Journal articles: 'Virus de Lassa'

1

Günther, Stephan, and Oliver Lenz. "Lassa Virus." Critical Reviews in Clinical Laboratory Sciences 41, no. 4 (2004): 339–90. http://dx.doi.org/10.1080/10408360490497456.

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Lukashevich, Igor, and Maria Salvato. "Lassa Virus Genome." Current Genomics 7, no. 6 (2006): 351–79. http://dx.doi.org/10.2174/138920206778948673.

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Goldsmith, C. S., H. G. Morrison, D. D. Auperin, S. G. Whitfield, and E. L. Palmer. "Vaccinia-lassa recombinant produces lassa-like inclusions." Proceedings, annual meeting, Electron Microscopy Society of America 47 (August 6, 1989): 1036–37. http://dx.doi.org/10.1017/s0424820100157164.

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Lassa virus, a member of the Arenaviridae, is the etiologic agent of Lassa fever. The virus is endemic in widespread areas of West Africa, particularly Nigeria, Liberia, and Sierra Leone. Rough estimates indicate that there are upwards of 300,000 human infections annually, resulting in approximately 5000 fatalities. A safe and effective vaccine for Lassa fever is not yet available. Recent studies in our laboratories have focused on the development of recombinant vaccinia viruses that express the nucleoprotein and envelope glycoproteins of Lassa virus as potential vaccine candidates. Tissue culture cells infected with various recombinant viruses were examined by thin-section TEH for any morphological alterations.Tissue culture cells were infected with wild-type Lassa virus or with recombinant vaccinia viruses expressing either the Lassa virus nucleoprotein (NP). the envelope glycoproteins (GPI,GP2), or NP, GPI, and GP2 in combination. Cells were fixed in 2.5% glutaraldehyde in 0.2M cacodylate buffer, postfixed in buffered 1% osmium tetroxide, and en bloc stained with 4% uranyl acetate. The samples were dehydrated and embedded in Polysciences Epon-substitute and Araldite. Sections were stained with uranyl acetate and lead citrate.

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Schmaljohn, Connie, and David Safronetz. "Editorial overview: Lassa virus." Current Opinion in Virology 37 (August 2019): vii—ix. http://dx.doi.org/10.1016/j.coviro.2019.09.001.

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Hansen, Frederick, Michael A. Jarvis, Heinz Feldmann, and Kyle Rosenke. "Lassa Virus Treatment Options." Microorganisms 9, no. 4 (2021): 772. http://dx.doi.org/10.3390/microorganisms9040772.

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Lassa fever causes an approximate 5000 to 10,000 deaths annually in West Africa and cases have been imported into Europe and the Americas, challenging public health. Although Lassa virus was first described over 5 decades ago in 1969, no treatments or vaccines have been approved to treat or prevent infection. In this review, we discuss current therapeutics in the development pipeline for the treatment of Lassa fever, focusing on those that have been evaluated in humans or animal models. Several treatments, including the antiviral favipiravir and a human monoclonal antibody cocktail, have shown efficacy in preclinical rodent and non-human primate animal models and have potential for use in clinical settings. Movement of the promising preclinical treatment options for Lassa fever into clinical trials is critical to continue addressing this neglected tropical disease.

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Cosset, François-Loic, Philippe Marianneau, Geraldine Verney, et al. "Characterization of Lassa Virus Cell Entry and Neutralization with Lassa Virus Pseudoparticles." Journal of Virology 83, no. 7 (2009): 3228–37. http://dx.doi.org/10.1128/jvi.01711-08.

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ABSTRACT The cell entry and humoral immune response of the human pathogen Lassa virus (LV), a biosafety level 4 (BSL4) Old World arenavirus, are not well characterized. LV pseudoparticles (LVpp) are a surrogate model system that has been used to decipher factors and routes involved in LV cell entry under BSL2 conditions. Here, we describe LVpp, which are highly infectious, with titers approaching those obtained with pseudoparticles displaying G protein of vesicular stomatitis virus and their the use for the characterization of LV cell entry and neutralization. Upon cell attachment, LVpp utilize endocytic vesicles for cell entry as described for many pH-dependent viruses. However, the fusion of the LV glycoproteins is activated at unusually low pH values, with optimal fusion occurring between pH 4.5 and 3, a pH range at which fusion characteristics of viral glycoproteins have so far remained largely unexplored. Consistent with a shifted pH optimum for fusion activation, we found wild-type LV and LVpp to display a remarkable resistance to exposure to low pH. Finally, LVpp allow the fast and quantifiable detection of neutralizing antibodies in human and animal sera and will thus facilitate the study of the humoral immune response in LV infections.

