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. 2017 Mar 31;69(6):401–407. doi: 10.1007/s00251-017-0982-x

Fig. 2.

Fig. 2

Bacterial binding is dependent on DMBT1 polymorphism. a Domain structure of the DMBT1-variant expressed from the large DMBT1 allele (DMBT1/8 kb, 13 SRCR domains within the SRCR/SID region) and the small DMBT1 allele (DMBT1/6 kb, 8 SRCR domains within the SRCR/SID region). Pink triangle leader peptide, blue box sequence contains unique epitope for mAb DMBT1H12, red ovals SRCR domains, orange ovals, SRCR interspersed domains (SIDs), purple boxes C1r/C1s-Uegf-Bmp1 domains, green oval zona pellucida domain, EHD Ebnerin-Homologous Domain. b Bacterial binding to DMBT1/8 kb and DMBT1/6 kb (A) was semi-quantified using S. mutans (S.m), S. gordonii (S.g.), E. coli (E.c.), and H. pylori (H.p.). Relative to the wild type DMBT1SAG/8 kb we found, on a molecular base, a decrease in bacterial binding to DMBT1SAG/6 kb for all bacteria tested. Error bars represent the standard error of the mean (SEM), P ≤ 0.05