KEGG   PATHWAY: csab05146
Entry
csab05146                   Pathway                                
Name
Amoebiasis - Chlorocebus sabaeus (green monkey)
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
csab05146  Amoebiasis
csab05146

Organism
Chlorocebus sabaeus (green monkey) [GN:csab]
Gene
103241278  IL1B; interleukin 1 beta [KO:K04519]
103241149  IL1R1; interleukin 1 receptor type 1 [KO:K04386]
103241146  IL1R2; interleukin 1 receptor type 2 [KO:K04387]
103236047  NFKB1; nuclear factor kappa B subunit 1 [KO:K02580]
103227364  RELA; RELA proto-oncogene, NF-kB subunit [KO:K04735]
103246661  heat shock protein beta-1 [KO:K04455]
103235330  MUC2; mucin 2, oligomeric mucus/gel-forming [KO:K10955]
103242943  COL1A1; collagen type I alpha 1 chain [KO:K06236]
103226536  COL1A2; collagen type I alpha 2 chain [KO:K06236]
103214793  COL4A2; collagen type IV alpha 2 chain [KO:K06237]
103214795  COL4A1; collagen type IV alpha 1 chain [KO:K06237]
103217991  COL4A3; collagen type IV alpha 3 chain [KO:K06237]
103217992  COL4A4; collagen type IV alpha 4 chain [KO:K06237]
103232468  COL4A5; collagen type IV alpha 5 chain [KO:K06237]
103232470  COL4A6; collagen type IV alpha 6 chain [KO:K06237]
103217800  FN1; fibronectin 1 [KO:K05717]
103240395  LAMA2; laminin subunit alpha 2 [KO:K05637]
103222731  LAMA1; laminin subunit alpha 1 [KO:K05637]
103243076  LAMA5; laminin subunit alpha 5 [KO:K06240]
103222632  LAMA3; laminin subunit alpha 3 [KO:K06240]
103240557  LAMA4; laminin subunit alpha 4 [KO:K06241]
103226726  LAMB1; laminin subunit beta 1 [KO:K05636]
103227619  LAMB2; laminin subunit beta 2 [KO:K06243]
103230157  LAMB3; laminin subunit beta 3 [KO:K06244]
103226727  LAMB4; laminin subunit beta 4 [KO:K06245]
103230459  LAMC1; laminin subunit gamma 1 [KO:K05635]
103230458  LAMC2; laminin subunit gamma 2 [KO:K06246]
103239930  LAMC3; laminin subunit gamma 3 [KO:K06247]
103236614  CASP3; caspase 3 [KO:K02187] [EC:3.4.22.56]
103229828  putative V-set and immunoglobulin domain-containing-like protein IGHV4OR15-8 [KO:K06856]
103224088  uncharacterized LOC103224088 [KO:K06856]
103229820  putative V-set and immunoglobulin domain-containing-like protein IGHV4OR15-8 [KO:K06856]
103229838  putative V-set and immunoglobulin domain-containing-like protein IGHV4OR15-8 [KO:K06856]
103229839  uncharacterized LOC103229839 [KO:K06856]
103229845  putative V-set and immunoglobulin domain-containing-like protein IGHV4OR15-8 [KO:K06856]
103229849  putative V-set and immunoglobulin domain-containing-like protein IGHV4OR15-8 [KO:K06856]
103229850  putative V-set and immunoglobulin domain-containing-like protein IGHV4OR15-8 [KO:K06856]
103229864  uncharacterized LOC103229864 [KO:K06856]
103247608  uncharacterized LOC103247608 [KO:K06856]
103229935  uncharacterized LOC103229935 [KO:K06856]
103229939  putative V-set and immunoglobulin domain-containing-like protein IGHV4OR15-8 [KO:K06856]
103229942  uncharacterized LOC103229942 [KO:K06856]
103229943  uncharacterized LOC103229943 [KO:K06856]
103219624  GNAQ; G protein subunit alpha q [KO:K04634]
103233670  GNA11; G protein subunit alpha 11 [KO:K04635]
103219621  GNA14; G protein subunit alpha 14 [KO:K04636]
103233671  GNA15; G protein subunit alpha 15 [KO:K04637]
103233299  PLCB3; phospholipase C beta 3 [KO:K05858] [EC:3.1.4.11]
103246591  PLCB4; phospholipase C beta 4 [KO:K05858] [EC:3.1.4.11]
103246657  PLCB1; phospholipase C beta 1 [KO:K05858] [EC:3.1.4.11]
103245842  PLCB2; phospholipase C beta 2 [KO:K05858] [EC:3.1.4.11]
103243171  PRKCA; protein kinase C alpha [KO:K02677] [EC:2.7.11.13]
103229829  PRKCB; protein kinase C beta [KO:K19662] [EC:2.7.11.13]
103235232  PRKCG; protein kinase C gamma [KO:K19663] [EC:2.7.11.13]
103243509  GNAS; GNAS complex locus [KO:K04632]
103243499  neuroendocrine secretory protein 55 [KO:K04632]
103222785  GNAL; G protein subunit alpha L [KO:K04633]
103226115  ADCY1; adenylate cyclase 1 [KO:K08041] [EC:4.6.1.1]
103219549  PRKACG; protein kinase cAMP-activated catalytic subunit gamma [KO:K04345] [EC:2.7.11.11]
103224540  PRKACB; protein kinase cAMP-activated catalytic subunit beta [KO:K04345] [EC:2.7.11.11]
103234377  cAMP-dependent protein kinase catalytic subunit alpha-like [KO:K04345] [EC:2.7.11.11]
103241745  RAB5A; RAB5A, member RAS oncogene family [KO:K07887]
103238494  RAB5B; RAB5B, member RAS oncogene family [KO:K07888]
103243420  RAB5C; RAB5C, member RAS oncogene family [KO:K07889]
103228088  RAB7A; RAB7A, member RAS oncogene family [KO:K07897]
103230208  RAB7B; RAB7B, member RAS oncogene family [KO:K07898]
103236415  toll-like receptor 2 [KO:K10159]
103218937  TLR4; toll like receptor 4 [KO:K10160]
103244663  CD14; CD14 molecule [KO:K04391]
103226390  IL6; interleukin 6 [KO:K05405]
