ArticleJournal of animal science2014
F4-related mutation and expression analysis of the aminopeptidase N gene in pigs.
Article in Journal of animal science, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
8 citing papers in PubMed, 8 citations in OpenAlex.
- Heat-labile enterotoxin enhances F4-producing enterotoxigenic E. coli adhesion to porcine intestinal epithelial cells by upregulating bacterial adhesins and STb enterotoxin.Veterinary research · 2022Article
- Swine enteric colibacillosis: Current treatment avenues and future directions.Frontiers in veterinary science · 2022Review
- Resistance to ETEC F4/F18-mediated piglet diarrhoea: opening the gene black box.Tropical animal health and production · 2019Review
- Binding determinants in the interplay between porcine aminopeptidase N and enterotoxigenic Escherichia coli F4 fimbriae.Veterinary research · 2018Article
- Animal Enterotoxigenic Escherichia coli.EcoSal Plus · 2016Review
- Proteome analysis for the global proteins in the jejunum tissues of enterotoxigenic Escherichia coli -infected piglets.Scientific reports · 2016Article
- Porcine aminopeptidase N binds to F4+ enterotoxigenic Escherichia coli fimbriae.Veterinary research · 2016Article
- Article
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Intestinal infections with F4 enterotoxigenic Escherichia coli (ETEC) are worldwide an important cause of diarrhea in neonatal and recently weaned pigs. Adherence of F4 ETEC to the small intestine by binding to specific receptors is mediated by F4 fimbriae. Porcine aminopeptidase N (ANPEP) was recently identified as a new F4 receptor. In this study, 7 coding mutations and 1 mutation in the 3' untranslated region (3' UTR)were identified in ANPEP by reverse transcriptase (RT-) PCR and sequencing using 3 F4 receptor-positive (F4R+) and 2 F4 receptor-negative (F4R-) pigs, which were F4 phenotyped based on the MUC4 TaqMan, oral immunization, and the in vitro villous adhesion assay. Three potential differential mutations (g.2615C > T, g.8214A > G, and g.16875C > G) identified by comparative analysis between the 3 F4R+ and 2 F4R- pigs were genotyped in 41 additional F4 phenotyped pigs. However, none of these 3 mutations could be associated with F4 ETEC susceptibility. In addition, the RT-PCR experiments did not reveal any differential expression or alternative splicing in the small intestine of F4R+ and F4R- pigs. In conclusion, we hypothesize that the difference in F4 binding to ANPEP is due to modifications in its carbohydrate moieties.
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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.