The Occurrence of a Tripeptidyl Peptidase I in Trophozoites of Entamoeba histolytica

Flockenhaus, Bettina; Pietersma, Mario; Bakker-Grunwald, Tilly; Scholze, Henning

doi:10.1016/s0188-4409(00)00138-7

Cited by 3 publications

(3 citation statements)

References 2 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Biochemical analysis revealed that these peptidases prefer the substrate Suc-AAF-AMC. This enzymatic feature is identical to that of the E. histolytica tripeptidyl serine peptidase purified by Flockenhaus and colleagues [22]. Unfortunately, no sequence of the purified tripeptidyl peptidase is available.…”

Section: Discussionsupporting

confidence: 66%

See 1 more Smart Citation

The Entamoeba histolytica genome: primary structure and expression of proteolytic enzymes

et al. 2007

View full text Add to dashboard Cite

show abstract

Section: Discussionsupporting

confidence: 66%

“…So far, a collagenase [19], a high molecular weight proteinase [20], a serine-metallo proteinase [21], a tripeptidyl peptidase I [22] and a serine protease [23] have been reported.…”

Section: Introductionmentioning

confidence: 99%

The Entamoeba histolytica genome: primary structure and expression of proteolytic enzymes

et al. 2007

View full text Add to dashboard Cite

show abstract

“…The endosome maturation culminates with the phagosome fusion to the lysosome, forming the phagolysosome, which contains hydrolytic enzymes (EhCP1, EhCP2, EhCP4, EhCP5, amoebapores, phospholipases, dipeptidyl aminopeptidase, β-hexosaminidase, and lysozymes) ( Long-Krug et al., 1985 ; Nickel et al., 1998 ; Flockenhaus et al., 2000 ; Que et al., 2002 ; Andrä et al., 2003 ; Furukawa et al., 2012 ); membrane receptors (Gal/GalNAc lectin) ( Petri et al., 2002 ); and proteins related to cytoskeletal rearrangements and vesicular trafficking, such as EhRabs ( Figure 4 ) ( Marion et al., 2005 ; Okada et al., 2006 ; Saito-Nakano et al., 2007 ; Verma and Datta, 2017 ). In this step, the role of Rabs is crucial to the protein transport and their degradation in lysosomes.…”

Section: The Escrt Machinery and Endosomal Compartments During Phagoc...mentioning

confidence: 99%

Molecular interplays of the Entamoeba histolytica endosomal sorting complexes required for transport during phagocytosis

Bañuelos

Betanzos

Javier-Reyna

et al. 2022

Front. Cell. Infect. Microbiol.

View full text Add to dashboard Cite

Entamoeba histolytica, the causative agent of human amoebiasis, exhibits a continuous membrane remodelling to exert its virulence properties. During this dynamic process, the Endosomal Sorting Complexes Required for Transport (ESCRT) machinery is a key player, particularly in phagocytosis, a virulence hallmark of this parasite. In addition to ESCRT, other molecules contribute to membrane remodelling, including the EhADH adhesin, EhRabs, actin, and the lysobisphosphatidic acid (LBPA). The endocytosis of a prey or molecules induces membrane invaginations, resulting in endosome and multivesicular bodies (MVBs) formation for cargo delivery into lysosomes. Alternatively, some proteins are recycled or secreted. Most of these pathways have been broadly characterized in other biological systems, but poorly described in protozoan parasites. Here, we encompass 10 years of ESCRT research in E. histolytica, highlighting the role of the ESCRT-I and ESCRT-III components and the EhADH and EhVps4-ATPase accessory proteins during phagocytosis. In particular, EhADH exhibits a multifunctional role along the endocytic pathway, from cargo recognition to endosome maturation and lysosomal degradation. Interestingly, the interaction of EhADH with EhVps32 seems to shape a concurrent route to the conventional one for MVBs biogenesis, that could optimize their formation. Furthermore, this adhesin is secreted, but its role in this event remains under study. Other components from the endosomal pathway, such as EhVps23 and LBPA, are also secreted. A proteomic approach performed here, using an anti-LBPA antibody, revealed that some proteins related to membrane trafficking, cellular transport, cytoskeleton dynamics, and transcriptional and translational functions are secreted and associated to LBPA. Altogether, the accumulated knowledge around the ESCRT machinery in E. histolytica, points it out as a dynamic platform facilitating the interaction of molecules participating in different cellular events. Seen as an integrated system, ESCRTs lead to a better understanding of E. histolytica phagocytosis.

show abstract

A novel protease from Entamoeba histolytica homologous to members of the family S28 of serine proteases

Barrios-Ceballos

Martínez‐Gallardo

Anaya-Velázquez

et al. 2005

Experimental Parasitology

View full text Add to dashboard Cite

The Occurrence of a Tripeptidyl Peptidase I in Trophozoites of Entamoeba histolytica

Cited by 3 publications

References 2 publications

The Entamoeba histolytica genome: primary structure and expression of proteolytic enzymes

The Entamoeba histolytica genome: primary structure and expression of proteolytic enzymes

Molecular interplays of the Entamoeba histolytica endosomal sorting complexes required for transport during phagocytosis

A novel protease from Entamoeba histolytica homologous to members of the family S28 of serine proteases

Contact Info

Product

Resources

About