Molecular cloning of porcine RP105/MD-1 involved in recognition of extracellular phosphopolysaccharides from Lactococcus lactis ssp. cremoris

Masanori Tohno, Tomoyuki Shimazu, Wataru Ueda, Daisuke Anzawa, Hisashi Aso, Junko Nishimura, Yasushi Kawai, Yasuo Saito, Tadao Saito, Haruki Kitazawa

Research output: Contribution to journalArticlepeer-review

16 Citations (Scopus)

Abstract

In this study, we cloned the cDNAs encoding porcine RP105 (poRP105) and porcine MD-1 (poMD-1) from Peyer's patches of adult swine. The complete open reading frames of poRP105 and poMD-1 contain 1986 and 480 bp and encode 661 and 159 amino acid residues, respectively. These two proteins were more similar to the human (77.6% and 76.5% amino acid identity) than the mouse counterparts (70.0% and 71.1% amino acid identity). The results of several experiments in cells cotransfected with poRP105 and poMD-1 indicated both lipopolysaccharide and extracellular phosphopolysaccharide from Lactococcus lactis subsp. cremoris (Lc. cremoris) strongly activate nuclear factor-κB and induce the expression of various cytokines via RP105. These effects were mediated by phosphatidylinositol 3-kinase and Bruton's tyrosine kinase. Thus, we identified extracellular polysaccharide from Lc. cremoris as an active substance that can induce immune activation via RP105 and MD-1.

Original languageEnglish
Pages (from-to)2566-2577
Number of pages12
JournalMolecular Immunology
Volume44
Issue number10
DOIs
Publication statusPublished - 2007 Apr

Keywords

  • Extracellular phosphopolysaccharide
  • Immunobiotics
  • Lactococcus lactis subsp. cremoris
  • MD-1
  • RP105
  • Swine
  • cDNA cloning

ASJC Scopus subject areas

  • Immunology
  • Molecular Biology

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