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Deleted in malignant brain tumors-1 protein (DMBT1): a pattern recognition receptor with multiple binding sites.

Ligtenberg AJ, Karlsson NG, Veerman EC - Int J Mol Sci (2010)

Bottom Line: Adjacent to each individual SRCR domain are glycosylation domains, where the attached carbohydrate chains play a role in the binding of influenza A virus and Helicobacter pylori.The composition of the carbohydrate chains is not only donor specific, but also varies between different organs.These data demonstrate a role for DMBT1s as pattern recognition molecules containing various peptide and carbohydrate binding motifs.

View Article: PubMed Central - PubMed

Affiliation: Periodontology and Oral Biochemistry, Academic Centre for Dentistry Amsterdam, G. Mahlerlaan 3004, 1081LA, Amsterdam, The Netherlands; E-Mail: e.veerman@acta.nl.

ABSTRACT
Deleted in Malignant Brain Tumors-1 protein (DMBT1), salivary agglutinin (DMBT1(SAG)), and lung glycoprotein-340 (DMBT1(GP340)) are three names for glycoproteins encoded by the same DMBT1 gene. All these proteins belong to the scavenger receptor cysteine-rich (SRCR) superfamily of proteins: a superfamily of secreted or membrane-bound proteins with SRCR domains that are highly conserved down to sponges, the most ancient metazoa. In addition to SRCR domains, all DMBT1s contain two CUB domains and one zona pellucida domain. The SRCR domains play a role in the function of DMBT1s, which is the binding of a broad range of pathogens including cariogenic streptococci, Helicobacter pylori and HIV. Mucosal defense proteins like IgA, surfactant proteins and lactoferrin also bind to DMBT1s through their SRCR domains. The binding motif on the SRCR domains comprises an 11-mer peptide in which a few amino acids are essential for binding (GRVEVLYRGSW). Adjacent to each individual SRCR domain are glycosylation domains, where the attached carbohydrate chains play a role in the binding of influenza A virus and Helicobacter pylori. The composition of the carbohydrate chains is not only donor specific, but also varies between different organs. These data demonstrate a role for DMBT1s as pattern recognition molecules containing various peptide and carbohydrate binding motifs.

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Related in: MedlinePlus

Schematic overview of the structural organization of antigen I/II polypeptides. All proteins contain a 38 residues leader peptide. 165 amino acid residues downstream of the leader peptide is the alanine-rich region containing 1–4 repeats of an 82 residues alanine-rich repeat. This is followed by a variable (V) region, followed by proline-rich P region containing 1–3 copies of a 39 residues repeat. The C-terminus shows ≥64% homology along the antigen I/II protein family. C-terminally is the cell wall anchoring sequence (CWA).
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f3-ijms-11-05212: Schematic overview of the structural organization of antigen I/II polypeptides. All proteins contain a 38 residues leader peptide. 165 amino acid residues downstream of the leader peptide is the alanine-rich region containing 1–4 repeats of an 82 residues alanine-rich repeat. This is followed by a variable (V) region, followed by proline-rich P region containing 1–3 copies of a 39 residues repeat. The C-terminus shows ≥64% homology along the antigen I/II protein family. C-terminally is the cell wall anchoring sequence (CWA).

Mentions: DMBT1SAG binds in a calcium-dependent manner to antigen I/II polypeptides, a group of surface receptors on S. mutans and related streptococci. Antigen I/II polypeptides have been characterized under different names in a variety of streptococci, S. mutans (antigen B, P1, Pac, SpaP, MSL-1), S. sobrinus (PAg, SpaA), S. gordonii (SspA, SspB), S. intermedius (Pas), S. pyogenes (aspA) and S. agalactiae (bspD) [82,83]. Antigen I/II polypeptides on oral streptococci have been studied extensively as candidates for vaccine development [84]. These polypeptides, between 826 and 1653 amino acids long, share a common primary sequence (Figure 3). All proteins start with a 38 amino acid (aa) leader sequence that is cleaved off during secretion. The A-region, containing one to four copies of an 82 aa residues alanine-rich sequence, is found 165 aa residues downstream of this leader. This is followed by a variable region (V-region) and then by a proline-rich P-region containing one to three copies of a 39 residue sequence block. The C-terminal region of about 615 amino acids shows 64% or more sequence homology between the I/II polypeptides.


Deleted in malignant brain tumors-1 protein (DMBT1): a pattern recognition receptor with multiple binding sites.

