{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,7,30]],"date-time":"2025-07-30T12:02:07Z","timestamp":1753876927776,"version":"3.41.2"},"reference-count":57,"publisher":"Oxford University Press (OUP)","license":[{"start":{"date-parts":[[2022,10,5]],"date-time":"2022-10-05T00:00:00Z","timestamp":1664928000000},"content-version":"am","delay-in-days":2,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>Many proteins are anchored to the cell surface of eukaryotes using a unique family of glycolipids called glycosylphosphatidylinositol (GPI) anchors. These glycolipids also exist without a covalently bound protein, in particular on the cell surfaces of protozoan parasites where they are densely populated. GPIs and GPI-anchored proteins participate in multiple cellular processes such as signal transduction, cell adhesion, protein trafficking and pathogenesis of Malaria, Toxoplasmosis, Trypanosomiasis and prion diseases, among others. All GPIs share a common conserved glycan core modified in a cell-dependent manner with additional side glycans or phosphoethanolamine residues. Here, we use atomistic molecular dynamic simulations and perform a systematic study to evaluate the structural properties of GPIs with different side chains inserted in lipid bilayers. Our results show a flop-down orientation of GPIs with respect to the membrane surface and the presentation of the side chain residues to the solvent. This finding agrees well with experiments showing the role of the side residues as active epitopes for recognition of GPIs by macrophages and induction of GPI-glycan-specific immune responses. Protein-GPI interactions were investigated by attaching parasitic GPIs to Green Fluorescent Protein. GPIs are observed to recline on the membrane surface and pull down the attached protein close to the membrane facilitating mutual contacts between protein, GPI and the lipid bilayer. This model is efficient in evaluating the interaction of GPIs and GPI-anchored proteins with membranes and can be extended to study other parasitic GPIs and proteins and develop GPI-based immunoprophylaxis to treat infectious diseases.<\/jats:p>","DOI":"10.1093\/glycob\/cwac037","type":"journal-article","created":{"date-parts":[[2022,10,5]],"date-time":"2022-10-05T14:47:15Z","timestamp":1664981235000},"source":"Crossref","is-referenced-by-count":2,"title":["The importance of side branches of glycosylphosphatidylinositol anchors: a molecular dynamics perspective"],"prefix":"10.1093","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-1714-2780","authenticated-orcid":false,"given":"Pallavi","family":"Banerjee","sequence":"first","affiliation":[{"name":"Department of Theory and Biosystems, Max Planck Institute of Colloids and Interfaces , Potsdam 14476 , Germany"},{"name":"Mathematisch-Naturwissenschaftlichen Fakult\u00e4t, University of Potsdam , Potsdam 14476 , Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Daniel Varon","family":"Silva","sequence":"additional","affiliation":[{"name":"Department of Theory and Biosystems, Max Planck Institute of Colloids and Interfaces , Potsdam 14476 , Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Reinhard","family":"Lipowsky","sequence":"additional","affiliation":[{"name":"Department of Theory and Biosystems, Max Planck Institute of Colloids and Interfaces , Potsdam 14476 , Germany"},{"name":"Mathematisch-Naturwissenschaftlichen Fakult\u00e4t, University of Potsdam , Potsdam 14476 , Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Mark","family":"Santer","sequence":"additional","affiliation":[{"name":"Department of Theory and Biosystems, Max Planck Institute of Colloids and Interfaces , Potsdam 14476 , Germany"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"286","published-online":{"date-parts":[[2022,10,3]]},"reference":[{"key":"2022100513190812900_ref1","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1016\/j.softx.2015.06.001","article-title":"GROMACS: High performance molecular simulations through multi-level parallelism from laptops to supercomputers","volume":"1","author":"Abraham","year":"2015","journal-title":"SoftwareX"},{"issue":"11","key":"2022100513190812900_ref2","doi-asserted-by":"crossref","first-page":"1914","DOI":"10.1016\/j.biocel.2006.05.006","article-title":"Toxoplasma gondii grown in human cells uses GalNAc- containing glycosylphosphatidylinositol precursors to anchor surface antigens while the immunogenic Glc\u2013GalNAc-containing precursors remain free at the parasite cell surface","volume":"38","author":"Azzouz","year":"2006","journal-title":"Int J Biochem Cell 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