KEGG   PATHWAY: ko05146
Entry
ko05146                     Pathway                                
Name
Amoebiasis
Description
Entamoeba histolytica, an extracellular protozoan parasite is a human pathogen that invades the intestinal epithelium. Infection occurs on ingestion of contaminated water and food. The pathogenesis of amoebiasis begins with parasite attachment and disruption of the intestinal mucus layer, followed by apoptosis of host epithelial cells. Intestinal tissue destruction causes severe dysentery and ulcerations in amoebic colitis. Several amoebic proteins such as lectins, cysteine proteineases, and amoebapores are associated with the invasion process. The parasite can cause extraintestinal infection like amoebic liver abscess by evading immune response.
Class
Human Diseases; Infectious disease: parasitic
Pathway map
ko05146  Amoebiasis
ko05146

Disease
H00360  Amoebiasis
Orthology
K00922  PIK3CA_B_D; phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit alpha/beta/delta [EC:2.7.1.153]
K01319  CTSG; cathepsin G [EC:3.4.21.20]
K01476  rocF, arg; arginase [EC:3.5.3.1]
K02187  CASP3; caspase 3 [EC:3.4.22.56]
K02580  NFKB1; nuclear factor NF-kappa-B p105 subunit
K02649  PIK3R1_2_3; phosphoinositide-3-kinase regulatory subunit alpha/beta/delta
K02677  PRKCA; classical protein kinase C alpha type [EC:2.7.11.13]
K03156  TNF, TNFA; tumor necrosis factor superfamily, member 2
K03997  C8A; complement component 8 subunit alpha
K03998  C8B; complement component 8 subunit beta
K03999  C8G; complement component 8 subunit gamma
K04000  C9; complement component 9
K04072  adhE; acetaldehyde dehydrogenase / alcohol dehydrogenase [EC:1.2.1.10 1.1.1.1]
K04345  PKA; protein kinase A [EC:2.7.11.11]
K04386  IL1R1, CD121a; interleukin 1 receptor type I
K04387  IL1R2, CD121b; interleukin 1 receptor type II
K04391  CD14; monocyte differentiation antigen CD14
K04455  HSPB1; heat shock protein beta-1
K04519  IL1B; interleukin 1 beta
K04632  GNAS; guanine nucleotide-binding protein G(s) subunit alpha
K04633  GNAL; guanine nucleotide-binding protein G(olf) subunit alpha
K04634  GNAQ; guanine nucleotide-binding protein G(q) subunit alpha
K04635  GNA11; guanine nucleotide-binding protein subunit alpha-11
K04636  GNA14; guanine nucleotide-binding protein subunit alpha-14
K04637  GNA15; guanine nucleotide-binding protein subunit alpha-15
K04687  IFNG; interferon gamma
K04735  RELA; transcription factor p65
K05405  IL6; interleukin 6
K05406  IL12A; interleukin 12A
K05425  IL12B; interleukin 12B
K05427  CSF2, GMCSF; granulocyte-macrophage colony-stimulating factor
K05443  IL10, CSIF; interleukin 10
K05505  CXCL1_2_3, GRO; C-X-C motif chemokine 1/2/3
K05635  LAMC1; laminin, gamma 1
K05636  LAMB1; laminin, beta 1
K05637  LAMA1_2; laminin, alpha 1/2
K05699  ACTN1_4; actinin alpha 1/4
K05700  VCL; vinculin
K05717  FN1; fibronectin 1
K05725  PTK2, FAK; focal adhesion kinase 1 [EC:2.7.10.2]
K05858  PLCB; phosphatidylinositol phospholipase C, beta [EC:3.1.4.11]
K06236  COL1A; collagen type I alpha
K06237  COL4A; collagen type IV alpha
K06240  LAMA3_5; laminin, alpha 3/5
K06241  LAMA4; laminin, alpha 4
K06243  LAMB2; laminin, beta 2
K06244  LAMB3; laminin, beta 3
