ArticlePLoS neglected tropical diseases2015
Peptidases compartmentalized to the Ascaris suum intestinal lumen and apical intestinal membrane.
Article in PLoS neglected tropical diseases, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 16 citations in OpenAlex.
- Getting around the roundworms: Identifying knowledge gaps and research priorities for the ascarids.Advances in parasitology · 2024Article
- Genome-Wide Analysis ofInternational journal of molecular sciences · 2023Article
- Diethylcarbamazine, TRP channels and CaScientific reports · 2022Article
- N-glycome and N-glycoproteome of a hematophagous parasitic nematodeComputational and structural biotechnology journal · 2021Article
- De novo identification of toxicants that cause irreparable damage to parasitic nematode intestinal cells.PLoS neglected tropical diseases · 2020Article
- Omics Driven Understanding of the Intestines of Parasitic Nematodes.Frontiers in genetics · 2019Review
- Cysteine proteases as digestive enzymes in parasitic helminths.PLoS neglected tropical diseases · 2018Review
- Compartmentalization of functions and predicted miRNA regulation among contiguous regions of the nematode intestine.RNA biology · 2017Article
- Direct experimental manipulation of intestinal cells in Ascaris suum, with minor influences on the global transcriptome.International journal for parasitology · 2017Article
- Pan-Nematoda Transcriptomic Elucidation of Essential Intestinal Functions and Therapeutic Targets With Broad Potential.EBioMedicine · 2015Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
The nematode intestine is a tissue of interest for developing new methods of therapy and control of parasitic nematodes. However, biological details of intestinal cell functions remain obscure, as do the proteins and molecular functions located on the apical intestinal membrane (AIM), and within the intestinal lumen (IL) of nematodes. Accordingly, methods were developed to gain a comprehensive identification of peptidases that function in the intestinal tract of adult female Ascaris suum. Peptidase activity was detected in multiple fractions of the A. suum intestine under pH conditions ranging from 5.0 to 8.0. Peptidase class inhibitors were used to characterize these activities. The fractions included whole lysates, membrane enriched fractions, and physiological- and 4 molar urea-perfusates of the intestinal lumen. Concanavalin A (ConA) was confirmed to bind to the AIM, and intestinal proteins affinity isolated on ConA-beads were compared to proteins from membrane and perfusate fractions by mass spectrometry. Twenty-nine predicted peptidases were identified including aspartic, cysteine, and serine peptidases, and an unexpectedly high number (16) of metallopeptidases. Many of these proteins co-localized to multiple fractions, providing independent support for localization to specific intestinal compartments, including the IL and AIM. This unique perfusion model produced the most comprehensive view of likely digestive peptidases that function in these intestinal compartments of A. suum, or any nematode. This model offers a means to directly determine functions of these proteins in the A. suum intestine and, more generally, deduce the wide array functions that exist in these cellular compartments of the nematode intestine.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.