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

doi:10.1007/s00251-017-0982-x

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 Journal › Article › Academic › peer-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 language	English
Pages (from-to)	401-407
Journal	Immunogenetics
Volume	69
Issue number	6
DOIs	https://doi.org/10.1007/s00251-017-0982-x
Publication status	Published - Jun 2017

Funding

This work was supported by the European Molecular Biology Organization (EMBO), grant ASTF 115-02, the Netherlands Organization for Scientific Research (NWO), grant ER 90-184, the Deutsche Krebshilfe, grant no. 1835-Mo I, and the Wilhelm Sander-Stiftung, grant no. 99.018.2.

Funders	Funder number
European Molecular Biology Organization	ASTF 115-02
Wilhelm Sander-Stiftung	99.018.2
Nederlandse Organisatie voor Wetenschappelijk Onderzoek	ER 90-184
Deutsche Krebshilfe	1835-Mo I

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https://hdl.handle.net/11245.1/eb0e2e62-65d8-4864-8f32-fce8e13c677a

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title = "The scavenging capacity of DMBT1 is impaired by germline deletions",

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.",

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

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AU - Bikker, F.J.

AU - End, C.

AU - Ligtenberg, A.J.M.

AU - Blaich, S.

AU - Lyer, S.

AU - Renner, M.

AU - Wittig, R.

AU - Nazmi, K.

AU - van Nieuw Amerongen, A.

AU - Poustka, A.

AU - Veerman, E.C.I.

AU - Mollenhauer, J.

PY - 2017/6

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AB - 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.

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The scavenging capacity of DMBT1 is impaired by germline deletions

Abstract

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