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Hoernstein, S.N.W.* ; Fode, B.* ; Wiedemann, G.* ; Lang, D. ; Niederkrüger, H.* ; Berg, B.* ; Schaaf, A.* ; Frischmuth, T.* ; Schlosser, A.* ; Decker, E.L.* ; Reski, R.*

Host cell proteome of Physcomitrella patens harbors proteases and protease inhibitors under bioproduction conditions.

J. Proteome Res. 17, 3749-3760 (2018)
DOI
Open Access Green as soon as Postprint is submitted to ZB.
Host cell proteins are inevitable contaminants of biopharmaceuticals. Here, we performed detailed analyses of the host cell proteome of moss (Physcomitrella patens) bioreactor supernatants using mass spectrometry and subsequent bioinformatics analysis. Distinguishing between the apparent secretome and intracellular contaminants, a complex extracellular proteolytic network including subtilisin-like proteases, metallo-proteases, and aspartic proteases was identified. Knockout of a subtilisin-like protease affected the overall extracellular proteolytic activity. Besides proteases, also secreted protease-inhibiting proteins such as serpins were identified. Further, we confirmed predicted cleavage sites of 40 endogenous signal peptides employing an N-terminomics approach. The present data provide novel aspects to optimize both product stability of recombinant biopharmaceuticals as well as their maturation along the secretory pathway. Data are available via ProteomeXchange with identifier PXDO09517.
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Publication type Article: Journal article
Document type Scientific Article
Keywords Bioreactor ; Biopharmaceutical ; Moss ; Proteases ; Signal Peptides; Predicting Signal Peptides; By-2 Suspension Cells; Aspartic Proteinase; Arabidopsis-thaliana; Secretory Pathway; Statistical-model; Mass-spectrometry; Moss Bioreactors; Identification; Expression
ISSN (print) / ISBN 1535-3893
e-ISSN 1535-3907
Quellenangaben Volume: 17, Issue: 11, Pages: 3749-3760 Article Number: , Supplement: ,
Publisher American Chemical Society (ACS)
Publishing Place 1155 16th St, Nw, Washington, Dc 20036 Usa
Reviewing status Peer reviewed