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Title 

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

Authors 

Sang Jick KimMyeong Hee JangJ T StapletonSun Ok YoonK S KimE S JeonHyo Jeong Hong

Publisher 

Elsevier

Issue Date 

2004

Citation 

Virology, vol. 318, no. 2, pp. 598-607

Keywords 

FabHAVhuman antibody libraryneutralization epitopephage displaymonoclonal antibodyantibody librarybacteriophagebinding affinitycorrelation analysis

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.

ISSN 

0042-6822

Link 

http://dx.doi.org/10.1016/j.virol.2003.10.014

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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