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Biochemistry ; 59(34): 3123-3128, 2020 09 01.
Artigo em Inglês | MEDLINE | ID: mdl-31580652

RESUMO

Sialic acids are sugars present in many animal glycoproteins and are of particular interest in biopharmaceuticals, where a lack of sialylation can reduce bioactivity. Here, we describe how α-2,6-sialyltransferase from Photobacterium damselae can be used to markedly increase the level of sialylation of CHO-produced α-1-antitrypsin. Detailed analysis of the sialylation products showed that in addition to the expected α-2,6-sialylation of galactose, a second disialyl galactose motif Neu5Ac-α2,3(Neu5Ac-α2,6)Gal was produced, which, to our knowledge, had never been detected on a mammalian glycoprotein. We exploited this disialyl galactose activity of the P. damselae in a multienzyme reaction to produce a highly sialylated α-1-antitrypsin. The influence of this unique disialylation on the in vitro activity of α-1-antitrypsin was studied, and a toolkit of mass spectrometry methods for identifying this new disialyl galactose motif in complex mixtures was developed.


Assuntos
Galactose/metabolismo , Ácido N-Acetilneuramínico/metabolismo , Photobacterium/enzimologia , Proteínas Recombinantes/metabolismo , Sialiltransferases/metabolismo , alfa 1-Antitripsina/metabolismo
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