The scavenging capacity of DMBT1 is impaired by germline deletions

F.J. Bikker, C. End, A.J.M. Ligtenberg, S. Blaich, S. Lyer, M. Renner, R. Wittig, K. Nazmi, A. van Nieuw Amerongen, A. Poustka, E.C.I. Veerman, J. Mollenhauer

Research output: Contribution to JournalArticleAcademicpeer-review

Abstract

The Scavenger Receptor Cysteine-Rich (SRCR) proteins are an archaic group of proteins characterized by the presence of multiple SRCR domains. They are membrane-bound or secreted proteins, which are generally related to host defense systems in animals. Deleted in Malignant Brain Tumors 1 (DMBT1) is a SRCR protein which is secreted in mucosal fluids and involved in host defense by pathogen binding by its SRCR domains. Genetic polymorphism within DMBT1 leads to DMBT1-alleles giving rise to polypeptides with interindividually different numbers of SRCR domains, ranging from 8 SRCR domains (encoded by 6 kb DMBT1 variant) to 13 SRCR domains (encoded by the 8 kb DMBT1 variant). In the present study, we have investigated whether reduction from 13 to 8 amino-terminal SRCR domains leads to reduction of bacterial binding. The 6 kb variant bound ~20–45% less bacteria compared to the 8 kb variant. These results support the hypothesis that genetic variation in DMBT1 may influence microbial defense.

Original languageEnglish
Pages (from-to)401-407
JournalImmunogenetics
Volume69
Issue number6
DOIs
Publication statusPublished - Jun 2017

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