ArticleEukaryotic cell2009
Role of CpSUB1, a subtilisin-like protease, in Cryptosporidium parvum infection in vitro.
Article in Eukaryotic cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
19 citing papers in PubMed, 38 citations in OpenAlex.
- Variant surface protein GP60 contributes to host infectivity of Cryptosporidium parvum.Communications biology · 2024Article
- Specific Cryptosporidium antigens associate with reinfection immunity and protection from cryptosporidiosis.The Journal of clinical investigation · 2023Article
- Maturation of subtilisin-like protease NbSLP1 from microsporidiaFrontiers in cellular and infection microbiology · 2022Article
- Comparative Pathobiology of the Intestinal Protozoan ParasitesPathogens (Basel, Switzerland) · 2019Review
- Article
- Comparative genomic analyses reveal the features for adaptation to nematodes in fungi.DNA research : an international journal for rapid publication of reports on genes and genomes · 2018Article
- Subtype analysis of zoonotic pathogen Cryptosporidium skunk genotype.Infection, genetics and evolution : journal of molecular epidemiology and evolutionary genetics in infectious diseases · 2017Article
- The in vitro and ex vivo effect of Auranta 3001 in preventingGut pathogens · 2017Article
- Article
- Identification of invasion proteins of Cryptosporidium parvum.World journal of microbiology & biotechnology · 2015Article
- Subtyping novel zoonotic pathogen Cryptosporidium chipmunk genotype I.Journal of clinical microbiology · 2015Article
- Cryptosporidium pathogenicity and virulence.Clinical microbiology reviews · 2013Review
- Inhibitory potential of prodomain of Plasmodium falciparum protease serine repeat antigen 5 for asexual blood stages of parasite.PloS one · 2012Article
- Cryptosporidiosis-an overview.Journal of biomedical research · 2012Article
- The cell biology of cryptosporidium infection.Microbes and infection · 2011Review
- Global identification of multiple substrates for Plasmodium falciparum SUB1, an essential malarial processing protease.Infection and immunity · 2011Article
- An atypical proprotein convertase in Giardia lamblia differentiation.Molecular and biochemical parasitology · 2011Article
- Human immune responses in cryptosporidiosis.Future microbiology · 2010Review
- Differential Gene Expression and Protein Localization of Cryptosporidium parvum Fatty Acyl-CoA Synthetase Isoforms.The Journal of eukaryotic microbiologyArticle
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
The apicomplexan parasite Cryptosporidium is a significant cause of diarrheal disease worldwide. Previously, we reported that a Cryptosporidium parvum subtilisin-like serine protease activity with furin-type specificity cleaves gp40/15, a glycoprotein that is proteolytically processed into gp40 and gp15, which are implicated in mediating infection of host cells. Neither the enzyme(s) responsible for the protease activity in C. parvum lysates nor those that process gp40/15 are known. There are no furin or other proprotein convertase genes in the C. parvum genome. However, a gene encoding CpSUB1, a subtilisin-like serine protease, is present. In this study, we cloned the CpSUB1 genomic sequence and expressed and purified the recombinant prodomain. Reverse transcriptase PCR analysis of RNA from C. parvum-infected HCT-8 cells revealed that CpSUB1 is expressed throughout infection in vitro. In immunoblots, antiserum to the recombinant CpSUB1 prodomain revealed two major bands, of approximately 64 kDa and approximately 48 kDa, for C. parvum lysates and proteins "shed" during excystation. In immunofluorescence assays, the antiserum reacted with the apical region of sporozoites and merozoites. The recombinant prodomain inhibited protease activity and processing of recombinant gp40/15 by C. parvum lysates but not by furin. Since prodomains are often selective inhibitors of their cognate enzymes, these results suggest that CpSUB1 may be a likely candidate for the protease activity in C. parvum and for processing of gp40/15. Importantly, the recombinant prodomain inhibited C. parvum infection of HCT-8 cells. These studies indicate that CpSUB1 plays a significant role in infection of host cells by the parasite and suggest that this enzyme may serve as a target for intervention.
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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.