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Antibody proteolysis: a common picture emerging from plants.

TitoloAntibody proteolysis: a common picture emerging from plants.
Tipo di pubblicazioneArticolo su Rivista peer-reviewed
Anno di Pubblicazione2015
AutoriDonini, Marcello, Lombardi Raffaele, Lonoce Chiara, Di Carli Mariasole, Marusic Carla, Morea Veronica, and Di Micco Patrizio
RivistaBioengineered
Volume6
Paginazione1-4
Data di pubblicazione2015 Jul 17
ISSN2165-5987
Parole chiaveAmino 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

URLhttps://www.scopus.com/inward/record.uri?eid=2-s2.0-85018224503&doi=10.1080%2f21655979.2015.1067740&partnerID=40&md5=0216dc4065c87db71c4342ef416564e3
DOI10.1080/21655979.2015.1067740
Citation Key5409