scholarly journals Erratum: Structural basis of potent Zika–dengue virus antibody cross-neutralization

Nature ◽  
2016 ◽  
Vol 539 (7628) ◽  
pp. 314-314 ◽  
Author(s):  
Giovanna Barba-Spaeth ◽  
Wanwisa Dejnirattisai ◽  
Alexander Rouvinski ◽  
Marie-Christine Vaney ◽  
Iris Medits ◽  
...  
Keyword(s):  
Dengue Virus ◽  
Structural Basis ◽  
Virus Antibody ◽  
Cross Neutralization

scholarly journals Structural basis of potent Zika–dengue virus antibody cross-neutralization

Nature ◽  
2016 ◽  
Vol 536 (7614) ◽  
pp. 48-53 ◽  
Author(s):  
Giovanna Barba-Spaeth ◽  
Wanwisa Dejnirattisai ◽  
Alexander Rouvinski ◽  
Marie-Christine Vaney ◽  
Iris Medits ◽  
...  
Keyword(s):  
Dengue Virus ◽  
Structural Basis ◽  
Virus Antibody ◽  
Cross Neutralization

The Structural Basis for Serotype-Specific Neutralization of Dengue Virus by a Human Antibody

2012 ◽  
Vol 4 (139) ◽  
pp. 139ra83-139ra83 ◽  
Author(s):  
E. P. Teoh ◽  
P. Kukkaro ◽  
E. W. Teo ◽  
A. P. C. Lim ◽  
T. T. Tan ◽  
...  
Keyword(s):  
Dengue Virus ◽  
Structural Basis ◽  
Human Antibody

scholarly journals Cryptic Properties of a Cluster of Dominant Flavivirus Cross-Reactive Antigenic Sites

2006 ◽  
Vol 80 (19) ◽  
pp. 9557-9568 ◽  
Author(s):  
Karin Stiasny ◽  
Stefan Kiermayr ◽  
Heidemarie Holzmann ◽  
Franz X. Heinz
Keyword(s):  
Structural Basis ◽  
Human Pathogens ◽  
E Proteins ◽  
Structural Element ◽  
Antigenic Sites ◽  
Tick Borne Encephalitis ◽  
Tbe Virus ◽  
Protective Antibodies ◽  
Cross Neutralization ◽  
Partially Occluded

ABSTRACT A number of flaviviruses are important human pathogens, including yellow fever, dengue, West Nile, Japanese encephalitis, and tick-borne encephalitis (TBE) viruses. Infection with or immunization against any of these viruses induces a subset of antibodies that are broadly flavivirus cross-reactive but do not exhibit significant cross-neutralization. Nevertheless, these antibodies can efficiently bind to the major envelope protein (E), which is the main target of neutralizing and protective antibodies because of its receptor-binding and membrane fusion functions. The structural basis for this phenomenon is still unclear. In our studies with TBE virus, we have provided evidence that such cross-reactive antibodies are specific for a cluster of epitopes that are partially occluded in the cage-like assembly of E proteins at the surfaces of infectious virions and involve—but are not restricted to—amino acids of the highly conserved internal fusion peptide loop. Virus disintegration leads to increased accessibility of these epitopes, allowing the cross-reactive antibodies to bind with strongly increased avidity. The cryptic properties of these sites in the context of infectious virions can thus provide an explanation for the observed lack of efficient neutralizing activity of broadly cross-reactive antibodies, despite their specificity for a functionally important structural element in the E protein.

Seroprevalence of Dengue Virus Antibody in Korea

2018 ◽  
Vol 25 (3) ◽  
pp. 132
Author(s):  
Ji Hyen Lee ◽  
Han Wool Kim ◽  
Kyung-Hyo Kim
Keyword(s):  
Dengue Virus ◽  
Virus Antibody
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