K06245  LAMB4; laminin, beta 4
K06246  LAMC2; laminin, gamma 2
K06247  LAMC3; laminin, gamma 3
K06448  CD1; T-cell surface glycoprotein CD1
K06461  ITGAM, CD11b; integrin alpha M
K06464  ITGB2, CD18; integrin beta 2
K06856  IGH; immunoglobulin heavy chain
K07887  RAB5A; Ras-related protein Rab-5A
K07888  RAB5B; Ras-related protein Rab-5B
K07889  RAB5C; Ras-related protein Rab-5C
K07897  RAB7A; Ras-related protein Rab-7A
K07898  RAB7B; Ras-related protein Rab-7B
K08041  ADCY1; adenylate cyclase 1 [EC:4.6.1.1]
K08570  EHCP; histolysain [EC:3.4.22.35]
K10030  IL8, CXCL8; interleukin 8
K10159  TLR2, CD282; toll-like receptor 2
K10160  TLR4, CD284; toll-like receptor 4
K10955  MUC2; mucin-2
K13241  NOS2; nitric-oxide synthase, inducible [EC:1.14.13.39]
K13279  PRDX1; peroxiredoxin 1 [EC:1.11.1.24]
K13375  TGFB1; transforming growth factor beta-1
K13376  TGFB2; transforming growth factor beta-2
K13377  TGFB3; transforming growth factor beta-3
K13963  SERPINB; serpin B
K13968  CP112; cysteine proteinase
K13969  ADH112; adhesin
K13970  HGL; galactose-inhibitable lectin heavy subunit
K13971  LGL; galactose-inhibitable lectin light subunit
K13972  IGL; galactose-inhibitable lectin intermediate subunit
K13973  AP; pore-forming peptide ameobapore
K13974  EHCBP; calcium-binding protein
K13975  PATMK; phagosome-associated TMK96
K13976  EHPAK; p21-activated kinase
K13977  EHLIMA; LIM domain-containing protein
K13978  ACTNL; actinin-like protein
K19662  PRKCB; classical protein kinase C beta type [EC:2.7.11.13]
K19663  PRKCG; classical protein kinase C gamma type [EC:2.7.11.13]
K19720  COL3A; collagen type III alpha
K23601  SREHP; serine-rich protein
K23602  EhSTIRP; serine-threonine-isoleucine rich protein
Compound
C00027  Hydrogen peroxide
C00062  L-Arginine
C00076  Calcium cation
C00165  Diacylglycerol
C00219  Arachidonate
C00533  Nitric oxide
C00575  3',5'-Cyclic AMP
C00584  Prostaglandin E2
C01074  N-Acetylgalactosamine
C01245  D-myo-Inositol 1,4,5-trisphosphate
C01498  Gelatine
C02737  Phosphatidylserine
C18287  Monocyte locomotion inhibitory factor
Reference
  Authors
Stanley SL
  Title
Pathophysiology of amoebiasis.
  Journal
Trends Parasitol 17:280-5 (2001)
DOI:10.1016/S1471-4922(01)01903-1
Reference
  Authors
Espinosa-Cantellano M, Martinez-Palomo A
  Title
Pathogenesis of intestinal amebiasis: from molecules to disease.
  Journal
Clin Microbiol Rev 13:318-31 (2000)
DOI:10.1128/CMR.13.2.318-331.2000
Reference
PMID:9832261
  Authors
Huston CD, Petri WA Jr
  Title
Host-pathogen interaction in amebiasis and progress in vaccine development.
  Journal
Eur J Clin Microbiol Infect Dis 17:601-14 (1998)
DOI:10.1007/BF01708342
Reference
  Authors
Huston CD
  Title
Parasite and host contributions to the pathogenesis of amebic colitis.
  Journal
Trends Parasitol 20:23-6 (2004)
DOI:10.1016/j.pt.2003.10.013
Reference
  Authors
Campos-Rodriguezp R, Jarillo-Luna A
  Title
The pathogenicity of Entamoeba histolytica is related to the capacity of evading innate immunity.
  Journal
Parasite Immunol 27:1-8 (2005)
DOI:10.1111/j.1365-3024.2005.00743.x
Reference
  Authors
Lejeune M, Rybicka JM, Chadee K
  Title
Recent discoveries in the pathogenesis and immune response toward Entamoeba histolytica.
