Pathogen Sensing by Nucleotide-binding Oligomerization Domain-containing Protein 2 (NOD2) Is Mediated by Direct Binding to Muramyl Dipeptide and ATP
Nucleotide binding and oligomerization domain-containing protein 2 (NOD2/Card15) is an intracellular protein that is involved in the recognition of bacterial cell wall-derived muramyl dipeptide. Mutations in the gene encoding NOD2 are associated with inherited inflammatory disorders, including Crohn...
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Published in | The Journal of biological chemistry Vol. 287; no. 27; pp. 23057 - 23067 |
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Main Authors | , , , , , |
Format | Journal Article |
Language | English |
Published |
United States
Elsevier Inc
29.06.2012
American Society for Biochemistry and Molecular Biology |
Subjects | |
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Abstract | Nucleotide binding and oligomerization domain-containing protein 2 (NOD2/Card15) is an intracellular protein that is involved in the recognition of bacterial cell wall-derived muramyl dipeptide. Mutations in the gene encoding NOD2 are associated with inherited inflammatory disorders, including Crohn disease and Blau syndrome. NOD2 is a member of the nucleotide-binding domain and leucine-rich repeat-containing protein gene (NLR) family. Nucleotide binding is thought to play a critical role in signaling by NLR family members. However, the molecular mechanisms underlying signal transduction by these proteins remain largely unknown. Mutations in the nucleotide-binding domain of NOD2 have been shown to alter its signal transduction properties in response to muramyl dipeptide in cellular assays. Using purified recombinant protein, we now demonstrate that NOD2 binds and hydrolyzes ATP. Additionally, we have found that the purified recombinant protein is able to bind directly to muramyl dipeptide and can associate with known NOD2-interacting proteins in vitro. Binding of NOD2 to muramyl dipeptide and homo-oligomerization of NOD2 are enhanced by ATP binding, suggesting a model of the molecular mechanism for signal transduction that involves binding of nucleotide followed by binding of muramyl dipeptide and oligomerization of NOD2 into a signaling complex. These findings set the stage for further studies into the molecular mechanisms that underlie detection of muramyl dipeptide and assembly of NOD2-containing signaling complexes.
Background: Nucleotide binding and oligomerization domain-containing protein 2 (NOD2) is a protein involved in the recognition of bacterial pathogens through detection of muramyl dipeptide.
Results: Purified recombinant NOD2 was found to bind ATP and muramyl dipeptide.
Conclusion: NOD2 is an intracellular signaling receptor for muramyl dipeptide.
Significance: These results help to define the molecular events involved in NOD2 signaling. |
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AbstractList | Background:
Nucleotide binding and oligomerization domain-containing protein 2 (NOD2) is a protein involved in the recognition of bacterial pathogens through detection of muramyl dipeptide.
Results:
Purified recombinant NOD2 was found to bind ATP and muramyl dipeptide.
Conclusion:
NOD2 is an intracellular signaling receptor for muramyl dipeptide.
Significance:
These results help to define the molecular events involved in NOD2 signaling.
Nucleotide binding and oligomerization domain-containing protein 2 (NOD2/Card15) is an intracellular protein that is involved in the recognition of bacterial cell wall-derived muramyl dipeptide. Mutations in the gene encoding NOD2 are associated with inherited inflammatory disorders, including Crohn disease and Blau syndrome. NOD2 is a member of the
n
ucleotide-binding domain and
l
eucine-rich
r
epeat-containing protein gene (NLR) family. Nucleotide binding is thought to play a critical role in signaling by NLR family members. However, the molecular mechanisms underlying signal transduction by these proteins remain largely unknown. Mutations in the nucleotide-binding domain of NOD2 have been shown to alter its signal transduction properties in response to muramyl dipeptide in cellular assays. Using purified recombinant protein, we now demonstrate that NOD2 binds and hydrolyzes ATP. Additionally, we have found that the purified recombinant protein is able to bind directly to muramyl dipeptide and can associate with known NOD2-interacting proteins
in vitro
