Immunobiotic Lactobacillus strains augment NLRP3 expression in newborn and adult porcine gut-associated lymphoid tissues

Masanori Tohno, Takeshi Shimosato, Hisashi Aso, Haruki Kitazawa

Research output: Contribution to journalArticlepeer-review

26 Citations (Scopus)


We isolated cDNA encoding porcine nucleotide-binding domain-like receptor family, pryin domain containing 3 (NLRP3) from Peyer's patches. The complete nucleotide open reading frame of porcine NLRP3 contains 3108-bp encoding a deduced polypeptide of 1036-amino acid residues. The porcine NLRP3 amino acid sequence is more similar to the longest isoform of human than the mouse counterpart. The predicted amino acid sequence of porcine NLRP3 presented nine C-terminal leucine-rich repeat domains. In newborn swine, the expression of NLRP3 was detected at higher levels in spleen and mesenteric lymph nodes, while lower levels were observed in intestinal tissues. In adult swine, NLRP3 was strongly expressed in Peyer's patches and the mesenteric lymph nodes, and the expression level in the lower intestinal tissues was comparable to that in spleen. Toll-like receptor and nucleotide-binding domain ligands, as well as Lactobacillus delbrueckii subsp. bulgaricus and Lactobacillus gasseri, enhanced NLRP3 expression in gut-associated lymphoid tissues (GALT) of newborn and adult swine. Our results should aid in understanding the intestinal immunoregulatory mechanisms underlying NLRP3 activation and the priming ability of immunobiotic lactic acid bacteria in porcine GALT.

Original languageEnglish
Pages (from-to)410-416
Number of pages7
JournalVeterinary Immunology and Immunopathology
Issue number3-4
Publication statusPublished - 2011 Dec 15


  • Gut-associated lymphoid tissues
  • Immunobiotics
  • Nucleotide-binding oligomerization domain (NOD)
  • Nucleotide-binding oligomerization domain-like receptor family
  • Porcine
  • Pryin domain containing 3 (NLRP3)
  • Toll-like receptor (TLR)


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