{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,22]],"date-time":"2026-10-22T12:34:05Z","timestamp":1792672445234,"version":"4.5.0"},"reference-count":49,"publisher":"Microbiology Society","issue":"9","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2005,9,1]]},"abstract":"<jats:p>Native rabies virus glycoprotein (RVGvir) is a trimeric, membrane-anchored protein that has been shown to interact with the p75<jats:sup>NTR<\/jats:sup>neurotrophin receptor. In order to determine if the RVG trimeric oligomerization state is required for its binding with p75<jats:sup>NTR<\/jats:sup>, different soluble recombinant molecules containing the entire RVG ectodomain (RVGect) were expressed alone or fused at its C terminus to the trimerization domain of the bacteriophage T4 fibritin, termed \u2018foldon\u2019. The oligomerization status of recombinant RVG was investigated using sedimentation in sucrose gradient and p75<jats:sup>NTR<\/jats:sup>binding assays. It was found that, in the absence of the fibritin foldon, recombinant RVGect forms unstable trimers that dissociate into monomers in a concentration-dependent manner. C-terminal fusion with the foldon induces stable RVG trimerization, which is concentration-independent. Furthermore, the fibritin foldon maintains the native antigenic structure of the carboxy part of RVGect. Cell binding experiments showed that RVG trimerization is required for efficient interaction with p75<jats:sup>NTR<\/jats:sup>. However, the exact mode of trimerization appears unimportant, as trimeric recombinant RVGect (fused to the fibritin foldon) and RVGvir both recognize p75<jats:sup>NTR<\/jats:sup>with similar nanomolar affinities, as shown by surface plasmon resonance experiments. Altogether, these results show that the C-terminal fusion of the RVG ectodomain with the fibritin foldon is a powerful way to obtain a recombinant trimeric native-like structure of the p75<jats:sup>NTR<\/jats:sup>binding domain of RVG.<\/jats:p>","DOI":"10.1099\/vir.0.81063-0","type":"journal-article","created":{"date-parts":[[2005,8,12]],"date-time":"2005-08-12T00:40:29Z","timestamp":1123807229000},"page":"2543-2552","source":"Crossref","is-referenced-by-count":61,"title":["Stable trimerization of recombinant rabies virus glycoprotein ectodomain is required for interaction with the p75NTR receptor"],"prefix":"10.1099","volume":"86","author":[{"given":"Ludmilla","family":"Sisso\u00ebff","sequence":"first","affiliation":[{"name":"Laboratoire de Virologie Mol\u00e9culaire et Structurale, UMR 2472 CNRS-INRA, 91198 Gif-sur-Yvette, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mohamed","family":"Mousli","sequence":"additional","affiliation":[{"name":"Laboratoire de Virologie Mol\u00e9culaire et Structurale, UMR 2472 CNRS-INRA, 91198 Gif-sur-Yvette, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Patrick","family":"England","sequence":"additional","affiliation":[{"name":"Plateforme de Biophysique des Macromol\u00e9cules et de leurs Interactions, Institut Pasteur, 75015 Paris, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christine","family":"Tuffereau","sequence":"additional","affiliation":[{"name":"Laboratoire de Virologie Mol\u00e9culaire et Structurale, UMR 2472 CNRS-INRA, 91198 Gif-sur-Yvette, France"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"345","reference":[{"key":"R1","doi-asserted-by":"crossref","first-page":"4594","DOI":"10.1074\/jbc.270.9.4594","article-title":"Zone mapping of the binding domain of the rat low affinity nerve growth factor receptor by the introduction of novel N -glycosylation sites","volume":"270","author":"Baldwin","year":"1995","journal-title":"J Biol Chem"},{"key":"R2","doi-asserted-by":"crossref","first-page":"4198","DOI":"10.1128\/JVI.65.8.4198-4203.1991","article-title":"Antigenicity of rabies virus glycoprotein","volume":"65","author":"Benmansour","year":"1991","journal-title":"J Virol"},{"key":"R3","doi-asserted-by":"crossref","first-page":"754","DOI":"10.1128\/IAI.16.3.754-759.1977","article-title":"Rabies virus glycoprotein. 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