A broadly cross-reactive monoclonal antibody against hepatitis E virus capsid antigen

S.4957-4973 To generate a hepatitis E virus (HEV) genotype 3 (HEV-3)-specific monoclonal antibody (mAb), the Escherichia coli-expressed carboxy-terminal part of its capsid protein was used to immunise BALB/c mice. The immunisation resulted in the induction of HEV-specific antibodies of high titre. T...

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Bibliographic Details
Published in:Applied Microbiology and Biotechnology
Main Authors: Kubickova, B., Schenk, J.A., Ramm, F., Markuskiene, K., Reetz, J., Dremsek, P., Tamosiunas, P.L., Cepulyte, L., Trinh, H.A., Scholz, J., Memczak, H., Hovestädt, M., Ryll, R., Petraityte-Burneikiene, R., Corman, V.M., Andersson, A., Becher, D., Groschup, M.H., Kubick, S., Sellrie, F., Johne, R., Ulrich, R.G.
Format: Article in Journal/Newspaper
Language:English
Published: 2021
Subjects:
610
660
620
Common vole
Online Access:https://publica.fraunhofer.de/handle/publica/270436
https://doi.org/10.1007/s00253-021-11342-7
Description
Summary:S.4957-4973 To generate a hepatitis E virus (HEV) genotype 3 (HEV-3)-specific monoclonal antibody (mAb), the Escherichia coli-expressed carboxy-terminal part of its capsid protein was used to immunise BALB/c mice. The immunisation resulted in the induction of HEV-specific antibodies of high titre. The mAb G117-AA4 of IgG1 isotype was obtained showing a strong reactivity with the homologous E. coli, but also yeast-expressed capsid protein of HEV-3. The mAb strongly cross-reacted with ratHEV capsid protein derivatives produced in both expression systems and weaker with an E. coli-expressed batHEV capsid protein fragment. In addition, the mAb reacted with capsid protein derivatives of genotypes HEV-2 and HEV-4 and common vole hepatitis E virus (cvHEV), produced by the cell-free synthesis in Chinese hamster ovary (CHO) and Spodoptera frugiperda (Sf21) cell lysates. Western blot and line blot reactivity of the mAb with capsid protein derivatives of HEV-1 to HEV-4, cvHEV, ratHEV and batHEV suggested a linear epitope. Use of truncated derivatives of ratHEV capsid protein in ELISA, Western blot, and a Pepscan analysis allowed to map the epitope within a partially surface-exposed region with the amino acid sequence LYTSV. The mAb was also shown to bind to human patient-derived HEV-3 from infected cell culture and to hare HEV-3 and camel HEV-7 capsid proteins from transfected cells by immunofluorescence assay. The novel mAb may serve as a useful tool for further investigations on the pathogenesis of HEV infections and might be used for diagnostic purposes. 105 Nr.12

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