Characterization of Lassa virus glycoprotein oligomerization and influence of cholesterol on virus replication.

Journal of Virology
Katrin SchlieThomas Strecker

Abstract

Mature glycoprotein spikes are inserted in the Lassa virus envelope and consist of the distal subunit GP-1, the transmembrane-spanning subunit GP-2, and the signal peptide, which originate from the precursor glycoprotein pre-GP-C by proteolytic processing. In this study, we analyzed the oligomeric structure of the viral surface glycoprotein. Chemical cross-linking studies of mature glycoprotein spikes from purified virus revealed the formation of trimers. Interestingly, sucrose density gradient analysis of cellularly expressed glycoprotein showed that in contrast to trimeric mature glycoprotein complexes, the noncleaved glycoprotein forms monomers and oligomers spanning a wide size range, indicating that maturation cleavage of GP by the cellular subtilase SKI-1/S1P is critical for formation of the correct oligomeric state. To shed light on a potential relation between cholesterol and GP trimer stability, we performed cholesterol depletion experiments. Although depletion of cholesterol had no effect on trimerization of the glycoprotein spike complex, our studies revealed that the cholesterol content of the viral envelope is important for the infectivity of Lassa virus. Analyses of the distribution of viral proteins in cholestero...Continue Reading

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Citations

Dec 4, 2012·Viruses·Shuzo Urata, Jiro Yasuda
Dec 4, 2012·Viruses·Dominique J BurriAntonella Pasquato
Dec 4, 2012·Viruses·Sarah Katharina FehlingThomas Strecker
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Mar 29, 2019·Frontiers in Immunology·Morgan E Brisse, Hinh Ly
Dec 1, 2020·Frontiers in Immunology·Danushka K WijesundaraKeith J Chappell

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