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Exploiting the Disialyl Galactose Activity of α2,6-Sialyltransferase from Photobacterium damselae To Generate a Highly Sialylated Recombinant α-1-Antitrypsin.
Pallister, Edward G; Choo, Matthew S F; Tai, Jien-Nee; Leong, Dawn S Z; Tang, Wen-Qin; Ng, Say-Kong; Huang, Kun; Marchesi, Andrea; Both, Peter; Gray, Christopher; Rudd, Pauline M; Flitsch, Sabine L; Nguyen-Khuong, Terry.
Afiliación
  • Pallister EG; Bioprocessing Technology Institute, Agency for Science Technology and Research, Singapore 138668.
  • Choo MSF; School of Chemistry and Manchester Institute of Biotechnology (MIB), The University of Manchester, Manchester M1 7DN, United Kingdom.
  • Tai JN; Bioprocessing Technology Institute, Agency for Science Technology and Research, Singapore 138668.
  • Leong DSZ; Bioprocessing Technology Institute, Agency for Science Technology and Research, Singapore 138668.
  • Tang WQ; Bioprocessing Technology Institute, Agency for Science Technology and Research, Singapore 138668.
  • Ng SK; Bioprocessing Technology Institute, Agency for Science Technology and Research, Singapore 138668.
  • Huang K; Bioprocessing Technology Institute, Agency for Science Technology and Research, Singapore 138668.
  • Marchesi A; School of Chemistry and Manchester Institute of Biotechnology (MIB), The University of Manchester, Manchester M1 7DN, United Kingdom.
  • Both P; School of Chemistry and Manchester Institute of Biotechnology (MIB), The University of Manchester, Manchester M1 7DN, United Kingdom.
  • Gray C; School of Chemistry and Manchester Institute of Biotechnology (MIB), The University of Manchester, Manchester M1 7DN, United Kingdom.
  • Rudd PM; School of Chemistry and Manchester Institute of Biotechnology (MIB), The University of Manchester, Manchester M1 7DN, United Kingdom.
  • Flitsch SL; Bioprocessing Technology Institute, Agency for Science Technology and Research, Singapore 138668.
  • Nguyen-Khuong T; School of Chemistry and Manchester Institute of Biotechnology (MIB), The University of Manchester, Manchester M1 7DN, United Kingdom.
Biochemistry ; 59(34): 3123-3128, 2020 09 01.
Article en En | MEDLINE | ID: mdl-31580652
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.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Photobacterium / Sialiltransferasas / Proteínas Recombinantes / Alfa 1-Antitripsina / Ácido N-Acetilneuramínico / Galactosa Idioma: En Revista: Biochemistry Año: 2020 Tipo del documento: Article Pais de publicación: Estados Unidos

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Photobacterium / Sialiltransferasas / Proteínas Recombinantes / Alfa 1-Antitripsina / Ácido N-Acetilneuramínico / Galactosa Idioma: En Revista: Biochemistry Año: 2020 Tipo del documento: Article Pais de publicación: Estados Unidos