Functional Characterization of a Lassa Virus Fusion Inhibitor Adaptive Mutant

Lassa virus (LASV) glycoprotein complex (GPC) contains retained stable-signal peptide (SSP), glycoprotein 1 (GP1), and glycoprotein 2 (GP2). Through serial passaging of LASV with inhibitors, adaptive mutants were obtained, most of which had mutations in the transmembrane (TM) domain of GP2. Characte...

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Main Authors: Jiao Guo, Yalan Du, Guangshun Zhang, Yang Liu, Junyuan Cao, Mengmeng Zhang, Xiaohao Lan, Yueli Zhang, Chenchen Liu, Gengfu Xiao, Wei Wang
Format: Article
Language:English
Published: Compuscript Ltd 2025-01-01
Series:Zoonoses
Online Access:https://www.scienceopen.com/hosted-document?doi=10.15212/ZOONOSES-2024-0051
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author Jiao Guo
Yalan Du
Guangshun Zhang
Yang Liu
Junyuan Cao
Mengmeng Zhang
Xiaohao Lan
Yueli Zhang
Chenchen Liu
Gengfu Xiao
Wei Wang
author_facet Jiao Guo
Yalan Du
Guangshun Zhang
Yang Liu
Junyuan Cao
Mengmeng Zhang
Xiaohao Lan
Yueli Zhang
Chenchen Liu
Gengfu Xiao
Wei Wang
author_sort Jiao Guo
collection DOAJ
description Lassa virus (LASV) glycoprotein complex (GPC) contains retained stable-signal peptide (SSP), glycoprotein 1 (GP1), and glycoprotein 2 (GP2). Through serial passaging of LASV with inhibitors, adaptive mutants were obtained, most of which had mutations in the transmembrane (TM) domain of GP2. Characterizing the fusion inhibitor target within the TM domain of GP2 provided insights for the development of drugs and vaccines. We conducted membrane fusion, IIH6 inhibition, thermostability, and viral growth kinetics assays to characterize the effects of the F446L mutation on GPC-mediated membrane fusion, receptor binding, thermostability, growth kinetics, and fitness. F446L conferred cross-resistance to structurally distinct inhibitors. Additionally, F446L increased the fusion activity of LASV and Mopeia virus (MOPV) GPC, thus elevating the pH threshold for LASV fusion and promoting MOPV fusion at neutral pH. However, F446L exerted little effect on the pseudotype viral growth profile or thermostability. Introduction of other residues at the conserved F446 locus indicated that this site showed low compatibility with similar retained aromatic cyclic tyrosine residues and did not tolerate charged residues. We characterized the effects of the F446L mutation on LASV, thus providing useful information for the development of vaccines and drugs.
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institution Kabale University
issn 2737-7466
2737-7474
language English
publishDate 2025-01-01
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record_format Article
series Zoonoses
spelling doaj-art-c59f6f8f28e84166ae123ffad3d778f02025-08-20T03:28:21ZengCompuscript LtdZoonoses2737-74662737-74742025-01-015199310.15212/ZOONOSES-2024-0051Functional Characterization of a Lassa Virus Fusion Inhibitor Adaptive MutantJiao GuoYalan DuGuangshun ZhangYang LiuJunyuan CaoMengmeng ZhangXiaohao LanYueli ZhangChenchen LiuGengfu XiaoWei WangLassa virus (LASV) glycoprotein complex (GPC) contains retained stable-signal peptide (SSP), glycoprotein 1 (GP1), and glycoprotein 2 (GP2). Through serial passaging of LASV with inhibitors, adaptive mutants were obtained, most of which had mutations in the transmembrane (TM) domain of GP2. Characterizing the fusion inhibitor target within the TM domain of GP2 provided insights for the development of drugs and vaccines. We conducted membrane fusion, IIH6 inhibition, thermostability, and viral growth kinetics assays to characterize the effects of the F446L mutation on GPC-mediated membrane fusion, receptor binding, thermostability, growth kinetics, and fitness. F446L conferred cross-resistance to structurally distinct inhibitors. Additionally, F446L increased the fusion activity of LASV and Mopeia virus (MOPV) GPC, thus elevating the pH threshold for LASV fusion and promoting MOPV fusion at neutral pH. However, F446L exerted little effect on the pseudotype viral growth profile or thermostability. Introduction of other residues at the conserved F446 locus indicated that this site showed low compatibility with similar retained aromatic cyclic tyrosine residues and did not tolerate charged residues. We characterized the effects of the F446L mutation on LASV, thus providing useful information for the development of vaccines and drugs.https://www.scienceopen.com/hosted-document?doi=10.15212/ZOONOSES-2024-0051
spellingShingle Jiao Guo
Yalan Du
Guangshun Zhang
Yang Liu
Junyuan Cao
Mengmeng Zhang
Xiaohao Lan
Yueli Zhang
Chenchen Liu
Gengfu Xiao
Wei Wang
Functional Characterization of a Lassa Virus Fusion Inhibitor Adaptive Mutant
Zoonoses
title Functional Characterization of a Lassa Virus Fusion Inhibitor Adaptive Mutant
title_full Functional Characterization of a Lassa Virus Fusion Inhibitor Adaptive Mutant
title_fullStr Functional Characterization of a Lassa Virus Fusion Inhibitor Adaptive Mutant
title_full_unstemmed Functional Characterization of a Lassa Virus Fusion Inhibitor Adaptive Mutant
title_short Functional Characterization of a Lassa Virus Fusion Inhibitor Adaptive Mutant
title_sort functional characterization of a lassa virus fusion inhibitor adaptive mutant
url https://www.scienceopen.com/hosted-document?doi=10.15212/ZOONOSES-2024-0051
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