. Binding of NOD2 to muramyl dipeptide and homo-oligomerization of NOD2 are enhanced by ATP binding, suggesting a model of the molecular mechanism for signal transduction that involves binding of nucleotide followed by binding of muramyl dipeptide and oligomerization of NOD2 into a signaling complex. These findings set the stage for further studies into the molecular mechanisms that underlie detection of muramyl dipeptide and assembly of NOD2-containing signaling complexes. Nucleotide binding and oligomerization domain-containing protein 2 (NOD2/Card15) is an intracellular protein that is involved in the recognition of bacterial cell wall-derived muramyl dipeptide. Mutations in the gene encoding NOD2 are associated with inherited inflammatory disorders, including Crohn disease and Blau syndrome. NOD2 is a member of the nucleotide-binding domain and leucine-rich repeat-containing protein gene (NLR) family. Nucleotide binding is thought to play a critical role in signaling by NLR family members. However, the molecular mechanisms underlying signal transduction by these proteins remain largely unknown. Mutations in the nucleotide-binding domain of NOD2 have been shown to alter its signal transduction properties in response to muramyl dipeptide in cellular assays. Using purified recombinant protein, we now demonstrate that NOD2 binds and hydrolyzes ATP. Additionally, we have found that the purified recombinant protein is able to bind directly to muramyl dipeptide and can associate with known NOD2-interacting proteins in vitro. Binding of NOD2 to muramyl dipeptide and homo-oligomerization of NOD2 are enhanced by ATP binding, suggesting a model of the molecular mechanism for signal transduction that involves binding of nucleotide followed by binding of muramyl dipeptide and oligomerization of NOD2 into a signaling complex. These findings set the stage for further studies into the molecular mechanisms that underlie detection of muramyl dipeptide and assembly of NOD2-containing signaling complexes.Nucleotide binding and oligomerization domain-containing protein 2 (NOD2/Card15) is an intracellular protein that is involved in the recognition of bacterial cell wall-derived muramyl dipeptide. Mutations in the gene encoding NOD2 are associated with inherited inflammatory disorders, including Crohn disease and Blau syndrome. NOD2 is a member of the nucleotide-binding domain and leucine-rich repeat-containing protein gene (NLR) family. Nucleotide binding is thought to play a critical role in signaling by NLR family members. However, the molecular mechanisms underlying signal transduction by these proteins remain largely unknown. Mutations in the nucleotide-binding domain of NOD2 have been shown to alter its signal transduction properties in response to muramyl dipeptide in cellular assays. Using purified recombinant protein, we now demonstrate that NOD2 binds and hydrolyzes ATP. Additionally, we have found that the purified recombinant protein is able to bind directly to muramyl dipeptide and can associate with known NOD2-interacting proteins in vitro. Binding of NOD2 to muramyl dipeptide and homo-oligomerization of NOD2 are enhanced by ATP binding, suggesting a model of the molecular mechanism for signal transduction that involves binding of nucleotide followed by binding of muramyl dipeptide and oligomerization of NOD2 into a signaling complex. These findings set the stage for further studies into the molecular mechanisms that underlie detection of muramyl dipeptide and assembly of NOD2-containing signaling complexes. Nucleotide binding and oligomerization domain-containing protein 2 (NOD2/Card15) is an intracellular protein that is involved in the recognition of bacterial cell wall-derived muramyl dipeptide. Mutations in the gene encoding NOD2 are associated with inherited inflammatory disorders, including Crohn disease and Blau syndrome. NOD2 is a member of the nucleotide-binding domain and leucine-rich repeat-containing protein gene (NLR) family. Nucleotide binding is thought to play a critical role in signaling by NLR family members. However, the molecular mechanisms underlying signal transduction by these proteins remain largely unknown. Mutations in the nucleotide-binding domain of NOD2 have been shown to alter its signal transduction properties in response to muramyl dipeptide in cellular assays. Using purified recombinant protein, we now demonstrate that NOD2 binds and hydrolyzes ATP. Additionally, we have found that the purified recombinant protein is able to bind directly to muramyl dipeptide and can associate with known NOD2-interacting proteins in vitro. Binding of NOD2 to muramyl dipeptide and homo-oligomerization of NOD2 are enhanced by ATP binding, suggesting a model of the molecular mechanism for signal transduction that involves binding of nucleotide followed by binding of muramyl dipeptide and oligomerization of NOD2 into a signaling complex. These findings set the stage for further studies into the molecular mechanisms that underlie detection of muramyl dipeptide and assembly of NOD2-containing signaling complexes. Nucleotide binding and oligomerization domain-containing protein 2 (NOD2/Card15) is an intracellular protein that is involved in the recognition of bacterial cell wall-derived muramyl dipeptide. Mutations in the gene encoding NOD2 are associated with inherited inflammatory disorders, including Crohn disease and Blau syndrome. NOD2 is a member of the nucleotide-binding domain and leucine-rich repeat-containing protein gene (NLR) family. Nucleotide binding is thought to play a