This subproject is one of many research subprojects utilizing theresources provided by a Center grant funded by NIH/NCRR. The subproject andinvestigator (PI) may have received primary funding from another NIH source,and thus could be represented in other CRISP entries. The institution listed isfor the Center, which is not necessarily the institution for the investigator.Professor Mariuzza is interested in an extracellular matrix protein called mindin. Mindin was recently shown to be an LPS-binding protein as well as an integrin ligand. The X-ray structure of mindin was previously determined and its integrin binding site has been mapped by mutational analysis. There are two forms of mindin. The recombinant protein, which is bacterially produced, does not bind to LPS. By contrast, the mindin, which is produced in mammalian cells (HEK 293), has both integrin- and LPS-binding activities. SDS-PAGE showed that mammalian mindin is post-translationally modified compared to bacterial mindin. It is suspected that this modification is required for LPS binding. Mindin has no N-linked glycosylation sites, but potential sites for both O-linked glycosylation and C-mannosylation were present. Dr. Mariuzza was interested in knowing the nature and location of this modification.
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