Direct and indirect interactions in the recognition between a cross‐neutralizing antibody and the four serotypes of dengue virus

@article{Lisova2014DirectAI,
  title={Direct and indirect interactions in the recognition between a cross‐neutralizing antibody and the four serotypes of dengue virus},
  author={O. Lisova and L. Belkadi and H. Bedouelle},
  journal={Journal of Molecular Recognition},
  year={2014},
  volume={27}
}
Dengue fever is the most important vector‐borne viral disease. Four serotypes of dengue virus, DENV1 to DENV4, coexist. Secondary infection by a different serotype is a risk factor for severe dengue. Monoclonal antibody mAb4E11 neutralizes the four serotypes of DENV with varying efficacies by recognizing an epitope located within domain‐III (ED3) of the viral envelope (E) protein. To better understand the cross‐reactivities between mAb4E11 and the four serotypes of DENV, we constructed… Expand
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References

SHOWING 1-10 OF 77 REFERENCES
Diversity and junction residues as hotspots of binding energy in an antibody neutralizing the dengue virus
TLDR
The genetic events that led to mAb4E11 during an immune response are recreated and an alanine scanning mutagenesis of its third hypervariable loops are performed and changes of residues that statistically do not participate in the contacts between antibodies and antigens but determine the structure of L‐CDR3 decreased the affinity between mAb 4E11 and its antigen. Expand
Structural insights into the neutralization mechanism of a higher primate antibody against dengue virus
TLDR
It is shown that human sera from patients recovering from DENV‐4 infection contain antibodies that bind to the 5H2 epitope region on domain I, which provides new information and tools for effective vaccine design to prevent dengue disease. Expand
Structural Analysis of a Dengue Cross-Reactive Antibody Complexed with Envelope Domain III Reveals the Molecular Basis of Cross-Reactivity
TLDR
The characterization of a mAb, 2H12, is reported, which is cross-reactive to all four serotypes in the dengue virus group and provides a structural basis for understanding Ab neutralization and enhancement of infection, which are crucial for the development of future d Dengue vaccines. Expand
Mechanism of dengue virus broad cross-neutralization by a monoclonal antibody.
TLDR
A comparative, high-resolution crystallographic analysis of an "A-strand" murine monoclonal antibody, Mab 4E11, in complex with its target domain of the envelope protein from the four DENVs reveals the determinants of this cross-reactivity. Expand
Cross-reactivities between human IgMs and the four serotypes of dengue virus as probed with artificial homodimers of domain-III from the envelope proteins
TLDR
The serotype specificity and cross-reactivity of human IgMs directed against ED3 is determined by using a well-characterized collection of 90 DENV-infected and 89DENV-uninfected human serums to help better understand the IgM immune response and protection against DENV. Expand
Mapping to completeness and transplantation of a group-specific, discontinuous, neutralizing epitope in the envelope protein of dengue virus.
TLDR
The energetic epitope of antibody mAb4E11, which neutralizes the four serotypes of DENV but no other flavivirus, and binds domain 3 of their envelope glycoprotein, was characterized and mechanisms for its neutralization potency are suggested. Expand
Variable Surface Epitopes in the Crystal Structure of Dengue Virus Type 3 Envelope Glycoprotein
TLDR
The crystal structure of a soluble fragment of the envelope glycoprotein E from dengue virus type 3 is determined and shows that neighboring glycans on the viral surface are spaced widely enough that they can interact with multiple carbohydrate recognition domains on oligomeric lectins such as DC-SIGN, ensuring maximum affinity for these putative receptors. Expand
Structural Basis of Differential Neutralization of DENV-1 Genotypes by an Antibody that Recognizes a Cryptic Epitope
TLDR
The results support the conclusion that potent neutralization depends on genotype-dependent exposure of the CC′ loop epitope, and establish new structural complexity of the DENV virion, which may be relevant for the choice of DENV strain for induction or analysis of neutralizing antibodies in the context of vaccine development. Expand
The human immune response to Dengue virus is dominated by highly cross-reactive antibodies endowed with neutralizing and enhancing activity.
TLDR
These findings reveal an unexpected degree of cross-reactivity in human antibodies against DENV and illustrate the potential for an antibody-based therapy to control severe dengue. Expand
Mapping of a dengue virus neutralizing epitope critical for the infectivity of all serotypes: insight into the neutralization mechanism.
TLDR
The data suggest that the DE(306-314) segment is critical for the infectivity of all dengue virus serotypes and that molecules that block the binding of DE( 306- 314) to HSHS may be antiviral reagents of therapeutic interest. Expand
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