Structural Analysis of a Dengue Cross-Reactive Antibody Complexed with Envelope Domain III Reveals the Molecular Basis of Cross-Reactivity (Q27678419)

9

Juthathip Mongkolsapaya

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Wanwisa Dejnirattisai

4

Wanwisa Dejnirattisai

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Jonathan Grimes

10

Jonathan M Grimes

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Thaneeya Duangchinda

8

Thaneeya Duangchinda

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Wiyada Wongwiwat

7

Wiyada Wongwiwat

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Kriangkrai Chawansuntati

5

Kriangkrai Chawansuntati

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author name string

Claire M Midgley

1

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Aleksandra Flanagan

2

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Hai Bac Tran

3

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Amonrat Jumnainsong

Mechanism of dengue virus broad cross-neutralization by a monoclonal antibody

6

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language of work or name

English

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publication date

15 May 2012

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published in

Journal of Immunology

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volume

188

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issue

10

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page(s)

4971-9

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cites work

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

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

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Antibodies to Envelope Glycoprotein of Dengue Virus during the Natural Course of Infection Are Predominantly Cross-Reactive and Recognize Epitopes Containing Highly Conserved Residues at the Fusion Loop of Domain II

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Binding of a neutralizing antibody to dengue virus alters the arrangement of surface glycoproteins

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Type- and Subcomplex-Specific Neutralizing Antibodies against Domain III of Dengue Virus Type 2 Envelope Protein Recognize Adjacent Epitopes

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A ligand-binding pocket in the dengue virus envelope glycoprotein

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Monoclonal Antibodies That Bind to Domain III of Dengue Virus E Glycoprotein Are the Most Efficient Blockers of Virus Adsorption to Vero Cells

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12 December 2020

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Identifiers

DOI

10.4049/JIMMUNOL.1200227

1 reference

1337758

1337758

1 reference

1 reference

1 reference