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Urata, Shuzo, Takeshi Noda, Yoshihiro Kawaoka, Hideyoshi Yokosawa, and Jiro Yasuda. "Cellular Factors Required for Lassa Virus Budding." Journal of Virology 80, no. 8 (2006): 4191–95. http://dx.doi.org/10.1128/jvi.80.8.4191-4195.2006.

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ABSTRACT It is known that Lassa virus Z protein is sufficient for the release of virus-like particles (VLPs) and that it has two L domains, PTAP and PPPY, in its C terminus. However, little is known about the cellular factor for Lassa virus budding. We examined which cellular factors are used in Lassa virus Z budding. We demonstrated that Lassa Z protein efficiently produces VLPs and uses cellular factors, Vps4A, Vps4B, and Tsg101, in budding, suggesting that Lassa virus budding uses the multivesicular body pathway functionally. Our data may provide a clue to develop an effective antiviral strategy for Lassa virus.

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Bowen, Michael D., Pierre E. Rollin, Thomas G. Ksiazek, et al. "Genetic Diversity among Lassa Virus Strains." Journal of Virology 74, no. 15 (2000): 6992–7004. http://dx.doi.org/10.1128/jvi.74.15.6992-7004.2000.

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ABSTRACT The arenavirus Lassa virus causes Lassa fever, a viral hemorrhagic fever that is endemic in the countries of Nigeria, Sierra Leone, Liberia, and Guinea and perhaps elsewhere in West Africa. To determine the degree of genetic diversity among Lassa virus strains, partial nucleoprotein (NP) gene sequences were obtained from 54 strains and analyzed. Phylogenetic analyses showed that Lassa viruses comprise four lineages, three of which are found in Nigeria and the fourth in Guinea, Liberia, and Sierra Leone. Overall strain variation in the partial NP gene sequence was found to be as high as 27% at the nucleotide level and 15% at the amino acid level. Genetic distance among Lassa strains was found to correlate with geographic distance rather than time, and no evidence of a “molecular clock” was found. A method for amplifying and cloning full-length arenavirus S RNAs was developed and used to obtain the complete NP and glycoprotein gene (GP1 and GP2) sequences for two representative Nigerian strains of Lassa virus. Comparison of full-length gene sequences for four Lassa virus strains representing the four lineages showed that the NP gene (up to 23.8% nucleotide difference and 12.0% amino acid difference) is more variable than the glycoprotein genes. Although the evolutionary order of descent within Lassa virus strains was not completely resolved, the phylogenetic analyses of full-length NP, GP1, and GP2 gene sequences suggested that Nigerian strains of Lassa virus were ancestral to strains from Guinea, Liberia, and Sierra Leone. Compared to the New World arenaviruses, Lassa and the other Old World arenaviruses have either undergone a shorter period of diverisification or are evolving at a slower rate. This study represents the first large-scale examination of Lassa virus genetic variation.

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Mateo, Mathieu, Stéphanie Reynard, Alexandra Journeaux, et al. "A single-shot Lassa vaccine induces long-term immunity and protects cynomolgus monkeys against heterologous strains." Science Translational Medicine 13, no. 597 (2021): eabf6348. http://dx.doi.org/10.1126/scitranslmed.abf6348.

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A safe and protective Lassa virus vaccine is crucially needed in Western Africa to stem the recurrent outbreaks of Lassa virus infections in Nigeria and the emergence of Lassa virus in previously unaffected countries, such as Benin and Togo. Major challenges in developing a Lassa virus vaccine include the high diversity of circulating strains and their reemergence from 1 year to another. To address each of these challenges, we immunized cynomolgus monkeys with a measles virus vector expressing the Lassa virus glycoprotein and nucleoprotein of the prototypic Lassa virus strain Josiah (MeV-NP). To evaluate vaccine efficacy against heterologous strains of Lassa virus, we challenged the monkeys a month later with heterologous strains from lineage II or lineage VII, finding that the vaccine was protective against these strains. A second cohort of monkeys was challenged 1 year later with the homologous Josiah strain, finding that a single dose of MeV-NP was sufficient to protect all vaccinated monkeys. These studies demonstrate that MeV-NP can generate both long-lasting immune responses and responses that are able to protect against diverse strains of Lassa virus.

