Antibody expression in protease-deficient strains of the methylotrophic yeast Ogataea minuta.
FEMS Yeast Res
; 7(8): 1307-16, 2007 Dec.
Article
in En
| MEDLINE
| ID: mdl-17714475
ABSTRACT
When human antibody genes were expressed in the methylotrophic yeast Ogataea minuta, the secreted antibody became partially degraded. To suppress the degradation, a vacuolar protease-deficient strain was constructed and its antibody production was evaluated. Although antibody productivity was improved in the vacuolar protease-deficient strain, the secreted antibody still became partially degraded. Peptide sequencing revealed that the cleavage occurred in the CH1 region of the heavy chain, implying that the cleavage was caused by an aspartic protease, Yps1p. To inhibit this cleavage, Yps1p-deficient strains were constructed and their antibody production was evaluated. As a result, the partial degradation of the antibody was suppressed in the O. minuta multiple-protease-deficient strains.
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Database:
MEDLINE
Main subject:
Peptide Hydrolases
/
Industrial Microbiology
/
Recombinant Proteins
/
Gene Deletion
/
Saccharomycetales
/
Antibodies
Limits:
Humans
Language:
En
Journal:
FEMS Yeast Res
Journal subject:
MICROBIOLOGIA
Year:
2007
Type:
Article
Affiliation country:
Japan