced Cell Death

Cells ◽  
2020 ◽  
Vol 9 (6) ◽  
pp. 1476 ◽  
Author(s):  
Mirjam Schilling ◽  
Anne Bridgeman ◽  
Nicki Gray ◽  
Jonny Hertzog ◽  
Philip Hublitz ◽  
...  
Keyword(s):  
Cell Death ◽  
Zika Virus ◽  
Dominant Role ◽  
A549 Cells ◽  
Effective Control ◽  
Type I ◽  
Type I Ifn ◽  
Structural Protein ◽  
Induced Apoptosis ◽  
The Individual

The Zika virus (ZIKV) has received much attention due to an alarming increase in cases of neurological disorders including congenital Zika syndrome associated with infection. To date, there is no effective treatment available. An immediate response by the innate immune system is crucial for effective control of the virus. Using CRISPR/Cas9-mediated knockouts in A549 cells, we investigated the individual contributions of the RIG-I-like receptors MDA5 and RIG-I to ZIKV sensing and control of this virus by using a Brazilian ZIKV strain. We show that RIG-I is the main sensor for ZIKV in A549 cells. Surprisingly, we observed that loss of RIG-I and consecutive type I interferon (IFN) production led to virus-induced apoptosis. ZIKV non-structural protein NS5 was reported to interfere with type I IFN receptor signaling. Additionally, we show that ZIKV NS5 inhibits type I IFN induction. Overall, our study highlights the importance of RIG-I-dependent ZIKV sensing for the prevention of virus-induced cell death and shows that NS5 inhibits the production of type I IFN.

scholarly journals Cleft analysis of Zika virus non-structural protein 1

2017 ◽  
Vol 7 (8) ◽  
pp. 763-764
Author(s):  
Somsri Wiwanitkit ◽  
Viroj Wiwanitkit
Keyword(s):  
Zika Virus ◽  
Structural Protein

scholarly journals An Attenuated Zika Virus Encoding Non-Glycosylated Envelope (E) and Non-Structural Protein 1 (NS1) Confers Complete Protection against Lethal Challenge in a Mouse Model

Vaccines ◽  
2019 ◽  
Vol 7 (3) ◽  
pp. 112 ◽  
Author(s):  
Arun S. Annamalai ◽  
Aryamav Pattnaik ◽  
Bikash R. Sahoo ◽  
Zack P. Guinn ◽  
Brianna L. Bullard ◽  
...  
Keyword(s):  
Zika Virus ◽  
Structural Protein ◽  
Complete Protection ◽  
Lethal Challenge ◽  
Live Virus ◽  
Virus Challenge ◽  
Glycosylation Sites ◽  
Viral Vaccine ◽  
Asian Lineage ◽  
Congenital Microcephaly

Zika virus (ZIKV), a mosquito-transmitted flavivirus, emerged in the last decade causing serious human diseases, including congenital microcephaly in newborns and Guillain-Barré syndrome in adults. Although many vaccine platforms are at various stages of development, no licensed vaccines are currently available. Previously, we described a mutant MR766 ZIKV (m2MR) bearing an E protein mutation (N154A) that prevented its glycosylation, resulting in attenuation and defective neuroinvasion. To further attenuate m2MR for its potential use as a live viral vaccine, we incorporated additional mutations into m2MR by substituting the asparagine residues in the glycosylation sites (N130 and N207) of NS1 with alanine residues. Examination of pathogenic properties revealed that the virus (m5MR) carrying mutations in E (N154A) and NS1 (N130A and N207A) was fully attenuated with no disease signs in infected mice, inducing high levels of humoral and cell-mediated immune responses, and protecting mice from subsequent lethal virus challenge. Furthermore, passive transfer of sera from m5MR-infected mice into naïve animals resulted in complete protection from lethal challenge. The immune sera from m5MR-infected animals neutralized both African and Asian lineage viruses equally well, suggesting that m5MR virus could be developed as a potentially broad live virus vaccine candidate.

scholarly journals Added value of IgA antibodies against Zika virus non-structural protein 1 in the diagnosis of acute Zika virus infections

2019 ◽  
Vol 267 ◽  
pp. 8-15 ◽  
Author(s):  
Jens M. Warnecke ◽  
Erik Lattwein ◽  
Sandra Saschenbrecker ◽  
Winfried Stöcker ◽  
Wolfgang Schlumberger ◽  
...  
Keyword(s):  
Zika Virus ◽  
Added Value ◽  
Structural Protein ◽  
Virus Infections ◽  
Iga Antibodies
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