Structural insights from random mutagenesis of Campylobacter jejuni oligosaccharyltransferase PglB

BMC Biotechnology

Volumn 12, Issue , 2012, Pages

  Ihssen, Julian ^a   Kowarik, Michael ^b   Wiesli, Luzia ^a   Reiss, Renate ^a   Wacker, Michael ^b   Thöny Meyer, Linda ^a  

^a SWISS FEDERAL LABORATORIES FOR MATERIALS SCIENCE AND TECHNOLOGY   (Switzerland)

^b GlycoVaxyn AG   (Switzerland)

Author keywords

Campylobacter jejuni; conjugate vaccine; directed evolution; ELISA; glycosylation; oligosaccharyltransferase; PglB; random mutagenesis; screening

Indexed keywords

CAMPYLOBACTER JEJUNI; CONJUGATE VACCINE; DIRECTED EVOLUTION; ELISA; OLIGOSACCHARYLTRANSFERASE; PGLB; RANDOM MUTAGENESIS;

AMIDES; AMINO ACIDS; ESCHERICHIA COLI; ESTERIFICATION; GLYCOPROTEINS; GLYCOSYLATION; MUTAGENESIS; RECOMBINANT PROTEINS; SCREENING; VACCINES;

BACTERIA;

ALANINE; AMINO ACID; ASPARAGINE; CYSTEINE; GLYCOPROTEIN; NITROGEN; OLIGOSACCHARIDE; OLIGOSACCHARYLTRANSFERASE PGIB; PHENYLALANINE; PSEUDOMONAS EXOTOXIN; TRANSFERASE; TRYPTOPHYLTRYPTOPHYLASPARTYLTYROSYLGLYCINE; UNCLASSIFIED DRUG; VALINE;

AMINO ACID SUBSTITUTION; ARTICLE; ATOM; BACTERIAL GENE; CAMPYLOBACTER JEJUNI; CRYSTAL STRUCTURE; CYTOPLASM; ENZYME LINKED IMMUNOSORBENT ASSAY; ESCHERICHIA COLI; GENE EXPRESSION; GENE MAPPING; GENE MUTATION; GENETIC ENGINEERING; GENETIC VARIABILITY; GLYCOSYLATION; HYDROPHOBICITY; MUTAGENESIS; NONHUMAN; POLYMERASE CHAIN REACTION; PROTEIN DOMAIN; PROTEIN INTERACTION; PROTEIN MOTIF; PSEUDOMONAS AERUGINOSA; SATURATION MUTAGENESIS; SEQUENCE HOMOLOGY; SEROTYPE; STAPHYLOCOCCUS AUREUS; WILD TYPE;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; BACTERIAL PROTEINS; CAMPYLOBACTER JEJUNI; ENZYME-LINKED IMMUNOSORBENT ASSAY; ESCHERICHIA COLI; GLYCOSYLATION; HEXOSYLTRANSFERASES; MEMBRANE PROTEINS; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS;

BACTERIA (MICROORGANISMS); CAMPYLOBACTER JEJUNI; ESCHERICHIA COLI; PSEUDOMONAS AERUGINOSA; STAPHYLOCOCCUS AUREUS;

EID: 84866514981     PISSN: None     EISSN: 14726750     Source Type: Journal    
DOI: 10.1186/1472-6750-12-67     Document Type: Article

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