This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. The innate immune system uses highly conserved receptors to recognize microbial pathogens. These receptors, called pattern-recognition receptors (PRRs), recognize pathogen-associated molecular patterns (PAMPs). PAMPs are conserved motifs in microbial pathogens such as lipopolysaccharide (LPS) and lipteichoic acid (LTA). Mindin is a member of the mindin-F-spondin family of secreted extracellular matrix (ECM) protein. The ECM not only serves as scaffolding to provide a structural framework for tissues but also regulates the behavior of the cells that contact it. Recent studies showed that Mindin agglutinates bacteria and directly binds to LPS and LTA and functions as an opsonin for macrophge phagocytosis of bacteria, which demonstrate that mindin is a pattern-recognition molecule that is essential in the initiation of the innate immune response. Determination of the crystal structure of mindin will advance our knowledge of innate immune recognition.
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