TABLE 2.
Oligonucleotide | NCBI accession no.b | Identification | Inhibition (fold)c |
---|---|---|---|
EH-IP0234.1 | 17.t00056 | Gal/GalNAc lectin 35 subunit Lgl-1 | 7.4 |
EH-IP0234.2 | 17.t00056 | Gal/GalNAc lectin 35 subunit Lgl-1 | 6.5 |
EH-IP0234.3 | 17.t00056 | Gal/GalNAc lectin 35 subunit Lgl-1 | 1.9 |
EH-IP0816 | 56.t00038 | Gal/GalNAc lectin 35 subunit Lgl-3 | 2.5 |
EH-IP0796.1 | 53.t00006 | Gal/GalNAc lectin subunit Igl1 | 1.8 |
EH-IP0796.2 | 53.t00006 | Gal/GalNAc lectin subunit Igl1 | 2.2 |
EH-IP0100 | 119.t00005 | Gal/GalNAc lectin subunit Igl2 | 6.6 |
EH-IP0491.2 | L14815d | Gal/GalNAc lectin subunit Hgl-3 | 2.4 |
EH-IP0715 | 442.t00004 | Peroxiredoxin | 7.6 |
EH-IP0160 | 136.t00007 | Peroxiredoxin | 18.6 |
EH-IP1002 | 963.t00001 | Peroxiredoxin | 16.7 |
EH-IP0928.2 | 79.t00025 | Cysteine protease 1 | 7.9 |
EH-IP0928.1 | 79.t00025 | Cysteine protease 1 | 9.1 |
EH-IP0409 | 242.t00001 | Cysteine protease 1 | 7.5 |
EH-IP0343.2 | 206.t00005 | Cysteine proteinase 2 | 7.1 |
EH-IP0343.1 | 206.t00005 | Cysteine proteinase 2 | 7.1 |
EH-IP0343.3 | 206.t00005 | Cysteine proteinase 2 | 7.5 |
EH-IP0343.6 | 206.t00005 | Cysteine proteinase 2 | 6.3 |
EH-IP0343.4 | 206.t00005 | Cysteine proteinase 2 | 6.1 |
EH-IP0343.5 | 206.t00005 | Cysteine proteinase 2 | 6.9 |
EH-IP1066 | X87214e | Cysteine protease 3 | 1.3 |
EH-IP0626.2 | 358.t00002 | Cysteine protease 8 | 6.0 |
EH-IP0626.1 | 358.t00002 | Cysteine protease 8 | 7.6 |
EH-IP1070 | AY156071f | Cysteine protease 13 | 2.6 |
EH-IP0261 | 180.t00007 | Cysteine protease 17 | 1.7 |
EH-IP0288.2 | 191.t00018 | Cysteine proteinase | 1.2 |
EH-IP0254.1 | 18.t00027 | Amoebapore C | 7.5 |
EH-IP0254.2 | 18.t00027 | Amoebapore C | 5.2 |
EH-IP0149.2 | 132.t00016 | 20-kDa antigen | 1.7 |
EH-IP0149.1 | 132.t00016 | 20-kDa antigen | 1.4 |
EH-IP0216 | 160.t00008 | Surface antigen ariel1 | 17.4 |
EH-IP0614 | 349.t00010 | Galactokinase | 16.4 |
Notice that the surface molecule ARIEL (an asparagine-rich E. histolytica antigen of unknown function) (12) was down regulated 17-fold by heat shock, whereas amoebapore C was down regulated fivefold. Galactokinase (with a 16-fold down regulation) catalyzes phosphorylation of galactose during its catabolism. The enzyme has attracted significant research attention because of its important metabolic role, notably in humans, where defects in the enzyme can result in the disease state referred to as galactosemia (6). In addition, galactokinase-like molecules have been shown to act as sensors for the intracellular galactose concentration and, under suitable conditions, to function as transcriptional regulators (17).
http://www.ncbi.nlm.nih.gov/gquery/gquery.fcgi?term=ENTAMOEBA.
Rate of inhibition of gene transcription after heat shock.
Hgl-3 allele published in reference 15.
CP3 sequence published in reference 4.
CP13 sequence published in reference 4.