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

Tiphanie Goetstouwers, Mario Van Poucke UGent, Ut Nguyen Van UGent, Vesna Melkebeek, Annelies Coddens UGent, Dieter Deforce UGent, Eric Cox UGent and Luc Peelman UGent (2014) JOURNAL OF ANIMAL SCIENCE. 92(5). p.1866-1873
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.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
keyword
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
journal title
JOURNAL OF ANIMAL SCIENCE
J. Anim. Sci.
volume
92
issue
5
pages
1866 - 1873
Web of Science type
Article
Web of Science id
000335830600006
ISSN
1525-3163
DOI
10.2527/jas2013-7307
language
English
UGent publication?
yes
classification
A1
copyright statement
I have transferred the copyright for this publication to the publisher
id
4430969
handle
http://hdl.handle.net/1854/LU-4430969
date created
2014-06-27 09:23:57
date last changed
2016-12-19 15:45:41
@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},
  keyword      = {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},
  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},
}

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.