critical role in signaling by NLR family members. However, the molecular mechanisms underlying signal transduction by these proteins remain largely unknown. Mutations in the nucleotide-binding domain of NOD2 have been shown to alter its signal transduction properties in response to muramyl dipeptide in cellular assays. Using purified recombinant protein, we now demonstrate that NOD2 binds and hydrolyzes ATP. Additionally, we have found that the purified recombinant protein is able to bind directly to muramyl dipeptide and can associate with known NOD2-interacting proteins in vitro. Binding of NOD2 to muramyl dipeptide and homo-oligomerization of NOD2 are enhanced by ATP binding, suggesting a model of the molecular mechanism for signal transduction that involves binding of nucleotide followed by binding of muramyl dipeptide and oligomerization of NOD2 into a signaling complex. These findings set the stage for further studies into the molecular mechanisms that underlie detection of muramyl dipeptide and assembly of NOD2-containing signaling complexes. Background: Nucleotide binding and oligomerization domain-containing protein 2 (NOD2) is a protein involved in the recognition of bacterial pathogens through detection of muramyl dipeptide. Results: Purified recombinant NOD2 was found to bind ATP and muramyl dipeptide. Conclusion: NOD2 is an intracellular signaling receptor for muramyl dipeptide. Significance: These results help to define the molecular events involved in NOD2 signaling. |
Author | Boyle, Joseph P. Howard, Christopher B. Monie, Tom P. Davis, Beckley K. Mo, Jinyao Duncan, Joseph A. |
Author_xml | – sequence: 1 givenname: Jinyao surname: Mo fullname: Mo, Jinyao organization: Department of Medicine, Division of Infectious Diseases, University of North Carolina, Chapel Hill, North Carolina 27599-7030 – sequence: 2 givenname: Joseph P. surname: Boyle fullname: Boyle, Joseph P. organization: Department of Biochemistry, University of Cambridge, Cambridge, United Kingdom – sequence: 3 givenname: Christopher B. surname: Howard fullname: Howard, Christopher B. organization: Department of Biochemistry, University of Cambridge, Cambridge, United Kingdom – sequence: 4 givenname: Tom P. surname: Monie fullname: Monie, Tom P. organization: Department of Biochemistry, University of Cambridge, Cambridge, United Kingdom – sequence: 5 givenname: Beckley K. surname: Davis fullname: Davis, Beckley K. email: Beckley.davis@fandm.edu organization: Lineberger Comprehensive Cancer Center, University of North Carolina, Chapel Hill, North Carolina 27599-7295 – sequence: 6 givenname: Joseph A. surname: Duncan fullname: Duncan, Joseph A. email: jaduncan@med.unc.edu organization: Department of Medicine, Division of Infectious Diseases, University of North Carolina, Chapel Hill, North Carolina 27599-7030 |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/22549783$$D View this record in MEDLINE/PubMed |
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DocumentTitleAlternate | NOD2 Is a Muramyl Dipeptide-binding ATPase |
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Keywords | Signal Transduction Nucleotide Binding and Oligomerization Domain-containing Protein 2 Innate Immunity Pathogen-associated Molecular Pattern (PAMP) Inflammation Nod-like Receptors (NLR) Cellular Immune Response Adenosine Triphosphate ATP Muramyl Dipeptide |
Language | English |
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Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 Present address: Dept. of Biology, Franklin and Marshall College, Lancaster, PA 17604. |
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SubjectTerms | Acetylmuramyl-Alanyl-Isoglutamine - metabolism Adenosine Triphosphatases - metabolism Adenosine Triphosphate Adenosine Triphosphate - analogs & derivatives Adenosine Triphosphate - metabolism Animals ATP Bacterial Proteins - metabolism Baculoviridae - genetics Cells, Cultured Cellular Immune Response Chromatography, Affinity HEK293 Cells Humans Immunity, Innate - physiology Immunology Inflammation Innate Immunity Insecta - cytology Muramyl Dipeptide Nod-like Receptors (NLR) Nod2 Signaling Adaptor Protein - genetics Nod2 Signaling Adaptor Protein - immunology Nod2 Signaling Adaptor Protein - metabolism Nucleotide Binding and Oligomerization Domain-containing Protein 2 Pathogen-associated Molecular Pattern (PAMP) Protein Binding - physiology Receptor-Interacting Protein Serine-Threonine Kinase 2 - metabolism Recombinant Proteins - genetics Recombinant Proteins - immunology Recombinant Proteins - metabolism Signal Transduction Signal Transduction - immunology |
Title | Pathogen Sensing by Nucleotide-binding Oligomerization Domain-containing Protein 2 (NOD2) Is Mediated by Direct Binding to Muramyl Dipeptide and ATP |
URI | https://dx.doi.org/10.1074/jbc.M112.344283 https://www.ncbi.nlm.nih.gov/pubmed/22549783 https://www.proquest.com/docview/1023292217 https://pubmed.ncbi.nlm.nih.gov/PMC3391102 |
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