Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structural conservation of Lassa virus glycoproteins and recognition by neutralizing antibodies.
Journal, issue, pages	Cell Rep, Vol. 42, Issue 5, Page 112524, Year 2023
Publish date	May 30, 2023
Authors	Hailee R Perrett / Philip J M Brouwer / Jonathan Hurtado / Maddy L Newby / Lin Liu / Helena Müller-Kräuter / Sarah Müller Aguirre / Judith A Burger / Joey H Bouhuijs / Grace Gibson / Terrence Messmer / John S Schieffelin / Aleksandar Antanasijevic / Geert-Jan Boons / Thomas Strecker / Max Crispin / Rogier W Sanders / Bryan Briney / Andrew B Ward /
PubMed Abstract	Lassa fever is an acute hemorrhagic fever caused by the zoonotic Lassa virus (LASV). The LASV glycoprotein complex (GPC) mediates viral entry and is the sole target for neutralizing antibodies. ...Lassa fever is an acute hemorrhagic fever caused by the zoonotic Lassa virus (LASV). The LASV glycoprotein complex (GPC) mediates viral entry and is the sole target for neutralizing antibodies. Immunogen design is complicated by the metastable nature of recombinant GPCs and the antigenic differences among phylogenetically distinct LASV lineages. Despite the sequence diversity of the GPC, structures of most lineages are lacking. We present the development and characterization of prefusion-stabilized, trimeric GPCs of LASV lineages II, V, and VII, revealing structural conservation despite sequence diversity. High-resolution structures and biophysical characterization of the GPC in complex with GP1-A-specific antibodies suggest their neutralization mechanisms. Finally, we present the isolation and characterization of a trimer-preferring neutralizing antibody belonging to the GPC-B competition group with an epitope that spans adjacent protomers and includes the fusion peptide. Our work provides molecular detail information on LASV antigenic diversity and will guide efforts to design pan-LASV vaccines.
External links	Cell Rep / PubMed:37209096 / PubMed Central
Methods	EM (single particle)
Resolution	3.13 - 3.81 Å
Structure data	28178 8ejd EMDB-28178, PDB-8ejd: Structure of lineage IV Lassa virus glycoprotein complex (strain Josiah) Method: EM (single particle) / Resolution: 3.8 Å 28179 8eje EMDB-28179, PDB-8eje: Structure of lineage II Lassa virus glycoprotein complex (strain NIG08-A41) Method: EM (single particle) / Resolution: 3.69 Å 28180 8ejf EMDB-28180, PDB-8ejf: Structure of lineage V Lassa virus glycoprotein complex (strain Soromba-R) Method: EM (single particle) / Resolution: 3.72 Å 28181 8ejg EMDB-28181, PDB-8ejg: Structure of lineage VII Lassa virus glycoprotein complex (strain Togo/2016/7082) Method: EM (single particle) / Resolution: 3.13 Å 28182 8ejh EMDB-28182, PDB-8ejh: Lassa virus glycoprotein complex (Josiah) bound to 12.1F Fab Method: EM (single particle) / Resolution: 3.71 Å 28183 8eji EMDB-28183, PDB-8eji: Lassa virus glycoprotein complex (Josiah) bound to 19.7E Fab Method: EM (single particle) / Resolution: 3.81 Å 28184 8ejj EMDB-28184, PDB-8ejj: Lassa virus glycoprotein complex (Josiah) bound to S370.7 Fab Method: EM (single particle) / Resolution: 3.22 Å
Chemicals	ChemComp-NAG: 2-acetamido-2-deoxy-beta-D-glucopyranose ChemComp-MAN: alpha-D-mannopyranose
Source	lassa mammarenavirus homo sapiens (human)
Keywords	VIRAL PROTEIN / glycoprotein complex / Lassa mammarenavirus / LASV / GPC / immune system / viral fusion protein / Lassa virus / lineage IV / Josiah / lineage II / NIG08-A41 / lineage V / Soromba-R / lineage VI / Togo/2016/7082 / 12.1F / 19.7E / VIRAL PROTEIN/IMMUNE SYSTEM / S370.7 / VIRAL PROTEIN-IMMUNE SYSTEM complex