103235789  CXCL1; C-X-C motif chemokine ligand 1 [KO:K05505]
103235792  growth-regulated protein homolog gamma-like [KO:K05505]
103235798  CXCL3; C-X-C motif chemokine ligand 3 [KO:K05505]
103236682  growth-regulated alpha protein-like [KO:K05505]
103244503  CSF2; colony stimulating factor 2 [KO:K05427]
103235786  CXCL8; C-X-C motif chemokine ligand 8 [KO:K10030]
103241402  IL12A; interleukin 12A [KO:K05406]
103244892  IL12B; interleukin 12B [KO:K05425]
103223791  CD1E; CD1e molecule [KO:K06448]
103223792  CD1B; CD1b molecule [KO:K06448]
103223793  CD1C; CD1c molecule [KO:K06448]
103223794  T-cell surface glycoprotein CD1a [KO:K06448]
103223798  CD1D; CD1d molecule [KO:K06448]
103225866  T-cell surface glycoprotein CD1a-like [KO:K06448]
103238673  IFNG; interferon gamma [KO:K04687]
103217501  COL3A1; collagen type III alpha 1 chain [KO:K19720]
103237724  PTK2; protein tyrosine kinase 2 [KO:K05725] [EC:2.7.10.2]
103215981  VCL; vinculin [KO:K05700]
103234638  ACTN4; actinin alpha 4 [KO:K05699]
103229232  ACTN1; actinin alpha 1 [KO:K05699]
103229213  ARG2; arginase 2 [KO:K01476] [EC:3.5.3.1]
103240376  ARG1; arginase 1 [KO:K01476] [EC:3.5.3.1]
103242598  nitric oxide synthase, inducible-like [KO:K13241] [EC:1.14.13.39]
103242600  NOS2; nitric oxide synthase 2 [KO:K13241] [EC:1.14.13.39]
103220048  ITGB2; integrin subunit beta 2 [KO:K06464]
103231383  ITGAM; integrin subunit alpha M [KO:K06461]
103234391  PIK3R2; phosphoinositide-3-kinase regulatory subunit 2 [KO:K02649]
103224900  PIK3R3; phosphoinositide-3-kinase regulatory subunit 3 [KO:K02649]
103222594  PIK3R1; phosphoinositide-3-kinase regulatory subunit 1 [KO:K02649]
103221212  PIK3CA; phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit alpha [KO:K00922] [EC:2.7.1.153]
103241599  PIK3CB; phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit beta [KO:K00922] [EC:2.7.1.153]
103225637  PIK3CD; phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit delta [KO:K00922] [EC:2.7.1.153]
103224911  PRDX1; peroxiredoxin 1 [KO:K13279] [EC:1.11.1.24]
103222289  SERPINB6; serpin family B member 6 [KO:K13963]
103222292  SERPINB9; serpin family B member 9 [KO:K13963]
103244154  serpin B4 [KO:K13963]
103244149  SERPINB10; serpin family B member 10 [KO:K13963]
103244157  SERPINB13; serpin family B member 13 [KO:K13963]
103244151  HMSD; histocompatibility minor serpin domain containing [KO:K13963]
103228742  CTSG; cathepsin G [KO:K01319] [EC:3.4.21.20]
103230190  IL10; interleukin 10 [KO:K05443]
103234729  TGFB1; transforming growth factor beta 1 [KO:K13375]
103230082  TGFB2; transforming growth factor beta 2 [KO:K13376]
103229367  TGFB3; transforming growth factor beta 3 [KO:K13377]
103224738  C8A; complement C8 alpha chain [KO:K03997]
103224737  C8B; complement C8 beta chain [KO:K03998]
103215165  C9; complement C9 [KO:K04000]
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
PMID:11378035
  Authors
Stanley SL
  Title
Pathophysiology of amoebiasis.
  Journal
Trends Parasitol 17:280-5 (2001)
DOI:10.1016/S1471-4922(01)01903-1
Reference
PMID:10756002
  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
PMID:14700586
  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
PMID:15813717
  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
PMID:19207103
  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
PMID:17576362
  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
PMID:12660071
  Authors
Stanley SL Jr
  Title
Amoebiasis.
  Journal
Lancet 361:1025-34 (2003)
DOI:10.1016/S0140-6736(03)12830-9
Reference
PMID:14502002
  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
PMID:12142490
  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
PMID:18725798
  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
PMID:12160867
  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
PMID:17702556
  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
PMID:20303955
  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
PMID:16380324
  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
PMID:10637584
  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
PMID:11352795
  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
PMID:20145703
  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
csab00330  Arginine and proline metabolism
csab00590  Arachidonic acid metabolism
csab04144  Endocytosis
csab04210  Apoptosis
csab04510  Focal adhesion
csab04610  Complement and coagulation cascades
csab04612  Antigen processing and presentation
csab04620  Toll-like receptor signaling pathway
csab04672  Intestinal immune network for IgA production
csab04810  Regulation of actin cytoskeleton
KO pathway
ko05146   
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