| Literature DB >> 26186119 |
Marcello Donini1, Raffaele Lombardi1, Chiara Lonoce1, Mariasole Di Carli1, Carla Marusic1, Veronica Morea2, Patrizio Di Micco3.
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.Entities:
Keywords: 2DE; Agrobacterium tumefaciens; N-terminal sequencing; agroinfiltration; immunoglobulin; molecular farming; plant proteases; plant proteolysis
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Year: 2015 PMID: 26186119 PMCID: PMC4825827 DOI: 10.1080/21655979.2015.1067740
Source DB: PubMed Journal: Bioengineered ISSN: 2165-5979 Impact factor: 3.269