Antibody engineering reveals the important role of J segments in the production efficiency of llama single-domain antibodies in Saccharomyces cerevisiae

Protein Engineering, Design and Selection

Volumn 25, Issue 1, 2012, Pages 39-46

  Gorlani, A ^a   Lutje Hulsik, D ^b   Adams, H ^c   Vriend, G ^d   Hermans, P ^c   Verrips, T ^a  

^a UTRECHT UNIVERSITY   (Netherlands)

^b UNIV GRENOBLE ALPES   (France)

^c BAC BV   (Netherlands)

^d RADBOUD UNIVERSITY MEDICAL CENTER   (Netherlands)

Author keywords

BiP chaperone; J segment; key residues; protein production; VHH stability

Indexed keywords

ANTIBODY ENGINEERING; BIP CHAPERONE; HEAVY-CHAIN ANTIBODIES; J SEGMENT; KEY RESIDUES; LOWER EUKARYOTES; PRODUCTION EFFICIENCY; PRODUCTION YIELD; PROTEIN PRODUCTION; SECRETION EFFICIENCY; SEQUENCE ANALYSIS; SINGLE DOMAINS; SITE-DIRECTED MUTATION; STRUCTURAL FEATURE; VARIABLE DOMAIN;

EFFICIENCY; MEDICAL APPLICATIONS; PHYSIOLOGY; PRODUCTION; YEAST;

ANTIBODIES;

CHAPERONE; IMMUNOGLOBULIN HEAVY CHAIN; IMMUNOGLOBULIN J CHAIN; LLAMA HEAVY CHAIN ANTIBODY; UNCLASSIFIED DRUG;

ANTIBODY ENGINEERING; ARTICLE; CONTROLLED STUDY; HUMAN; HUMAN CELL; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN SECRETION; SACCHAROMYCES CEREVISIAE; SEQUENCE ANALYSIS; SITE DIRECTED MUTAGENESIS;

AMINO ACID SEQUENCE; ANIMALS; ANTIBODIES; BINDING SITES; CAMELIDS, NEW WORLD; COMPLEMENTARITY DETERMINING REGIONS; HEK293 CELLS; HUMANS; IMMUNOGLOBULIN HEAVY CHAINS; IMMUNOGLOBULIN VARIABLE REGION; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN ENGINEERING; PROTEIN REFOLDING; PROTEIN STRUCTURE, SECONDARY; SACCHAROMYCES CEREVISIAE; SEQUENCE HOMOLOGY, AMINO ACID; TEMPERATURE;

EUKARYOTA; LAMA (MAMMAL); SACCHAROMYCES CEREVISIAE;

EID: 84555194928     PISSN: 17410126     EISSN: 17410134     Source Type: Journal    
DOI: 10.1093/protein/gzr057     Document Type: Article

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