| Titolo | Antibody proteolysis: a common picture emerging from plants. |
|---|---|
| Tipo di pubblicazione | Articolo su Rivista peer-reviewed |
| Anno di Pubblicazione | 2015 |
| Autori | Donini, Marcello, Lombardi Raffaele, Lonoce Chiara, Di Carli Mariasole, Marusic Carla, Morea Veronica, and Di Micco Patrizio |
| Rivista | Bioengineered |
| Volume | 6 |
| Paginazione | 1-4 |
| Data di pubblicazione | 2015 Jul 17 |
| ISSN | 2165-5987 |
| Parole chiave | Amino Acid Sequence, Antibodies, binding site, Binding Sites, chemistry, Genetically Modified, genetics, human, Humans, metabolism, molecular genetics, Molecular Sequence Data, Monoclonal, Monoclonal antibody, Plants, procedures, protein binding, protein degradation, protein engineering, Proteolysis, transgenic plant |
| Abstract | We have recently characterized the degradation profiles of 2 human IgG1 monoclonal antibodies, the tumor-targeting mAb H10 and the anti-HIV mAb 2G12. Both mAbs were produced in plants either as stable transgenics or using a transient expression system based on leaf agroinfiltration. The purified antibodies were separated by 1DE and protein bands were characterized by N-terminal sequencing. The proteolytic cleavage sites identified in the heavy chain (HC) of both antibodies were localized in 3 inter-domain regions, suggesting that the number of proteolytic cleavage events taking place in plants is limited. One of the cleavage sites, close to the hinge region, was common to both antibodies. |
| Note | cited By 5 |
| URL | https://www.scopus.com/inward/record.uri?eid=2-s2.0-85018224503&doi=10.1080%2f21655979.2015.1067740&partnerID=40&md5=0216dc4065c87db71c4342ef416564e3 |
| DOI | 10.1080/21655979.2015.1067740 |
| Citation Key | 5409 |
