In vivo deglycosylation of recombinant proteins in plants by co-expression with bacterial PNGase F

Mamedov T., Yusibov V.

BIOENGINEERED, cilt.4, sa.5, ss.338-342, 2013 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 4 Sayı: 5
  • Basım Tarihi: 2013
  • Doi Numarası: 10.4161/bioe.23449
  • Dergi Adı: BIOENGINEERED
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.338-342
  • Anahtar Kelimeler: N-linked glycosylation, PNGase F, deglycosylation, plant transient expression, recombinant proteins, malaria vaccine candidate Pfs48/45, ABERRANT N-GLYCOSYLATION, PLASMODIUM-FALCIPARUM, ANTIGEN PFS48/45, TUNICAMYCIN, SUBUNIT
  • Akdeniz Üniversitesi Adresli: Hayır

Özet

At present, several eukaryotic expression systems including yeast, insect and mammalian cells and plants are used for the production of recombinant proteins. Proteins with potential N-glycosylation sites are efficiently glycosylated when expressed in these systems. However, the ability of the eukaryotic expression systems to glycosylate may be not desirable for some proteins. If target proteins that do not carry N-linked glycans in the native host contain potential N-linked glycosylation sites, they can be aberrantly glycosylated in the eukaryotic expression systems, thus, potentially impairing biological activity. Recently, we have developed a strategy of enzymatic deglycosylation of proteins in vivo by co-introducing bacterial PNGase F via agroinfiltration followed by transient expression in plants. 1 Here, we summarize our work on this topic and its potential implications.