Recombinant O-mannosylated protein production (PstS-1) from Mycobacterium tuberculosis in Pichia pastoris (Komagataella phaffii) as a tool to study tuberculosis infection
Giroshi Bando-Campos, Daniel Juárez-López, Sergio A. Román-González, Antonia I. Castillo‐Rodal, Clarita Olvera, Yolanda López‐Vidal, Roberto Arreguı́n-Espinosa, Clara Espitia, et al. (10 authors)
Microbial Cell Factories · 2019-01
Abstract
Background: Pichia pastoris (syn. Komagataella phaffii) is one of the most highly utilized eukaryotic expression systems for the production of heterologous glycoproteins, being able to perform both N-and O-mannosylation. In this study, we present the expression in P. pastoris of an O-mannosylated recombinant version of the 38 kDa glycolipoprotein PstS-1 from Mycobacterium tuberculosis (Mtb), that is similar in primary structure to the native secreted protein.
MeSH terms
- Pichia pastoris
- Recombinant DNA
- Biology
- Heterologous
- Microbiology
- Mycobacterium tuberculosis
- Signal peptide
- Secretory protein
- Glycoprotein
- Secretion
- Biochemistry
- Molecular biology