| Title |
A broadly cross-reactive monoclonal antibody against hepatitis E virus capsid antigen / |
| Authors |
Kubickova, Barbara ; Schenk, Jörg A ; Ramm, Franziska ; Marcinkevičiūtė, Kornelija ; Reetz, Jochen ; Dremsek, Paul ; Tamošiūnas, Paulius Lukas ; Čepulytė, Laima ; Trinh, Hoai Anh ; Scholz, Johannes ; Memczak, Henry ; Hovestädt, Marc ; Ryll, René ; Petraitytė-Burneikienė, Rasa ; Corman, Victor M ; Andersson, Anika ; Becher, Dietmar ; Groschup, Martin H ; Kubick, Stefan ; Sellrie, Frank ; Johne, Reimar ; Ulrich, Rainer G |
| DOI |
10.1007/s00253-021-11342-7 |
| Full Text |
|
| Is Part of |
Applied microbiology and biotechnology.. New York : Springer. 2021, vol. 105, iss. 12, p. 4957-4973.. ISSN 0175-7598. eISSN 1432-0614 |
| Keywords [eng] |
Cell-free synthesis ; Cross-reactivity ; HEV-1 ; HEV-2 ; HEV-3 ; HEV-4 ; HEV-7 ; Hepatitis E virus ; Monoclonal antibody ; batHEV ; cvHEV ; ratHEV |
| Abstract [eng] |
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. KEY POINTS: • The antibody showed cross-reactivity with capsid proteins of different hepeviruses. • The linear epitope of the antibody was mapped in a partially surface-exposed region. • The antibody detected native HEV-3 antigen in infected mammalian cells. |
| Published |
New York : Springer |
| Type |
Journal article |
| Language |
English |
| Publication date |
2021 |
| CC license |
|
