Streamlining N-terminally anchored yeast surface display via structural insights into S. cerevisiae Pir proteins.

ABSTRACT: Surface display co-opts yeast's innate ability to embellish its cell wall with mannoproteins, thus converting the yeast's outer surface into a growing and self-sustaining catalyst. However, the efficient toolbox for converting the enzyme of interest into its surface-displayed isoform is currently lacking, especially if the isoform needs to be anchored to the cell wall near the isoform's N-terminus, e.g., through a short GPI-independent protein anchor. Aiming to advance such N-terminally anchored surface display, we employed in silico and machine-learning strategies to study the 3D structure, function, genomic organisation, and evolution of the Pir protein family, whose members evolved to covalently attach themselves near their N-terminus to the β-1,3-glucan of the cell wall. Through the ne

SUBMITTER: Martinic Cezar T 

PROVIDER: S-EPMC10483737 | biostudies-literature | 2023 Sep

REPOSITORIES: biostudies-literature