Ligtenberg AJ, Karlsson NG, Veerman EC - Int J Mol Sci (2010)

Schematic overview of the structural organization of antigen I/II polypeptides. All proteins contain a 38 residues leader peptide. 165 amino acid residues downstream of the leader peptide is the alanine-rich region containing 1–4 repeats of an 82 residues alanine-rich repeat. This is followed by a variable (V) region, followed by proline-rich P region containing 1–3 copies of a 39 residues repeat. The C-terminus shows ≥64% homology along the antigen I/II protein family. C-terminally is the cell wall anchoring sequence (CWA).
© Copyright Policy - open-access
Related In: Results  -  Collection

License 1 - License 2
Show All Figures
getmorefigures.php?uid=PMC3100851&req=5

f3-ijms-11-05212: Schematic overview of the structural organization of antigen I/II polypeptides. All proteins contain a 38 residues leader peptide. 165 amino acid residues downstream of the leader peptide is the alanine-rich region containing 1–4 repeats of an 82 residues alanine-rich repeat. This is followed by a variable (V) region, followed by proline-rich P region containing 1–3 copies of a 39 residues repeat. The C-terminus shows ≥64% homology along the antigen I/II protein family. C-terminally is the cell wall anchoring sequence (CWA).
Mentions: DMBT1SAG binds in a calcium-dependent manner to antigen I/II polypeptides, a group of surface receptors on S. mutans and related streptococci. Antigen I/II polypeptides have been characterized under different names in a variety of streptococci, S. mutans (antigen B, P1, Pac, SpaP, MSL-1), S. sobrinus (PAg, SpaA), S. gordonii (SspA, SspB), S. intermedius (Pas), S. pyogenes (aspA) and S. agalactiae (bspD) [82,83]. Antigen I/II polypeptides on oral streptococci have been studied extensively as candidates for vaccine development [84]. These polypeptides, between 826 and 1653 amino acids long, share a common primary sequence (Figure 3). All proteins start with a 38 amino acid (aa) leader sequence that is cleaved off during secretion. The A-region, containing one to four copies of an 82 aa residues alanine-rich sequence, is found 165 aa residues downstream of this leader. This is followed by a variable region (V-region) and then by a proline-rich P-region containing one to three copies of a 39 residue sequence block. The C-terminal region of about 615 amino acids shows 64% or more sequence homology between the I/II polypeptides.

Bottom Line: Adjacent to each individual SRCR domain are glycosylation domains, where the attached carbohydrate chains play a role in the binding of influenza A virus and Helicobacter pylori.The composition of the carbohydrate chains is not only donor specific, but also varies between different organs.These data demonstrate a role for DMBT1s as pattern recognition molecules containing various peptide and carbohydrate binding motifs.

View Article: PubMed Central - PubMed

Affiliation: Periodontology and Oral Biochemistry, Academic Centre for Dentistry Amsterdam, G. Mahlerlaan 3004, 1081LA, Amsterdam, The Netherlands; E-Mail: e.veerman@acta.nl.

ABSTRACT
Deleted in Malignant Brain Tumors-1 protein (DMBT1), salivary agglutinin (DMBT1(SAG)), and lung glycoprotein-340 (DMBT1(GP340)) are three names for glycoproteins encoded by the same DMBT1 gene. All these proteins belong to the scavenger receptor cysteine-rich (SRCR) superfamily of proteins: a superfamily of secreted or membrane-bound proteins with SRCR domains that are highly conserved down to sponges, the most ancient metazoa. In addition to SRCR domains, all DMBT1s contain two CUB domains and one zona pellucida domain. The SRCR domains play a role in the function of DMBT1s, which is the binding of a broad range of pathogens including cariogenic streptococci, Helicobacter pylori and HIV. Mucosal defense proteins like IgA, surfactant proteins and lactoferrin also bind to DMBT1s through their SRCR domains. The binding motif on the SRCR domains comprises an 11-mer peptide in which a few amino acids are essential for binding (GRVEVLYRGSW). Adjacent to each individual SRCR domain are glycosylation domains, where the attached carbohydrate chains play a role in the binding of influenza A virus and Helicobacter pylori. The composition of the carbohydrate chains is not only donor specific, but also varies between different organs. These data demonstrate a role for DMBT1s as pattern recognition molecules containing various peptide and carbohydrate binding motifs.

Show MeSH
Related in: MedlinePlus