Please ensure Javascript is enabled for purposes of website accessibility
Home / Bacteria & Viruses related products / Lassa Virus (LASV)
Product Menu
Product Menu Close
Lassa Virus (LASV)


Lassa virus virion structureViruses vol. Jul. 2016

 

The virions of arenaviruses are spherical in appearance and between 40 and 200 nm in diameter. The surface has a spike structure formed by the envelope glycoprotein GPC (glycoprotein complex). The inner support of the virus envelope is the matrix protein Z (RING finger zinc-binding protein), the nucleocapsid protein NP (nucleocapsid protein)wraps two single-stranded RNA genes, and together with the RNA-dependent RNA polymerase L protein (RNA-dependent RNA polymerase) constitutes thenucleocapsid protein  (ribonucleoprotein) of the virus.

Lassa virus is a double-segmented negative-strand RNA virus. The genome includes an S segment of about 3500 nt and an L segment of 7200 nt. Each genome encodes two proteins, separated by a non-coding intergenic region IGR (intergenic region). The S segment encodes the nucleoprotein NP (63 kDa) and the glycoprotein precursor GPC (75 kDa), and the L segment encodes the RNA polymerase L protein (200 kDa) and the matrix protein Z.

Arenaviruses are surrounded by a lipid bilayer containing the post-translationally processed viral glycoprotein involved in receptor binding (GP1) and viral cell entry (GP2). Underneath the lipid bilayer is a protein layer composed of the Z protein, which plays a major role in viral assembly and budding, and is the arenavirus counterpart of the matrix protein present in other enveloped negative-stranded (NS) RNA viruses. The core of the virus is made of a viral ribonucleoprotein (vRNP) complex, composed of the viral genome segments encapsidated by the viral NP . Incorporation of the vRNPs into newly nascent virions is mediated by NP-Z interaction. Associated with the vRNPs is the L polymerase protein that,together with NP , are the minimal components for viral genome replication and gene transcription.

 

Pre-glycoprotein polyprotein GP complex(P08669)

Function

Glycoprotein G1

Interacts with the host receptor (By similarity).

Mediates virus attachment to host receptor alpha-dystroglycan DAG1. This attachment induces virion internalization predominantly through clathrin- and caveolin-independent endocytosis 

 

Glycoprotein G2

Class I viral fusion protein that directs fusion of viral and host endosomal membranes, leading to delivery of the nucleocapsid into the cytoplasm. Membrane fusion is mediated by irreversible conformational changes induced upon acidification in the endosome.

 

Stable signal peptide (SSP)

Cleaved and functions as a signal peptide. In addition, it is also retained as the third component of the GP complex. The SSP is required for efficient glycoprotein expression, post-translational maturation cleavage of GP1 and GP2, glycoprotein transport to the cell surface plasma membrane, formation of infectious virus particles, and acid pH-dependent glycoprotein-mediated cell fusion.

 

Nucleoprotein(P13699)

Function

Encapsidates the genome, protecting it from nucleases. The encapsidated genomic RNA is termed the nucleocapsid (NC). Serves as template for viral transcription and replication. The increased presence of protein N in host cell does not seem to trigger the switch from transcription to replication as observed in other negative strain RNA viruses. Through the interaction with host IKBKE, strongly inhibits the phosphorylation and nuclear translocation of host IRF3, a protein involved in interferon activation pathway, leading to the inhibition of interferon-beta and IRF3-dependent promoters activation. Encodes also a functional 3'-5' exoribonuclease that degrades preferentially dsRNA substrates and thereby participates in the suppression of interferon induction.

 

RING finger protein Z(O73557)

Function

Plays a crucial role in virion assembly and budding. Expressed late in the virus life cycle, it acts as an inhibitor of viral transcription and RNA synthesis by interacting with the viral polymerase L. Presumably recruits the NP encapsidated genome to cellular membranes at budding sites via direct interaction with NP. Plays critical roles in the final steps of viral release by interacting with host TSG101, a member of the vacuolar protein-sorting pathway and using other cellular host proteins involved in vesicle formation pathway. The budding of the virus progeny occurs after association of protein Z with the viral glycoprotein complex SSP-GP1-GP2 at the cell periphery, step that requires myristoylation of protein Z. Also selectively represses protein production by associating with host eIF4E.

 

RNA-directed RNA polymerase L(O09705)

Function

RNA-dependent RNA polymerase which is responsible for replication and transcription of the viral RNA genome. During transcription, synthesizes 4 subgenomic RNAs, and assures their capping by a cap-snatching mechanism, in which cellular capped pre-mRNAs are used to generate primers for viral transcription. The 3'-end of subgenomic mRNAs molecules are heterogeneous and not polyadenylated. The replicase function is to direct synthesis of antigenomic and genomic RNA which are encapsidated and non capped. As a consequence of the use of the same enzyme for both transcription and replication, these mechanisms need to be well coordinated. These processes may be regulated by proteins N and Z in a dose-dependent manner.

 

References

  • 1. Lassa virus. PMID: 15487592
  • 2. Lassa virus glycoprotein complex review: insights into its unique fusion machinery. PMID: 35088070
  • 3. Lassa fever diagnostics: past, present, and future. PMID: 31518896
  • 4. Editorial overview: Lassa virus. PMID: 31564289
  • 5. Animal models for Lassa virus infection. PMID: 31442921
  • 6. Lassa virus diversity and feasibility for universal prophylactic vaccine. PMID: 30774934
  • 7. Lassa Fever Virus Binds Matriglycan-A Polymer of Alternating Xylose and Glucuronate-On alpha-Dystroglycan. PMID: 34578260
  • 8. Lassa virus glycoprotein: stopping a moving target. PMID: 29843991
  • 9. Phylogeography of Lassa Virus in Nigeria. PMID: 31413134
  • 10. Inter-Lineage Variation of Lassa Virus Glycoprotein Epitopes: A Challenge to Lassa Virus Vaccine Development. PMID: 32244402
  • 11. Immunobiology of Ebola and Lassa virus infections. PMID: 28111475
  • 12. Lassa virus circulating in Liberia: a retrospective genomic characterisation. PMID: 31588039
  • 13. Systematics, Ecology, and Host Switching: Attributes Affecting Emergence of the Lassa Virus in Rodents across Western Africa. PMID: 32183319
  • 14. A Lassa Virus Live-Attenuated Vaccine Candidate Based on Rearrangement of the Intergenic Region. PMID: 32209677
  • 15. Immune responses and Lassa virus infection. PMID: 23202504
  • 16. Lassa Virus Vaccine Candidate ML29 Generates Truncated Viral RNAs Which Contribute to Interfering Activity and Attenuation. PMID: 33573250
  • 17. Lassa Virus Reverse Genetics. PMID: 28508222
  • 18. Reverse genetics systems as tools to overcome the genetic diversity of Lassa virus. PMID: 31357141
1 product selected Compare
Terms of sale Website terms of use Cookie policy Privacy
Copyright © 2024 AntibodySystem SAS. All Rights Reserved.            All Products are for Research Use Only