Pertussis toxin

Pertussis toxin, subunit 1
The crystal structure of pertussis toxin,[1]
Identifiers
SymbolPertussis_S1
PfamPF02917
InterProIPR003898
SCOP21bcp / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
Pertussis toxin, subunit 2 and 3
Identifiers
SymbolPertussis_S2S3
PfamPF02918
InterProIPR003899
SCOP21bcp / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
Pertussis toxin, subunit 4
Identifiers
SymbolPertus-S4-tox
PfamPF09275
InterProIPR015355
SCOP21prt / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
Pertussis toxin, subunit 5
Identifiers
SymbolPertus-S5-tox
PfamPF09276
InterProIPR015356
SCOP21prt / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

Pertussis toxin (PT) is a protein-based AB5-type exotoxin produced by the bacterium Bordetella pertussis,[2] which causes whooping cough. PT is involved in the colonization of the respiratory tract and the establishment of infection.[3] Research suggests PT may have a therapeutic role in treating a number of common human ailments, including hypertension,[4] viral infection,[5] and autoimmunity.[6][7][8]

  1. ^ Stein PE, Boodhoo A, Armstrong GD, Cockle SA, Klein MH, Read RJ (January 1994). "The crystal structure of pertussis toxin". Structure. 2 (1): 45–57. doi:10.1016/S0969-2126(00)00007-1. PMID 8075982.
  2. ^ Ryan KJ, Ray CG, eds. (2004). Sherris Medical Microbiology (4th ed.). McGraw Hill. ISBN 0-8385-8529-9.
  3. ^ Carbonetti NH, Artamonova GV, Mays RM, Worthington ZE (November 2003). "Pertussis Toxin Plays an Early Role in Respiratory Tract Colonization by Bordetella pertussis". Infect. Immun. 71 (11): 6358–66. doi:10.1128/IAI.71.11.6358-6366.2003. PMC 219603. PMID 14573656.
  4. ^ Kost C, Herzer W, Li P, Jackson E (1999). "Pertussis toxin-sensitive G-proteins and regulation of blood pressure in the spontaneously hypertensive rat". Clin Exp Pharmacol Physiol. 26 (5–6): 449–55. doi:10.1046/j.1440-1681.1999.03058.x. PMID 10386237. S2CID 12902466.
  5. ^ Alfano M, Pushkarsky T, Poli G, Bukrinsky M (2000). "The B-Oligomer of Pertussis Toxin Inhibits Human Immunodeficiency Virus Type 1 Replication at Multiple Stages". J Virol. 74 (18): 8767–70. doi:10.1128/JVI.74.18.8767-8770.2000. PMC 116391. PMID 10954581.
  6. ^ Bagley K, Abdelwahab S, Tuskan R, Fouts T, Lewis G (2002). "Pertussis toxin and the adenylate cyclase toxin from Bordetella pertussis activate human monocyte-derived dendritic cells and dominantly inhibit cytokine production through a cAMP-dependent pathway". J Leukoc Biol. 72 (5): 962–9. doi:10.1189/jlb.72.5.962. PMID 12429718. S2CID 16457655.
  7. ^ Locht C, Keith JM (1986). "Pertussis toxin gene: nucleotide sequence and genetic organization". Science. 232 (4755): 1258–1264. Bibcode:1986Sci...232.1258L. doi:10.1126/science.3704651. PMID 3704651.
  8. ^ Rappuoli R, Nicosia A, Perugini M, Franzini C, Casagli MC, Borri MG, Antoni G, Almoni M, Neri P, Ratti G (1986). "Cloning and sequencing of the pertussis toxin genes: operon structure and gene duplication". Proc. Natl. Acad. Sci. U.S.A. 83 (13): 4631–4635. Bibcode:1986PNAS...83.4631N. doi:10.1073/pnas.83.13.4631. PMC 323795. PMID 2873570.