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Safronetz, David, Job E. Lopez, Nafomon Sogoba, et al. "Detection of Lassa Virus, Mali." Emerging Infectious Diseases 16, no. 7 (2010): 1123–26. http://dx.doi.org/10.3201/eid1607.100146.

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Charrel, Rémi N., and Xavier de Lamballerie. "Arenaviruses other than Lassa virus." Antiviral Research 57, no. 1-2 (2003): 89–100. http://dx.doi.org/10.1016/s0166-3542(02)00202-4.

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12

Saluzzo, J. F., F. Adam, J. B. McCormick, and J. P. Digoutte. "Lassa Fever Virus in Senegal." Journal of Infectious Diseases 157, no. 3 (1988): 605. http://dx.doi.org/10.1093/infdis/157.3.605.

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Hass, Meike, Uta Gölnitz, Stefanie Müller, Beate Becker-Ziaja, and Stephan Günther. "Replicon System for Lassa Virus." Journal of Virology 78, no. 24 (2004): 13793–803. http://dx.doi.org/10.1128/jvi.78.24.13793-13803.2004.

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ABSTRACT Lassa virus is endemic to West Africa and causes hemorrhagic fever in humans. To facilitate the functional analysis of this virus, a replicon system was developed based on Lassa virus strain AV. Genomic and antigenomic minigenomes (MG) were constructed consisting of the intergenic region of S RNA and a reporter gene (Renilla luciferase) in antisense orientation, flanked by the 5′ and 3′ untranslated regions of S RNA. MGs were expressed under the control of the T7 promoter. Nucleoprotein (NP), L protein, and Z protein were expressed from plasmids containing the T7 promoter and internal ribosomal entry site. Transfection of cells stably expressing T7 RNA polymerase (BSR T7/5) with MG in the form of DNA or RNA and plasmids for the expression of NP and L protein resulted in high levels of Renilla luciferase expression. The replicon system was optimized with respect to the ratio of the transfected constructs and by modifying the 5′ end of the MG. Maximum activity was observed 24 to 36 h after transfection with a signal-to-noise ratio of 2 to 3 log units. Northern blot analysis provided evidence for replication and transcription of the MG. Z protein downregulated replicon activity close to background levels. Treatment with ribavirin and alpha interferon inhibited replicon activity, suggesting that both act on the level of RNA replication, transcription, or ribonucleoprotein assembly. In conclusion, this study describes the first replicon system for a highly pathogenic arenavirus. It is a tool for investigating the mechanisms of replication and transcription of Lassa virus and may facilitate the testing of antivirals outside a biosafety level 4 laboratory.

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Attar, Naomi. "The history of Lassa virus." Nature Reviews Microbiology 13, no. 10 (2015): 600–601. http://dx.doi.org/10.1038/nrmicro3550.

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Ash, Caroline. "Mobile detection of Lassa virus." Science 363, no. 6422 (2019): 39.2–39. http://dx.doi.org/10.1126/science.363.6422.39-b.

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Malo, Courtney S. "One shot for Lassa virus." Science 372, no. 6547 (2021): 1162.20–1164. http://dx.doi.org/10.1126/science.372.6547.1162-t.

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Müller, Stefanie, and Stephan Günther. "Broad-Spectrum Antiviral Activity of Small Interfering RNA Targeting the Conserved RNA Termini of Lassa Virus." Antimicrobial Agents and Chemotherapy 51, no. 6 (2007): 2215–18. http://dx.doi.org/10.1128/aac.01368-06.

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ABSTRACT Small interfering RNAs targeting the conserved RNA termini upstream of NP and L gene were found to reduce reporter gene expression from Lassa virus replicon and Lassa virus mRNA expression construct and to inhibit replication of different Lassa virus strains, lymphocytic choriomeningitis virus, and Mopeia virus in cell culture.

