N-acetyl-β-d-hexosaminidase from Trichomonas vaginalis: substrate specificity and activity of inhibitors

Sanon, Albertine; Tournaire‐Arellano, Cecile; Hage, Salim; Bories, Christian; Caujolle, R.; Loiseau, Philippe M.

doi:10.1016/j.biopha.2004.09.013

Cited by 8 publications

(12 citation statements)

References 10 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The effect of HgCl 2 on Pcb-NAHA1 activity is in accordance with properties of b-N-acetylhexosaminidase from rice [13,52,53]. Moreover, 0.1 mM HgCl 2 was able to inhibit the b-N-acetylhexosaminidase from green crab (Scylla serrata) [42].…”

Section: Effect Of Chemical Compounds On Enzyme Activitysupporting

confidence: 70%

“…For other b-N-acetylhexosaminidases, K m values ranging from 0.006 to 1.65 mM have been reported [4,52,53]. Variations in the K m can occur among different b-N-acetylhexosaminidases, which can be more or less specific towards the same substrate.…”

Section: Determination Of K M and V Maxmentioning

confidence: 99%

“…Additionally, when different substrates are used with the same enzyme, a considerable variation in K m values can be observed. For example, the N-acetyl-b-D-hexosaminidase from T. vaginalis showed a K m value 1000 times lower when assayed against 4-MUsubstrates than when using PNP-substrates [52].…”

Section: Determination Of K M and V Maxmentioning

confidence: 99%

See 2 more Smart Citations

Identification of a novel β-N-acetylhexosaminidase (Pcb-NAHA1) from marine Zoanthid Palythoa caribaeorum (Cnidaria, Anthozoa, Zoanthidea)

Souza

Grossi-de-Sá

Silva

et al. 2008

Protein Expression and Purification

View full text Add to dashboard Cite

Section: Effect Of Chemical Compounds On Enzyme Activitysupporting

confidence: 70%

Section: Determination Of K M and V Maxmentioning

confidence: 99%

See 1 more Smart Citation

Identification of a novel β-N-acetylhexosaminidase (Pcb-NAHA1) from marine Zoanthid Palythoa caribaeorum (Cnidaria, Anthozoa, Zoanthidea)

Souza

Grossi-de-Sá

Silva

et al. 2008

Protein Expression and Purification

View full text Add to dashboard Cite

Section: Discussionmentioning

confidence: 79%

“…Interestingly, one copy (TVAG_110660) possesses a single TMD and was shared between the secretome and the surface proteome. Its cell membrane localization and previously determined N-acetyl-β-D-glucosaminidase activity in T. vaginalis ( 88 ) suggest that β-hexosaminidase may participate in T. vaginalis virulence via host mucin degradation. Interestingly, in E. histolytica , β-hexosaminidase is transported to the phagolysosome by a unique cysteine protease binding protein family 8 (CPBF8) receptor that is not present in T. vaginalis ( 26 ).…”

Section: Discussionmentioning

confidence: 82%

Proteomic Analysis of Trichomonas vaginalis Phagolysosome, Lysosomal Targeting, and Unconventional Secretion of Cysteine Peptidases

Zimmann

Rada

Žárský

et al. 2022

Molecular & Cellular Proteomics

View full text Add to dashboard Cite

The lysosome represents a central degradative compartment of eukaryote cells, yet little is known about the biogenesis and function of this organelle in parasitic protists. Whereas the mannose 6-phosphate (M6P)-dependent system is dominant for lysosomal targeting in metazoans, oligosaccharide-independent sorting has been reported in other eukaryotes. In this study, we investigated the phagolysosomal proteome of the human parasite Trichomonas vaginalis , its protein targeting and the involvement of lysosomes in hydrolase secretion. The organelles were purified using Percoll and OptiPrep gradient centrifugation and a novel purification protocol based on the phagocytosis of lactoferrin-covered magnetic nanoparticles. The analysis resulted in a lysosomal proteome of 462 proteins, which were sorted into 21 classes. Hydrolases represented the largest functional class and included proteases, lipases, phosphatases, and glycosidases. Identification of a large set of proteins involved in vesicular trafficking (80) and turnover of actin cytoskeleton rearrangement (29) indicate a dynamic phagolysosomal compartment. Several cysteine proteases such as TvCP2 were previously shown to be secreted. Our experiments showed that secretion of TvCP2 was strongly inhibited by chloroquine, which increases intralysosomal pH, thus indicating that TvCP2 secretion occurs through lysosomes rather than the classical secretory pathway. Unexpectedly, we identified divergent homologues of the M6P receptor TvMPR in the phagolysosomal proteome, although T. vaginalis lacks enzymes for M6P formation. To test whether oligosaccharides are involved in lysosomal targeting, we selected the lysosome-resident cysteine protease CLCP, which possesses two glycosylation sites. Mutation of any of the sites redirected CLCP to the secretory pathway. Similarly, the introduction of glycosylation sites to secreted β-amylase redirected this protein to lysosomes. Thus, unlike other parasitic protists, T. vaginalis seems to utilize glycosylation as a recognition marker for lysosomal hydrolases. Our findings provide the first insight into the complexity of T. vaginalis phagolysosomes, their biogenesis, and role in the unconventional secretion of cysteine peptidases.

show abstract

Biodegradable Polymeric Nanoparticles for Brain-Targeted Drug Delivery

Kempe

Nicolazzo

2020

Neuromethods

View full text Add to dashboard Cite

N-acetyl-β-d-hexosaminidase from Trichomonas vaginalis: substrate specificity and activity of inhibitors

Cited by 8 publications

References 10 publications

Identification of a novel β-N-acetylhexosaminidase (Pcb-NAHA1) from marine Zoanthid Palythoa caribaeorum (Cnidaria, Anthozoa, Zoanthidea)

Identification of a novel β-N-acetylhexosaminidase (Pcb-NAHA1) from marine Zoanthid Palythoa caribaeorum (Cnidaria, Anthozoa, Zoanthidea)

Proteomic Analysis of Trichomonas vaginalis Phagolysosome, Lysosomal Targeting, and Unconventional Secretion of Cysteine Peptidases

Biodegradable Polymeric Nanoparticles for Brain-Targeted Drug Delivery

Contact Info

Product

Resources

About