A common binding motif for various bacteria of the bacteria-binding peptide SRCRP2 of DMBT1/gp-340/salivary agglutinin |
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Authors: | Leito Jelani T D Ligtenberg Antoon J M Nazmi Kamran de Blieck-Hogervorst Jolanda M A Veerman Enno C I Nieuw Amerongen Arie V |
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Institution: | Department of Oral Biochemistry, Academic Centre for Dentistry Amsterdam (ACTA), Vrije Universiteit and Universiteit van Amsterdam, Van der Boechorstsraat 7, NL-1081 BT Amsterdam, The Netherlands. j.leito@vumc.nl |
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Abstract: | Abstract Salivary agglutinin (DMBT1SAG) is identical to lung glycoprotein-340 and encoded by deleted in malignant brain tumors-1. It is a member of the scavenger receptor cysteine-rich (SRCR) superfamily, proteins that have one or more SRCR domains. Salivary agglutinin plays a role in oral innate immunity by the binding and agglutination of oral streptococci. S. mutans has been shown to bind to a 16-mer peptide (QGRVEVLYRGSWGTVC) located within the SRCR domains. Within this peptide, designated SRCR Peptide 2, residues VEVL and W were critical for binding. The aim of this study was to investigate binding of DMBT1SAG to other bacteria. Therefore, interaction between a series of bacteria and DMBT1(SAG), SRCR peptide 2 and its alanine substitution variants was studied in adhesion and agglutination assays. For different bacteria there was a highly significant correlation between adhesion to DMBT1SAG and adhesion to SRCR peptide 2 suggesting that SRCR peptide 2 is the major bacteria binding site. An alanine substitution scan showed that 8 amino acids were involved in binding (xRVEVLYxxSWxxxx). The binding motifs varied for different species were found, but the residues VxVxY and W were always present. In conclusion, a common binding motif (RVEVLYxxxSW) within the SRCR domains is responsible for the broad bacteria-binding spectrum of DMBT1SAG. |
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