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Smither, Sophie J., Lin S. Eastaugh, James S. Findlay, Lyn M. O’Brien, and Mark S. Lever. "Survival of Lassa Virus in Blood and Tissue Culture Media and in a Small Particle Aerosol." Pathogens 9, no. 9 (2020): 680. http://dx.doi.org/10.3390/pathogens9090680.

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Knowledge of the survival and stability of a pathogen is important for understanding its risk, reducing its transmission, and establishing control measures. Lassa virus is endemic in West Africa, causes severe disease, and is an emerging pathogen of concern. Our study examined the survival of Lassa virus in blood and tissue culture media at two different temperatures. The stability of Lassa virus held within a small particle aerosol was also measured. In liquids, Lassa virus was found to decay more quickly at 30 °C compared to room temperature. Sealed samples protected from environmental desiccation were more stable than samples open to the environment. In a small particle aerosol, the decay rate of Lassa virus was determined at 2.69% per minute. This information can contribute to risk assessments and inform mitigation strategies in the event of an outbreak of Lassa virus.

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Pushko, Peter, Joan Geisbert, Michael Parker, Peter Jahrling, and Jonathan Smith. "Individual and Bivalent Vaccines Based on Alphavirus Replicons Protect Guinea Pigs against Infection with Lassa and Ebola Viruses." Journal of Virology 75, no. 23 (2001): 11677–85. http://dx.doi.org/10.1128/jvi.75.23.11677-11685.2001.

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ABSTRACT Lassa and Ebola viruses cause acute, often fatal, hemorrhagic fever diseases, for which no effective vaccines are currently available. Although lethal human disease outbreaks have been confined so far to sub-Saharan Africa, they also pose significant epidemiological concern worldwide as demonstrated by several instances of accidental importation of the viruses into North America and Europe. In the present study, we developed experimental individual vaccines for Lassa virus and bivalent vaccines for Lassa and Ebola viruses that are based on an RNA replicon vector derived from an attenuated strain of Venezuelan equine encephalitis virus. The Lassa and Ebola virus genes were expressed from recombinant replicon RNAs that also encoded the replicase function and were capable of efficient intracellular self-amplification. For vaccinations, the recombinant replicons were incorporated into virus-like replicon particles. Guinea pigs vaccinated with particles expressing Lassa virus nucleoprotein or glycoprotein genes were protected from lethal challenge with Lassa virus. Vaccination with particles expressing Ebola virus glycoprotein gene also protected the animals from lethal challenge with Ebola virus. In order to evaluate a single vaccine protecting against both Lassa and Ebola viruses, we developed dual-expression particles that expressed glycoprotein genes of both Ebola and Lassa viruses. Vaccination of guinea pigs with either dual-expression particles or with a mixture of particles expressing Ebola and Lassa virus glycoprotein genes protected the animals against challenges with Ebola and Lassa viruses. The results showed that immune responses can be induced against multiple vaccine antigens coexpressed from an alphavirus replicon and suggested the possibility of engineering multivalent vaccines based upon alphavirus vectors for arenaviruses, filoviruses, and possibly other emerging pathogens.

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Okokhere, Peter O., Idowu A. Bankole, Christopher O. Iruolagbe, et al. "Aseptic Meningitis Caused by Lassa Virus: Case Series Report." Case Reports in Neurological Medicine 2016 (2016): 1–4. http://dx.doi.org/10.1155/2016/1978461.

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The Lassa virus is known to cause disease in different organ systems of the human body, with varying clinical manifestations. The features of severe clinical disease may include bleeding and/or central nervous system manifestations. Whereas Lassa fever encephalopathy and encephalitis are well described in the literature, there is paucity of data on Lassa virus meningitis. We present the clinical description, laboratory diagnosis, and management of 4 consecutive cases of aseptic meningitis associated with Lassa virus infection without bleeding seen in a region of Nigeria known to be endemic for both the reservoir rodent and Lassa fever. The 4 patients recovered fully following intravenous ribavirin treatment and suffered no neurologic complications.

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Cohen-Dvashi, Hadas, Nadav Cohen, Hadar Israeli, and Ron Diskin. "Molecular Mechanism for LAMP1 Recognition by Lassa Virus." Journal of Virology 89, no. 15 (2015): 7584–92. http://dx.doi.org/10.1128/jvi.00651-15.

