Characterization of Neutralizing Epitopes of Varicella-zoster Virus Glycoprotein H

Overview

Journal J Virol

Publisher American Society for Microbiology

Date 2008 Dec 17

PMID 19073736

Citations 5

Authors

Yasushi Akahori

Kazuhiro Suzuki

Tohru Daikoku

Masae Iwai

Yoshihiro Yoshida

Yoshizo Asano

Yoshikazu Kurosawa

Kimiyasu Shiraki

Affiliations

Soon will be listed here.

Abstract

Varicella-zoster virus (VZV) glycoprotein H (gH) is the major neutralization target of VZV, and its neutralizing epitope is conformational. Ten neutralizing human monoclonal antibodies to gH were used to map the epitopes by immunohistochemical analysis and were categorized into seven epitope groups. The combinational neutralization efficacy of two epitope groups was not synergistic. Each epitope was partially or completely resistant to concanavalin A blocking of the glycomoiety of gH, and their antibodies inhibited the cell-to-cell spread of infection. The neutralization epitope comprised at least seven independent protein portions of gH that served as the target to inhibit cell-to-cell spread.

Citing Articles

Breadth and Functionality of Varicella-Zoster Virus Glycoprotein-Specific Antibodies Identified after Zostavax Vaccination in Humans.

Sullivan N, Reuter-Monslow M, Sei J, Durr E, Davis C, Chang C J Virol. 2018; 92(14).

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Defensive Perimeter in the Central Nervous System: Predominance of Astrocytes and Astrogliosis during Recovery from Varicella-Zoster Virus Encephalitis.

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Human anti-varicella-zoster virus (VZV) recombinant monoclonal antibody produced after Zostavax immunization recognizes the gH/gL complex and neutralizes VZV infection.

Birlea M, Owens G, Eshleman E, Ritchie A, Traktinskiy I, Bos N J Virol. 2012; 87(1):415-21.

PMID: 23077312 PMC: 3536365. DOI: 10.1128/JVI.02561-12.

Neutralizing anti-gH antibody of Varicella-zoster virus modulates distribution of gH and induces gene regulation, mimicking latency.

Shiraki K, Daikoku T, Takemoto M, Yoshida Y, Suzuki K, Akahori Y J Virol. 2011; 85(16):8172-80.

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