title: Cholera toxin B: one subunit with many pharmaceutical applications.
abstract: Cholera, a waterborne acute diarrheal disease caused by Vibrio cholerae, remains prevalent in underdeveloped countries and is a serious health threat to those living in unsanitary conditions. The major virulence factor is cholera toxin (CT), which consists of two subunits: the A subunit (CTA) and the B subunit (CTB). CTB is a 55 kD homopentameric, non-toxic protein binding to the GM1 ganglioside on mammalian cells with high affinity. Currently, recombinantly produced CTB is used as a component of an internationally licensed oral cholera vaccine, as the protein induces potent humoral immunity that can neutralize CT in the gut. Additionally, recent studies have revealed that CTB administration leads to the induction of anti-inflammatory mechanisms in vivo. This review will cover the potential of CTB as an immunomodulatory and anti-inflammatory agent. We will also summarize various recombinant expression systems available for recombinant CTB bioproduction.
authors: Department of Pharmacology and Toxicology, University of Louisville School of Medicine, Louisville, KY 40202, USA. keegan.baldauf@louisville.edu.
authors: Keegan J
authors: KJ
authors: Baldauf
authors: Owensboro Cancer Research Program of James Graham Brown Cancer Center at University of Louisville School of Medicine, Owensboro, KY 42303, USA. joshua.royal@ocrp.org.
authors: Joshua M
authors: JM
authors: Royal
authors: Owensboro Cancer Research Program of James Graham Brown Cancer Center at University of Louisville School of Medicine, Owensboro, KY 42303, USA. krystal.hamorsky@ocrp.org.|Department of Medicine, University of Louisville School of Medicine, Louisville, KY 40202, USA. krystal.hamorsky@ocrp.org.
authors: Krystal Teasley
authors: KT
authors: Hamorsky
authors: Department of Pharmacology and Toxicology, University of Louisville School of Medicine, Louisville, KY 40202, USA. n.matoba@louisville.edu.|Owensboro Cancer Research Program of James Graham Brown Cancer Center at University of Louisville School of Medicine, Owensboro, KY 42303, USA. n.matoba@louisville.edu.
authors: Nobuyuki
authors: N
authors: Matoba
mesh_terms: D000893:Anti-Inflammatory Agents / Q000276:immunology / Q000494:pharmacology; D002772:Cholera Toxin / Q000096:biosynthesis / Q000276:immunology / Q000494:pharmacology*; D022121:Cholera Vaccines / Q000737:chemistry / Q000276:immunology; D005677:G(M1) Ganglioside / Q000378:metabolism; D011485:Protein Binding; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000276:immunology; D014734:Vibrio cholerae / Q000737:chemistry
chemical_list: D000893:Anti-Inflammatory Agents; D022121:Cholera Vaccines; D011994:Recombinant Proteins; D005677:G(M1) Ganglioside; D002772:Cholera Toxin