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TitleNeutralizing Antibodies against Lassa Virus Lineage I.
Journal, issue, pagesmBio, Vol. 13, Issue 4, Page e0127822, Year 2022
Publish dateAug 30, 2022
AuthorsTierra K Buck / Adrian S Enriquez / Sharon L Schendel / Michelle A Zandonatti / Stephanie S Harkins / Haoyang Li / Alex Moon-Walker / James E Robinson / Luis M Branco / Robert F Garry / Erica Ollmann Saphire / Kathryn M Hastie /
PubMed AbstractLassa virus (LASV) is the causative agent of the deadly Lassa fever (LF). Seven distinct LASV lineages circulate through western Africa, among which lineage I (LI), the first to be identified, is ...Lassa virus (LASV) is the causative agent of the deadly Lassa fever (LF). Seven distinct LASV lineages circulate through western Africa, among which lineage I (LI), the first to be identified, is particularly resistant to antibody neutralization. Lineage I LASV evades neutralization by half of known antibodies in the GPC-A antibody competition group and all but one of the antibodies in the GPC-B competition group. Here, we solve two cryo-electron microscopy (cryo-EM) structures of LI GP in complex with a GPC-A and a GPC-B antibody. We used complementary structural and biochemical techniques to identify single-amino-acid substitutions in LI that are responsible for immune evasion by each antibody group. Further, we show that LI infection is more dependent on the endosomal receptor lysosome-associated membrane protein 1 (LAMP1) for viral entry relative to LIV. In the absence of LAMP1, LI requires a more acidic fusion pH to initiate membrane fusion with the host cell relative to LIV. No vaccine or therapeutics are approved to prevent LASV infection or treat LF. All vaccine platforms currently under development present only the LIV GP sequence. However, our data suggest that the high genetic diversity of LASV may be problematic for designing both a broadly reactive immunogen and therapeutic. Here, we examine antibodies that are highly potent against LIV yet are ineffective against LI. By pinpointing LI mutations responsible for this decrease in antibody efficacy, we suggest that future vaccine platforms may need to incorporate specific LI-like mutations in order to generate a broadly neutralizing antibody response against all LASV lineages.
External linksmBio / PubMed:35730904 / PubMed Central
MethodsEM (single particle)
Resolution3.1 - 3.59 Å
Structure data

26458

7uds

EMDB-26458, PDB-7uds:
Structure of lineage I (Pinneo) Lassa virus glycoprotein bound to Fab 25.10C
Method: EM (single particle) / Resolution: 3.1 Å

26594

7ul7

EMDB-26594, PDB-7ul7:
Lineage I (Pinneo) Lassa virus glycoprotein bound to 18.5C-M30 Fab
Method: EM (single particle) / Resolution: 3.59 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

Source
  • homo sapiens (human)
  • lassa mammarenavirus
KeywordsVIRAL PROTEIN/IMMUNE SYSTEM / viral glycoprotein / antibody Fab fragment / VIRAL PROTEIN / VIRAL PROTEIN-IMMUNE SYSTEM complex / glycoprotein / antibody / lassa virus

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