  Journal
Future Microbiol 4:105-18 (2009)
DOI:10.2217/17460913.4.1.105
Reference
  Authors
Carrero JC, Cervantes-Rebolledo C, Aguilar-Diaz H, Diaz-Gallardo MY, Laclette JP, Morales-Montor J
  Title
The role of the secretory immune response in the infection by Entamoeba histolytica.
  Journal
Parasite Immunol 29:331-8 (2007)
DOI:10.1111/j.1365-3024.2007.00955.x
Reference
  Authors
Stanley SL Jr
  Title
Amoebiasis.
  Journal
Lancet 361:1025-34 (2003)
DOI:10.1016/S0140-6736(03)12830-9
Reference
  Authors
Stauffer W, Ravdin JI
  Title
Entamoeba histolytica: an update.
  Journal
Curr Opin Infect Dis 16:479-85 (2003)
DOI:10.1097/01.qco.0000092821.42392.ca
Reference
  Authors
Petri WA Jr, Haque R, Mann BJ
  Title
The bittersweet interface of parasite and host: lectin-carbohydrate interactions during human invasion by the parasite Entamoeba histolytica.
  Journal
Annu Rev Microbiol 56:39-64 (2002)
DOI:10.1146/annurev.micro.56.012302.160959
Reference
  Authors
Baxt LA, Singh U
  Title
New insights into Entamoeba histolytica pathogenesis.
  Journal
Curr Opin Infect Dis 21:489-94 (2008)
DOI:10.1097/QCO.0b013e32830ce75f
Reference
  Authors
Petri WA Jr
  Title
Pathogenesis of amebiasis.
  Journal
Curr Opin Microbiol 5:443-7 (2002)
DOI:10.1016/S1369-5274(02)00335-1
Reference
  Authors
Guo X, Houpt E, Petri WA Jr
  Title
Crosstalk at the initial encounter: interplay between host defense and ameba survival strategies.
  Journal
Curr Opin Immunol 19:376-84 (2007)
DOI:10.1016/j.coi.2007.07.005
Reference
  Authors
Mortimer L, Chadee K
  Title
The immunopathogenesis of Entamoeba histolytica.
  Journal
Exp Parasitol 126:366-80 (2010)
DOI:10.1016/j.exppara.2010.03.005
Reference
  Authors
Meza I, Talamas-Rohana P, Vargas MA
  Title
The cytoskeleton of Entamoeba histolytica: structure, function, and regulation by signaling pathways.
  Journal
Arch Med Res 37:234-43 (2006)
DOI:10.1016/j.arcmed.2005.09.008
Reference
  Authors
Meza I
  Title
Extracellular matrix-induced signaling in Entamoeba histolytica: its role in invasiveness.
  Journal
Parasitol Today 16:23-8 (2000)
DOI:10.1016/S0169-4758(99)01586-0
Reference
  Authors
Stanley SL Jr, Reed SL
  Title
Microbes and microbial toxins: paradigms for microbial-mucosal interactions. VI. Entamoeba histolytica: parasite-host interactions.
  Journal
Am J Physiol Gastrointest Liver Physiol 280:G1049-54 (2001)
DOI:10.1152/ajpgi.2001.280.6.G1049
Reference
  Authors
Wong-Baeza I, Alcantara-Hernandez M, Mancilla-Herrera I, Ramirez-Saldivar I, Arriaga-Pizano L, Ferat-Osorio E, Lopez-Macias C, Isibasi A
  Title
The role of lipopeptidophosphoglycan in the immune response to Entamoeba histolytica.
  Journal
J Biomed Biotechnol 2010:254521 (2010)
DOI:10.1155/2010/254521
Related
pathway
ko00330  Arginine and proline metabolism
ko00590  Arachidonic acid metabolism
ko04144  Endocytosis
ko04210  Apoptosis
ko04510  Focal adhesion
ko04610  Complement and coagulation cascades
ko04612  Antigen processing and presentation
ko04620  Toll-like receptor signaling pathway
ko04672  Intestinal immune network for IgA production
ko04810  Regulation of actin cytoskeleton

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