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5VK2

Structural basis for antibody-mediated neutralization of Lassa virus

Summary for 5VK2
Entry DOI10.2210/pdb5vk2/pdb
DescriptorPre-glycoprotein polyprotein GP complex, Fab 37.7H heavy chain, Fab 37.7H light chain, ... (9 entities in total)
Functional Keywordslassa, glycoprotein, arenavirus, antibody, viral protein-immune system complex, viral protein/immune system
Biological sourceLassa virus (LASV)
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Total number of polymer chains12
Total formula weight299802.02
Authors
Hastie, K.M.,Zandonatti, M.A.,Kleinfelter, L.M.,Rowland, M.L.,Rowland, M.M.,Chandra, K.,Branco, L.M.,Robinson, J.E.,Garry, R.F.,Saphire, E.O. (deposition date: 2017-04-20, release date: 2017-05-31, Last modification date: 2024-10-23)
Primary citationHastie, K.M.,Zandonatti, M.A.,Kleinfelter, L.M.,Heinrich, M.L.,Rowland, M.M.,Chandran, K.,Branco, L.M.,Robinson, J.E.,Garry, R.F.,Saphire, E.O.
Structural basis for antibody-mediated neutralization of Lassa virus.
Science, 356:923-928, 2017
Cited by
PubMed Abstract: The arenavirus Lassa causes severe hemorrhagic fever and a significant disease burden in West Africa every year. The glycoprotein, GPC, is the sole antigen expressed on the viral surface and the critical target for antibody-mediated neutralization. Here we present the crystal structure of the trimeric, prefusion ectodomain of Lassa GP bound to a neutralizing antibody from a human survivor at 3.2-angstrom resolution. The antibody extensively anchors two monomers together at the base of the trimer, and biochemical analysis suggests that it neutralizes by inhibiting conformational changes required for entry. This work illuminates pH-driven conformational changes in both receptor-binding and fusion subunits of Lassa virus, illustrates the unique assembly of the arenavirus glycoprotein spike, and provides a much-needed template for vaccine design against these threats to global health.
PubMed: 28572385
DOI: 10.1126/science.aam7260
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.201 Å)
Structure validation

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