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TitleCleavage-intermediate Lassa virus trimer elicits neutralizing responses, identifies neutralizing nanobodies, and reveals an apex-situated site-of-vulnerability.
Journal, issue, pagesNat Commun, Vol. 15, Issue 1, Page 285, Year 2024
Publish dateJan 4, 2024
AuthorsJason Gorman / Crystal Sao-Fong Cheung / Zhijian Duan / Li Ou / Maple Wang / Xuejun Chen / Cheng Cheng / Andrea Biju / Yaping Sun / Pengfei Wang / Yongping Yang / Baoshan Zhang / Jeffrey C Boyington / Tatsiana Bylund / Sam Charaf / Steven J Chen / Haijuan Du / Amy R Henry / Tracy Liu / Edward K Sarfo / Chaim A Schramm / Chen-Hsiang Shen / Tyler Stephens / I-Ting Teng / John-Paul Todd / Yaroslav Tsybovsky / Raffaello Verardi / Danyi Wang / Shuishu Wang / Zhantong Wang / Cheng-Yan Zheng / Tongqing Zhou / Daniel C Douek / John R Mascola / David D Ho / Mitchell Ho / Peter D Kwong /
PubMed AbstractLassa virus (LASV) infection is expanding outside its traditionally endemic areas in West Africa, posing a pandemic biothreat. LASV-neutralizing antibodies, moreover, have proven difficult to elicit. ...Lassa virus (LASV) infection is expanding outside its traditionally endemic areas in West Africa, posing a pandemic biothreat. LASV-neutralizing antibodies, moreover, have proven difficult to elicit. To gain insight into LASV neutralization, here we develop a prefusion-stabilized LASV glycoprotein trimer (GPC), pan it against phage libraries comprising single-domain antibodies (nanobodies) from shark and camel, and identify one, D5, which neutralizes LASV. Cryo-EM analyses reveal D5 to recognize a cleavage-dependent site-of-vulnerability at the trimer apex. The recognized site appears specific to GPC intermediates, with protomers lacking full cleavage between GP1 and GP2 subunits. Guinea pig immunizations with the prefusion-stabilized cleavage-intermediate LASV GPC, first as trimer and then as a nanoparticle, induce neutralizing responses, targeting multiple epitopes including that of D5; we identify a neutralizing antibody (GP23) from the immunized guinea pigs. Collectively, our findings define a prefusion-stabilized GPC trimer, reveal an apex-situated site-of-vulnerability, and demonstrate elicitation of LASV-neutralizing responses by a cleavage-intermediate LASV trimer.
External linksNat Commun / PubMed:38177144 / PubMed Central
MethodsEM (single particle)
Resolution4.7 - 6.58 Å
Structure data

EMDB-26740: Ligand-free Lassa GPC Trimer with C1 Symmetry
Method: EM (single particle) / Resolution: 6.58 Å

EMDB-26859: Ligand-free Lassa GPC Trimer with C3 Symmetry
Method: EM (single particle) / Resolution: 5.7 Å

41048

8t5c

EMDB-41048, PDB-8t5c:
Lassa GPC Trimer in complex with Fab 8.11G and nanobody D5
Method: EM (single particle) / Resolution: 4.7 Å

EMDB-41302: Lassa GPC trimer in complex with Fab GP23
Method: EM (single particle) / Resolution: 5.4 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine

Source
  • lassa virus josiah
  • camelus bactrianus (Bactrian camel)
  • homo sapiens (human)
  • Cavia porcellus (domestic guinea pig)
KeywordsVIRAL PROTEIN/IMMUNE SYSTEM / vaccine / GPC / GP1 / GP2 / VIRAL PROTEIN-IMMUNE SYSTEM complex

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