Limits...
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.

Show MeSH

Related in: MedlinePlus

Correlation between bacteria binding to DMBT1SAG and SRCRP2 [67].
© Copyright Policy - open-access
Related In: Results  -  Collection

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

f2-ijms-11-05212: Correlation between bacteria binding to DMBT1SAG and SRCRP2 [67].

Mentions: For DMBT1 SAG, the SRCR domains are identified as bacteria-binding sites. Proteolytic cleavage of DMBT1SAG with Lys-C results in a protein fragment of 1722 amino acids, only containing SRCR domains and SIDs, which still binds to S. mutans [65]. The SRCR domains in this protein fragment show a high degree of homology, which justifies the design of a consensus sequence. Based on this consensus sequence, synthetic peptides were designed consisting of the fragments between the cysteine residues covering the full SRCR domain and SID fragments. Bacterial binding was restricted to a 16-mer peptide (QGRVEVLYRGSWGTVC) representing the second fragment in the SRCR domain and therefore named SRCRP2 [65]. This peptide binds S. mutans and a number of other bacterial species including Streptococcus gordonii, Staphylococcus aureus, Escherichia coli and H. pylori [66]. Bacterial adhesion to the peptide correlates with adhesion to the full molecule (Figure 2) [67].


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)

Correlation between bacteria binding to DMBT1SAG and SRCRP2 [67].
© Copyright Policy - open-access
Related In: Results  -  Collection

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

f2-ijms-11-05212: Correlation between bacteria binding to DMBT1SAG and SRCRP2 [67].
Mentions: For DMBT1 SAG, the SRCR domains are identified as bacteria-binding sites. Proteolytic cleavage of DMBT1SAG with Lys-C results in a protein fragment of 1722 amino acids, only containing SRCR domains and SIDs, which still binds to S. mutans [65]. The SRCR domains in this protein fragment show a high degree of homology, which justifies the design of a consensus sequence. Based on this consensus sequence, synthetic peptides were designed consisting of the fragments between the cysteine residues covering the full SRCR domain and SID fragments. Bacterial binding was restricted to a 16-mer peptide (QGRVEVLYRGSWGTVC) representing the second fragment in the SRCR domain and therefore named SRCRP2 [65]. This peptide binds S. mutans and a number of other bacterial species including Streptococcus gordonii, Staphylococcus aureus, Escherichia coli and H. pylori [66]. Bacterial adhesion to the peptide correlates with adhesion to the full molecule (Figure 2) [67].

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