Neutralizing human monoclonal antibodies to hepatitis A virus recovered by phage display

Sang Jick Kim; Myeong Hee Jang; Jack T Stapleton; Sun Ok Yoon; Keun-Soo Kim; Eun-Seok Jeon; Hyo Jeong Hong

doi:10.1016/j.virol.2003.10.014

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Neutralizing human monoclonal antibodies to hepatitis A virus recovered by phage display

Journal article

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Peer reviewed

Neutralizing human monoclonal antibodies to hepatitis A virus recovered by phage display

Sang Jick Kim, Myeong Hee Jang, Jack T Stapleton, Sun Ok Yoon, Keun-Soo Kim, Eun-Seok Jeon and Hyo Jeong Hong

Virology (New York, N.Y.), Vol.318(2), pp.598-607

2004

DOI: 10.1016/j.virol.2003.10.014

PMID: 14972527

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Abstract

Four human monoclonal antibodies (MAbs) to hepatitis A virus (HAV) were isolated from a phage-displayed antibody library constructed from the peripheral blood lymphocytes (PBLs) of HAV-immune donors. The four MAbs showed differences in their affinity: two (HA6, HA9) of them were dominant after four rounds of panning, and showed higher affinity than the other two (HA1, HA12). All four MAbs showed HAV-neutralizing activity in radioimmunofocus inhibition assay and their neutralizing activity was positively correlated with their affinities. Analysis of their epitope specificity by cross-competition binding assays suggested that HA6 and HA9 recognize extensively overlapping epitopes, which overlap with those of HA1 and HA12, although HA1 and HA12 recognize distinct epitopes. In addition, competition assays with known neutralizing murine MAbs suggested that the epitopes of four human MAbs extensively overlap with those of B5B3 and K34C8 which are distinct but reside within the single, immunodominant neutralization site on the HAV capsid. The human MAbs (HA6 and HA9) with highest affinity may be useful in the immunoprophylaxis of HAV infection.

Neutralization epitope

Phage display

Human antibody library

HAV

Fab

Details

Title: Subtitle: Neutralizing human monoclonal antibodies to hepatitis A virus recovered by phage display
Creators: Sang Jick Kim - Antibody Engineering Research Unit, Korea Research Institute of Bioscience and Biotechnology, Taejon 305-600, South Korea
Myeong Hee Jang - Antibody Engineering Research Unit, Korea Research Institute of Bioscience and Biotechnology, Taejon 305-600, South Korea
Jack T Stapleton - Department of Internal Medicine, Helen C. Levitt Center for Viral Pathogenesis, The University of Iowa, Iowa City, IA 52242, USA
Sun Ok Yoon - Antibody Engineering Research Unit, Korea Research Institute of Bioscience and Biotechnology, Taejon 305-600, South Korea
Keun-Soo Kim - Aprogen, Inc., Korea Research Institute of Bioscience and Biotechnology, Taejon 305-600, South Korea
Eun-Seok Jeon - Department of Internal Medicine, College of Medicine, Chungnam National University, Taejon 301-040, South Korea
Hyo Jeong Hong - Antibody Engineering Research Unit, Korea Research Institute of Bioscience and Biotechnology, Taejon 305-600, South Korea
Resource Type: Journal article
Publication Details: Virology (New York, N.Y.), Vol.318(2), pp.598-607
DOI: 10.1016/j.virol.2003.10.014
PMID: 14972527
NLM abbreviation: Virology
ISSN: 0042-6822
eISSN: 1096-0341
Publisher: Elsevier Inc
Language: English
Date published: 2004
Academic Unit: Microbiology and Immunology; Infectious Diseases; Internal Medicine
Record Identifier: 9984094548302771

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