Advanced search
1 file | 980.45 KB

F4-related mutation and expression analysis of the aminopeptidase N gene in pigs

Tiphanie Goetstouwers (UGent) , Mario Van Poucke (UGent) , Ut Nguyen Van (UGent) , Vesna Melkebeek (UGent) , Annelies Coddens (UGent) , Dieter Deforce (UGent) , Eric Cox (UGent) and Luc Peelman (UGent)
(2014) JOURNAL OF ANIMAL SCIENCE. 92(5). p.1866-1873
Author
Organization
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.
Keywords
pig, F4 enterotoxigenic Escherichia coli, mutation, F4 phenotyping, F4 receptor, SUSCEPTIBILITY, PORCINE, CORONAVIRUSES, RECEPTOR, K88 ANTIGEN, F4 FIMBRIAE, PROTEIN SUBUNIT, BRUSH-BORDERS, NUCLEOTIDE-SEQUENCE, aminopeptidase N, ENTEROTOXIGENIC ESCHERICHIA-COLI

Downloads

  • (...).pdf
    • full text
    • |
    • UGent only
    • |
    • PDF
    • |
    • 980.45 KB

Citation

Please use this url to cite or link to this publication:

Chicago
Goetstouwers, Tiphanie, Mario Van Poucke, Ut Nguyen Van, Vesna Melkebeek, Annelies Coddens, Dieter Deforce, Eric Cox, and Luc Peelman. 2014. “F4-related Mutation and Expression Analysis of the Aminopeptidase N Gene in Pigs.” Journal of Animal Science 92 (5): 1866–1873.
APA
Goetstouwers, T., Van Poucke, M., Nguyen Van, U., Melkebeek, V., Coddens, A., Deforce, D., Cox, E., et al. (2014). F4-related mutation and expression analysis of the aminopeptidase N gene in pigs. JOURNAL OF ANIMAL SCIENCE, 92(5), 1866–1873.
Vancouver
1.
Goetstouwers T, Van Poucke M, Nguyen Van U, Melkebeek V, Coddens A, Deforce D, et al. F4-related mutation and expression analysis of the aminopeptidase N gene in pigs. JOURNAL OF ANIMAL SCIENCE. 2014;92(5):1866–73.
MLA
Goetstouwers, Tiphanie, Mario Van Poucke, Ut Nguyen Van, et al. “F4-related Mutation and Expression Analysis of the Aminopeptidase N Gene in Pigs.” JOURNAL OF ANIMAL SCIENCE 92.5 (2014): 1866–1873. Print.
@article{4430969,
  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{\textquotesingle} untranslated region (3{\textquoteright} 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 {\textrangle} T, g.8214A {\textrangle} G, and g.16875C {\textrangle} 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.},
  author       = {Goetstouwers, Tiphanie and Van Poucke, Mario and Nguyen Van, Ut and Melkebeek, Vesna and Coddens, Annelies and Deforce, Dieter and Cox, Eric and Peelman, Luc},
  issn         = {1525-3163},
  journal      = {JOURNAL OF ANIMAL SCIENCE},
  language     = {eng},
  number       = {5},
  pages        = {1866--1873},
  title        = {F4-related mutation and expression analysis of the aminopeptidase N gene in pigs},
  url          = {http://dx.doi.org/10.2527/jas2013-7307},
  volume       = {92},
  year         = {2014},
}

Altmetric
View in Altmetric
Web of Science
Times cited: