A novel expression system for Salmonella typhimurium allowing high production levels, product secretion and efficient recovery.
A novel expression system for heterologous production in Salmonella typhimurium, taking advantage of the promoter, signal sequence and two IgG-binding domains (ZZ) from staphylococcal protein A, has been investigated. The production of two different fusion proteins, ZZ-M3 and ZZ-M5, was characterized in terms of production levels, product localization (periplasma or culture medium) and product quality after affinity purification. High expression levels and efficient product secretion were obtained, making the system attractive for vaccine development. The potential use of S. typhimurium as host for heterologous production in biotechnology is discussed.
Liljeqvist
S
S
Department of Biochemistry and Biotechnology, Royal Institute of Technology (KTH), Stockholm, Sweden.
Haddad
D
D
Berzins
K
K
Uhlén
M
M
Ståhl
S
S
D000595:Amino Acid Sequence; D001665:Binding Sites; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism*; D005798:Genes, Bacterial; D007074:Immunoglobulin G / Q000378:metabolism; D008969:Molecular Sequence Data; D008970:Molecular Weight; D011401:Promoter Regions, Genetic; D021382:Protein Sorting Signals / Q000096:biosynthesis / Q000378:metabolism; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis* / Q000302:isolation & purification; D012486:Salmonella typhimurium / Q000235:genetics / Q000254:growth & development / Q000378:metabolism*; D013205:Staphylococcal Protein A / Q000096:biosynthesis* / Q000302:isolation & purification
D007074:Immunoglobulin G; D021382:Protein Sorting Signals; D011993:Recombinant Fusion Proteins; D013205:Staphylococcal Protein A