Expression of a recombinant bacterial L-asparaginase in human cells.
Raquel Caminha DantasLudmilla Freire CaetanoAriany Lima Sousa TorresMatheus Soares AlvesEmanuelly Thays Muniz Figueiredo SilvaLouhanna Pinheiro Rodrigues TeixeiraDaniel Câmara TeixeiraRenato de Azevedo MoreiraMarcela Helena Gambim FonsecaSaul Gaudêncio NetoLeonardo Tondello MartinsGilvan Pessoa FurtadoKaio Cesar Simiano TavaresPublished in: BMC research notes (2019)
Recombinant ASNase was expressed in human cells with a molecular weight of 60 kDa, larger than in Escherichia coli, which is 35 kDa. N-glycosylation analysis demonstrated that the increased molecular weight resulted from the addition of glycans to the protein by mammalian cells. The glycosylated ASNase presented in vitro activity at physiological pH and temperature. Given that glycosylation can act to reduce antigenicity by masking protein epitopes, our data may contribute to the development of an alternative ASNase in the treatment of ALL in patients who demonstrate side effects to currently marketed enzymes.