A homologue of the cysteine proteinase gene (ACP or Eh-CPp) of pathogenic Entamoeba histolytica is present in non-pathogenic E. dispar strains

Mirelman, David; Nuchamowitz, Yael; Böhm-Gloning, B; Walderich, Brigitte

doi:10.1016/s0166-6851(96)02603-5

Cited by 16 publications

(9 citation statements)

References 19 publications

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“…The most abundant RNA in E. dispar corresponded to edcp3, a gene previously suggested not to be present in E. dispar (Reed et al, 1993). Our results, however, are in agreement with very recent data indicating the presence and expression of a gene in E. dispar that has a high degree of homology to E. histolytica ehcp3 (Bruchhaus and Tannich, 1996;Mirelman et al, 1996). On the other hand, our results indicate that analogues to two other cysteine proteinase genes, namely ehcp1 and ehcp5, are not present in E. dispar.…”

Section: Discussionsupporting

confidence: 92%

Entamoeba histolytica and Entamoeba dispar: differences in numbers and expression of cysteine proteinase genes

Bruchhaus

Jacobs

Leippe

et al. 1996

Molecular Microbiology

164

142

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In order to identify molecules that might be responsible for the difference in pathogenicity between the two closely related protozoan parasites Entamoeba histolytica and Entamoeba dispar, we focussed on cysteine proteinases because this class of enzymes has been considered important for pathogenic tissue destruction. By screening a genomic library derived from an E. histolytica isolate, a total of six distinct genes (ehcp1-ehcp6) encoding typical prepro-forms of cysteine proteinases were identified which differed from each other by 40% to 85% of their nucleotide sequences. Three of these genes, ehcp1, ehcp2, and ehcp5, which exhibited high levels of expression, were found to be responsible for approximately 90% of cysteine proteinase transcripts, whereas the remaining three were either not or only marginally expressed. Expression of the different genes directly correlated with the level of activity of the respective enzymes in trophozoite lysates. Purification of the enzymes and N-terminal sequencing revealed that virtually all cysteine proteinase activity of E. histolytica can be attributed to three enzymes namely EhCP1, EhCP2 and EhCP5. Southern blot analysis indicated that just two of these abundantly expressed genes are missing in E. dispar. On the other hand, genes analogous to four of the six genes identified in E. histolytica were found to be present in E. dispar, but only two of these are expressed within the trophozoite stage.

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Section: Discussionsupporting

confidence: 92%

Entamoeba histolytica and Entamoeba dispar: differences in numbers and expression of cysteine proteinase genes

Bruchhaus

Jacobs

Leippe

et al. 1996

Molecular Microbiology

164

142

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“…The molecular mass of the purified amoeba protease described in our present work is 70 kDa, whereas the products of all the cysteine protease genes reported (Reed et al 1993;Bruchhaus et al 1996;Mirelman et al 1996) predicted proteases of around 28 kDa. It must be taken into account that the protease was purified and analysed under non-reducing conditions, since the proteolytic activity is well preserved during its purification.…”

Section: Discussioncontrasting

confidence: 45%

Inhibition of Entamoeba histolytica proteolytic activity by human salivary IgA antibodies

Guerrero-Manríquez

Sánchez-Ibarra

Ávila

1998

APMIS

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Entamoeba histolytica is a protozoan parasite that causes amoebiasis in humans; as the infection occurs mainly in the intestinal epithelium, the secretory immune response of the host could have an influence on the outcome. Secretory IgA antibodies against E. histolytica have been detected in asymptomatic and symptomatic patients, but little is known about their protective role. E. histolytica cysteine proteases seem to be involved in the pathogenesis of amoebiasis; therefore, it is important to evaluate the human IgA response against these proteases and its effect on their enzymatic activity. When human saliva samples with and without antibodies against E. histolytica were tested by Western blot against one purified 70 kDa amoebic cysteine protease, 84% of anti‐amoeba‐positive samples recognized it. The secretory IgA purified from a pool of anti‐protease‐positive samples had a strong in vitro inhibitory effect on the E. histolytica proteolytic activity. These results suggest that this effect, if it occurs in vivo, could be an important protective factor against this parasite.

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“…There is debate as to which genes are present in E. histolytica but absent in E. dispar. acp1 (ehcp3) was initially reported to be present in E. histolytica alone (84), but a related homologue (edcp3) with 95% identity was found in E. dispar (12,62). ehcp1 (acp3) is a second gene reported to be unique to E. histolytica (12), but sequences were detected in clinical strains of E. dispar (84).…”

Section: Structure and Processing Of Amebic Cysteine Proteinasesmentioning

confidence: 99%

Cysteine Proteinases and the Pathogenesis of Amebiasis

Que

Reed

2000

Clinical Microbiology Reviews

206

108

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A homologue of the cysteine proteinase gene (ACP or Eh-CPp) of pathogenic Entamoeba histolytica is present in non-pathogenic E. dispar strains

Cited by 16 publications

References 19 publications

Entamoeba histolytica and Entamoeba dispar: differences in numbers and expression of cysteine proteinase genes

Entamoeba histolytica and Entamoeba dispar: differences in numbers and expression of cysteine proteinase genes

Inhibition of Entamoeba histolytica proteolytic activity by human salivary IgA antibodies

Cysteine Proteinases and the Pathogenesis of Amebiasis

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