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

doi:10.1016/j.molimm.2006.12.021

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 journal › Article › peer-review

19 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 language	English
Pages (from-to)	2566-2577
Number of pages	12
Journal	Molecular Immunology
Volume	44
Issue number	10
DOIs	https://doi.org/10.1016/j.molimm.2006.12.021
Publication status	Published - 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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10.1016/j.molimm.2006.12.021

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@article{c4b0f7d099e64d6c80ebfcc80db1330e,

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

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.",

keywords = "Extracellular phosphopolysaccharide, Immunobiotics, Lactococcus lactis subsp. cremoris, MD-1, RP105, Swine, cDNA cloning",

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

note = "Funding Information: We sincerely thank Dr. T. Shimosato (Section of Retroviral Immunology, Center for Biologics Evaluation Research, US Food and Drug Administration, USA) for helpful discussions and Dr. H. Inadera (Department of Public Health, Toyama Medical and Pharmaceutical University, Japan) for the kind gifts of the pGLM-ENH-luci vector. This study was partly supported by a Grant-in-Aid for Scientific Research (B) (2) (Nos. 15380183, 18380158) from the Japan Society for the Promotion of Science to Dr. H. Kitazawa, and the Secure and Healthy Animal Production project from the Ministry of Agriculture, Forestry and Fisheries of Japan to Drs. H. Aso and H. Kitazawa. M. Tohno is supported by JSPS research fellow (Research Fellowships for Young Scientists Program, No. 18005121). ",

year = "2007",

month = apr,

doi = "10.1016/j.molimm.2006.12.021",

language = "English",

volume = "44",

pages = "2566--2577",

journal = "Immunochemistry",

issn = "0161-5890",

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number = "10",

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TY - JOUR

T1 - Molecular cloning of porcine RP105/MD-1 involved in recognition of extracellular phosphopolysaccharides from Lactococcus lactis ssp. cremoris

AU - Tohno, Masanori

AU - Shimazu, Tomoyuki

AU - Ueda, Wataru

AU - Anzawa, Daisuke

AU - Aso, Hisashi

AU - Nishimura, Junko

AU - Kawai, Yasushi

AU - Saito, Yasuo

AU - Saito, Tadao

AU - Kitazawa, Haruki

N1 - Funding Information: We sincerely thank Dr. T. Shimosato (Section of Retroviral Immunology, Center for Biologics Evaluation Research, US Food and Drug Administration, USA) for helpful discussions and Dr. H. Inadera (Department of Public Health, Toyama Medical and Pharmaceutical University, Japan) for the kind gifts of the pGLM-ENH-luci vector. This study was partly supported by a Grant-in-Aid for Scientific Research (B) (2) (Nos. 15380183, 18380158) from the Japan Society for the Promotion of Science to Dr. H. Kitazawa, and the Secure and Healthy Animal Production project from the Ministry of Agriculture, Forestry and Fisheries of Japan to Drs. H. Aso and H. Kitazawa. M. Tohno is supported by JSPS research fellow (Research Fellowships for Young Scientists Program, No. 18005121).

PY - 2007/4

Y1 - 2007/4

N2 - 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.

AB - 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.

KW - Extracellular phosphopolysaccharide

KW - Immunobiotics

KW - Lactococcus lactis subsp. cremoris

KW - MD-1

KW - RP105

KW - Swine

KW - cDNA cloning

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U2 - 10.1016/j.molimm.2006.12.021

DO - 10.1016/j.molimm.2006.12.021

M3 - Article

C2 - 17254634

AN - SCOPUS:33846920620

SN - 0161-5890

VL - 44

SP - 2566

EP - 2577

JO - Immunochemistry

JF - Immunochemistry

IS - 10

ER -

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

Abstract

Keywords

ASJC Scopus subject areas

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