Antigenic analysis of West Nile virus strains using monoclonal antibodies

1988 ◽  
Vol 99 (1-2) ◽  
pp. 75-88 ◽  
Author(s):  
Terry G. Besselaar ◽  
N. K. Blackburn
Keyword(s):  
Monoclonal Antibodies ◽  
West Nile Virus ◽  
Antigenic Analysis ◽  
West Nile ◽  
Virus Strains

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 Introductions of West Nile Virus Strains to Mexico

2006 ◽  
Vol 12 (2) ◽  
pp. 314-318 ◽  
Author(s):  
Eleanor Deardorff ◽  
José G. Estrada-Franco ◽  
Aaron C. Brault ◽  
Roberto Navarro-Lopez ◽  
Arturo Campomanes-Cortes ◽  
...  
Keyword(s):  
West Nile Virus ◽  
West Nile ◽  
Virus Strains

scholarly journals Experimental infection of house sparrows (Passer domesticus) with West Nile virus strains of lineages 1 and 2

2014 ◽  
Vol 172 (3-4) ◽  
pp. 542-547 ◽  
Author(s):  
Javier Del Amo ◽  
Francisco Llorente ◽  
Elisa Pérez-Ramirez ◽  
Ramón C. Soriguer ◽  
Jordi Figuerola ◽  
...  
Keyword(s):  
West Nile Virus ◽  
Experimental Infection ◽  
Passer Domesticus ◽  
West Nile ◽  
House Sparrows ◽  
Virus Strains

scholarly journals Antigenic Characterization of New Lineage II Insect-Specific Flaviviruses in Australian Mosquitoes and Identification of Host Restriction Factors

mSphere ◽  
2020 ◽  
Vol 5 (3) ◽  
Author(s):  
Jessica J. Harrison ◽  
Jody Hobson-Peters ◽  
Agathe M. G. Colmant ◽  
Joanna Koh ◽  
Natalee D. Newton ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
West Nile Virus ◽  
Cell Lines ◽  
Yellow Fever Virus ◽  
West Nile ◽  
Host Restriction ◽  
Antiviral Responses ◽  
Vertebrate Cell ◽  
Wide Range ◽  
Chimeric Viruses

ABSTRACT We describe two new insect-specific flaviviruses (ISFs) isolated from mosquitoes in Australia, Binjari virus (BinJV) and Hidden Valley virus (HVV), that grow efficiently in mosquito cells but fail to replicate in a range of vertebrate cell lines. Phylogenetic analysis revealed that BinJV and HVV were closely related (90% amino acid sequence identity) and clustered with lineage II (dual-host affiliated) ISFs, including the Lammi and Nounané viruses. Using a panel of monoclonal antibodies prepared to BinJV viral proteins, we confirmed a close relationship between HVV and BinJV and revealed that they were antigenically quite divergent from other lineage II ISFs. We also constructed chimeric viruses between BinJV and the vertebrate-infecting West Nile virus (WNV) by swapping the structural genes (prM and E) to produce BinJ/WNVKUN-prME and WNVKUN/BinJV-prME. This allowed us to assess the role of different regions of the BinJV genome in vertebrate host restriction and revealed that while BinJV structural proteins facilitated entry to vertebrate cells, the process was inefficient. In contrast, the BinJV replicative components in wild-type BinJV and BinJ/WNVKUN-prME failed to initiate replication in a wide range of vertebrate cell lines at 37°C, including cells lacking components of the innate immune response. However, trace levels of replication of BinJ/WNVKUN-prME could be detected in some cultures of mouse embryo fibroblasts (MEFs) deficient in antiviral responses (IFNAR−/− MEFs or RNase L−/− MEFs) incubated at 34°C after inoculation. This suggests that BinJV replication in vertebrate cells is temperature sensitive and restricted at multiple stages of cellular infection, including inefficient cell entry and susceptibility to antiviral responses. IMPORTANCE The globally important flavivirus pathogens West Nile virus, Zika virus, dengue viruses, and yellow fever virus can infect mosquito vectors and be transmitted to humans and other vertebrate species in which they cause significant levels of disease and mortality. However, the subgroup of closely related flaviviruses, known as lineage II insect-specific flaviviruses (Lin II ISFs), only infect mosquitoes and cannot replicate in cells of vertebrate origin. Our data are the first to uncover the mechanisms that restrict the growth of Lin II ISFs in vertebrate cells and provides new insights into the evolution of these viruses and the mechanisms associated with host switching that may allow new mosquito-borne viral diseases to emerge. The new reagents generated in this study, including the first Lin II ISF-reactive monoclonal antibodies and Lin II ISF mutants and chimeric viruses, also provide new tools and approaches to enable further research advances in this field.

Genetic characterization of West Nile Virus strains during neuroinvasives infection outbreak in Tunisia, 2018

2020 ◽  
Author(s):  
Wasfi Fares ◽  
Mariem Gdoura ◽  
Haifa Dhrif ◽  
Henda Touzi ◽  
Nahed Hogga ◽  
...  
Keyword(s):  
West Nile Virus ◽  
Genetic Characterization ◽  
West Nile ◽  
Virus Strains

scholarly journals Monoclonal antibodies to the West Nile virus NS5 protein map to linear and conformational epitopes in the methyltransferase and polymerase domains

2009 ◽  
Vol 90 (12) ◽  
pp. 2912-2922 ◽  
Author(s):  
Roy A. Hall ◽  
Si En Tan ◽  
Barbara Selisko ◽  
Rachael Slade ◽  
Jody Hobson-Peters ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
West Nile Virus ◽  
Binding Sites ◽  
Synthetic Peptides ◽  
Structural Model ◽  
Full Length ◽  
Physical Interaction ◽  
Rdrp Activity ◽  
The West ◽  
West Nile

The West Nile virus (WNV) NS5 protein contains a methyltransferase (MTase) domain involved in RNA capping and an RNA-dependent RNA polymerase (RdRp) domain essential for virus replication. Crystal structures of individual WNV MTase and RdRp domains have been solved; however, the structure of full-length NS5 has not been determined. To gain more insight into the structure of NS5 and interactions between the MTase and RdRp domains, we generated a panel of seven monoclonal antibodies (mAbs) to the NS5 protein of WNV (Kunjin strain) and mapped their binding sites using a series of truncated NS5 proteins and synthetic peptides. Binding sites of four mAbs (5D4, 4B6, 5C11 and 6A10) were mapped to residues 354–389 in the fingers subdomain of the RdRp. This is consistent with the ability of these mAbs to inhibit RdRp activity in vitro and suggests that this region represents a potential target for RdRp inhibitors. Using a series of synthetic peptides, we also identified a linear epitope (bound by mAb 5H1) that mapped to a 13 aa stretch surrounding residues 47 and 49 in the MTase domain, a region predicted to interact with the palm subdomain of the RdRp. The failure of one mAb (7G6) to bind both N- and C-terminally truncated NS5 recombinants indicates that the antibody recognizes a conformational epitope that requires the presence of residues in both the MTase and RdRp domains. These data support a structural model of the full-length NS5 molecule that predicts a physical interaction between the MTase and the RdRp domains.

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