<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Martin GM</submitter><funding>U.S. Department of Health &amp;amp; Human Services | NIH | National Institute of Allergy and Infectious Diseases</funding><funding>NIAID NIH HHS</funding><funding>Medical Research Council</funding><funding>EC | Horizon 2020 Framework Programme</funding><funding>Bill and Melinda Gates Foundation</funding><pagination>101</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC10345191</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>8(1)</volume><pubmed_abstract>Chemical cross-linking is used to stabilize protein structures with additional benefits of pathogen and toxin inactivation for vaccine use, but its use has been restricted by the potential for local or global structural distortion. This is of particular importance when the protein in question requires a high degree of structural conservation for inducing a biological outcome such as the elicitation of antibodies to conformationally sensitive epitopes. The HIV-1 envelope glycoprotein (Env) trimer is metastable and shifts between different conformational states, complicating its use as a vaccine antigen. Here we have used the hetero-bifunctional zero-length reagent 1-Ethyl-3-(3-Dimethylaminopropyl)-Carbodiimide (EDC) to cross-link two soluble Env trimers, selected well-folded trimer species </pubmed_abstract><journal>NPJ vaccines</journal><pubmed_title>Profound structural conservation of chemically cross-linked HIV-1 envelope glycoprotein experimental vaccine antigens.</pubmed_title><pmcid>PMC10345191</pmcid><funding_grant_id>G0000635</funding_grant_id><funding_grant_id>UM1AI144462</funding_grant_id><funding_grant_id>UM1 AI144462</funding_grant_id><funding_grant_id>681137</funding_grant_id><funding_grant_id>OPP1115782</funding_grant_id><funding_grant_id>OPP1170236</funding_grant_id><funding_grant_id>UM1 AI100663</funding_grant_id><pubmed_authors>Sanders RW</pubmed_authors><pubmed_authors>Schiffner T</pubmed_authors><pubmed_authors>Shattock R</pubmed_authors><pubmed_authors>Aldon Y</pubmed_authors><pubmed_authors>Sattentau QJ</pubmed_authors><pubmed_authors>Fabian K</pubmed_authors><pubmed_authors>Harris S</pubmed_authors><pubmed_authors>Tolazzi M</pubmed_authors><pubmed_authors>Jovanoska L</pubmed_authors><pubmed_authors>McFarlane L</pubmed_authors><pubmed_authors>Katinger D</pubmed_authors><pubmed_authors>Russell RA</pubmed_authors><pubmed_authors>Cheeseman H</pubmed_authors><pubmed_authors>Martin GM</pubmed_authors><pubmed_authors>Schermer EE</pubmed_authors><pubmed_authors>Mundsperger P</pubmed_authors><pubmed_authors>Scarlatti G</pubmed_authors><pubmed_authors>Breemen M</pubmed_authors><pubmed_authors>Ward AB</pubmed_authors><pubmed_authors>Kunert R</pubmed_authors><pubmed_authors>Trajano LF</pubmed_authors><pubmed_authors>Sliepen K</pubmed_authors></additional><is_claimable>false</is_claimable><name>Profound structural conservation of chemically cross-linked HIV-1 envelope glycoprotein experimental vaccine antigens.</name><description>Chemical cross-linking is used to stabilize protein structures with additional benefits of pathogen and toxin inactivation for vaccine use, but its use has been restricted by the potential for local or global structural distortion. This is of particular importance when the protein in question requires a high degree of structural conservation for inducing a biological outcome such as the elicitation of antibodies to conformationally sensitive epitopes. The HIV-1 envelope glycoprotein (Env) trimer is metastable and shifts between different conformational states, complicating its use as a vaccine antigen. Here we have used the hetero-bifunctional zero-length reagent 1-Ethyl-3-(3-Dimethylaminopropyl)-Carbodiimide (EDC) to cross-link two soluble Env trimers, selected well-folded trimer species </description><dates><release>2023-01-01T00:00:00Z</release><publication>2023 Jul</publication><modification>2026-06-02T06:38:54.508Z</modification><creation>2025-07-12T03:04:47.255Z</creation></dates><accession>S-EPMC10345191</accession><cross_references><pubmed>37443366</pubmed><doi>10.1038/s41541-023-00696-w</doi></cross_references></HashMap>