A broadly cross-reactive monoclonal antibody against hepatitis E virus capsid antigen
| Autor: | Paulius Lukas Tamosiunas, Martin H. Groschup, Kornelija Markuškienė, Marc Hovestädt, Frank Sellrie, Johannes Scholz, Laima Cepulyte, Henry Memczak, Franziska Ramm, Victor M. Corman, Rasa Petraityte-Burneikiene, Jochen Reetz, D. Becher, Jörg A. Schenk, René Ryll, Paul Dremsek, Stefan Kubick, Anika Andersson, Rainer G. Ulrich, Reimar Johne, Hoai Anh Trinh, Barbara Kubickova |
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| Přispěvatelé: | Publica |
| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: |
Cell-free synthesis
Cross-reactivity HEV-1 HEV-2 HEV-3 HEV-4 HEV-7 Hepatitis E virus Monoclonal antibody batHEV cvHEV ratHEV viruses medicine.disease_cause Applied Microbiology and Biotechnology Epitope Mice Cricetinae 0303 health sciences Mice Inbred BALB C biology Chemistry Antibodies Monoclonal virus diseases General Medicine Capsid Antibody 600 Technik Medizin angewandte Wissenschaften::610 Medizin und Gesundheit::615 Pharmakologie Therapeutik Biotechnology medicine.drug_class CHO Cells 03 medical and health sciences Cricetulus Antigen medicine Escherichia coli Animals Humans 030304 developmental biology Linear epitope 030306 microbiology Virology Biotechnological Products and Process Engineering digestive system diseases Pepscan biology.protein Capsid Proteins |
| Zdroj: | Applied microbiology and biotechnology, New York : Springer, 2021, vol. 105, iss. 12, p. 4957-4973 Applied Microbiology and Biotechnology |
| ISSN: | 0175-7598 1432-0614 |
| Popis: | Abstract 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. |
| Databáze: | OpenAIRE |
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