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Role of BGS13 in the Secretory Mechanism of Pichia pastoris
Author(s) -
Christopher A. Naranjo,
Anita Jivan,
Maria Vo,
Katherine Helen de Sa Campos,
Jared Deyarmin,
Ryan Hekman,
Christina Uribe,
Aaron Hang,
Kai Her,
Michelle M. Fong,
Joyce Choi,
Caroline Chou,
Taylor Rabara,
Gina Myers,
Pachai Moua,
Der Thor,
Douglas D. Risser,
Craig Vierra,
Andreas H. Franz,
Joan LinCereghino,
Geoff P. LinCereghino
Publication year - 2019
Publication title -
applied and environmental microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.552
H-Index - 324
eISSN - 1070-6291
pISSN - 0099-2240
DOI - 10.1128/aem.01615-19
Subject(s) - pichia pastoris , mechanism (biology) , pichia , biology , computational biology , evolutionary biology , genetics , recombinant dna , gene , philosophy , epistemology
The yeastPichia pastoris is used as a host system for the expression of recombinant proteins. Many of these products, including antibodies, vaccine antigens, and therapeutic proteins such as insulin, are currently on the market or in late stages of development. However, one major weakness is that sometimes these proteins are not secreted from the yeast cell efficiently, which impedes and raises the cost of purification of these vital proteins. Our laboratory has isolated a mutant strain ofPichia pastoris that shows enhanced secretion of many proteins. The mutant produces a modified version of Bgs13p. Our goal is to understand how the change in the Bgs13p function leads to improved secretion. Once the Bgs13p mechanism is illuminated, we should be able to apply this understanding to engineer newP. pastoris strains that efficiently produce and secrete life-saving recombinant proteins, providing medical and economic benefits.

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