Publication details

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

Authors	KUBÍČKOVÁ Barbara SCHENK Joerg A. RAMM Franziska MARKUSKIENE Kornelija REETZ Jochen DREMSEK Paul TAMOSIUNAS Paulius Lukas CEPULYTE Laima TRINH Hoai Anh SCHOLZ Johannes MEMCZAK Henry HOVESTAEDT Marc RYLL Rene PETRAITYTE-BURNEIKIENE Rasa CORMAN Victor M. ANDERSSON Anika BECHER Dietmar GROSCHUP Martin H. KUBICK Stefan SELLRIE Frank JOHNE Reimar ULRICH Rainer G.
Year of publication	2021
Type	Article in Periodical
Magazine / Source	Applied Microbiology and Biotechnology
MU Faculty or unit	Faculty of Science
Citation
Web	https://link.springer.com/article/10.1007%2Fs00253-021-11342-7
Doi	http://dx.doi.org/10.1007/s00253-021-11342-7
Keywords	Hepatitis E virus; HEV-1; HEV-2; HEV-3; HEV-4; HEV-7; ratHEV; batHEV; cvHEV; Monoclonal antibody; Cross-reactivity; Cell-free synthesis
Description	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.