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ABSTRACTLassa virus is a notorious human pathogen that infects many thousands of people each year in West Africa, causing severe viral hemorrhagic fevers and significant mortality. The surface glycoprotein of Lassa virus mediates receptor recognition through its GP1 subunit. Here we report the crystal structure of GP1 from Lassa virus, which is the first representative GP1 structure for Old World arenaviruses. We identify a unique triad of histidines that forms a binding site for LAMP1, a known lysosomal protein recently discovered to be a critical receptor for internalized Lassa virus at acidic pH. We demonstrate that mutation of this histidine triad, which is highly conserved among Old World arenaviruses, impairs LAMP1 recognition. Our biochemical and structural data further suggest that GP1 from Lassa virus may undergo irreversible conformational changes that could serve as an immunological decoy mechanism. Together with a variable region that we identify on the surface of GP1, those could be two distinct mechanisms that Lassa virus utilizes to avoid antibody-based immune response.IMPORTANCEStructural data at atomic resolution for viral proteins is key for understanding their function at the molecular level and can facilitate novel avenues for combating viral infections. Here we used X-ray protein crystallography to decipher the crystal structure of the receptor-binding domain (GP1) from Lassa virus. This is a pathogenic virus that causes significant illness and mortality in West Africa. This structure reveals the overall architecture of GP1 domains from the group of viruses known as the Old World arenaviruses. Using this structural information, we elucidated the mechanisms for pH switch and binding of Lassa virus to LAMP1, a recently identified host receptor that is critical for successful infection. Lastly, our structural analysis suggests two novel immune evasion mechanisms that Lassa virus may utilize to escape antibody-based immune response.

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Asper, Marcel, Thomas Sternsdorf, Meike Hass, et al. "Inhibition of Different Lassa Virus Strains by Alpha and Gamma Interferons and Comparison with a Less Pathogenic Arenavirus." Journal of Virology 78, no. 6 (2004): 3162–69. http://dx.doi.org/10.1128/jvi.78.6.3162-3169.2004.

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ABSTRACT The high pathogenicity of Lassa virus is assumed to involve resistance to the effects of interferon (IFN). We have analyzed the effects of alpha IFN (IFN-α), IFN-γ, and tumor necrosis factor alpha (TNF-α) on replication of Lassa virus compared to the related, but less pathogenic, lymphocytic choriomeningitis virus (LCMV). Three low-passage Lassa virus strains (AV, NL, and CSF), isolated from humans with mild to fulminant Lassa fever, were tested. Lassa virus replication was inhibited by IFN-α and IFN-γ, but not TNF-α, in Huh7 and Vero cells. The degree of IFN sensitivity of a Lassa virus isolate did not correlate with disease severity in human patients. Furthermore, cytokine effects observed for Lassa virus and LCMV (strains CH-5692, Armstrong, and WE) were similar. To address the mechanisms involved in the IFN effect, we used cell lines in which overexpression of IFN-stimulated proteins promyelocytic leukemia protein (PML) and Sp100 could be induced. Both proteins reside in PML bodies, a cellular target of the LCMV and Lassa virus Z proteins. Overexpression of PML or Sp100 did not affect replication of either virus. This, together with the previous finding that PML knockout facilitates LCMV replication in vitro and in vivo (M. Djavani, J. Rodas, I. S. Lukashevich, D. Horejsh, P. P. Pandolfi, K. L. Borden, and M. S. Salvato, J. Virol. 75:6204-6208, 2001; W. V. Bonilla, D. D. Pinschewer, P. Klenerman, V. Rousson, M. Gaboli, P. P. Pandolfi, R. M. Zinkernagel, M. S. Salvato, and H. Hengartner, J. Virol. 76:3810-3818, 2002), describes PML as a mediator within the antiviral pathway rather than as a direct effector protein. In conclusion, the high pathogenicity of Lassa virus compared to LCMV is probably not due to increased resistance to the effects of IFN-α or IFN-γ. Both cytokines inhibit replication which is relevant for the design of antiviral strategies against Lassa fever with the aim of enhancing the IFN response.

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McCormick, Joseph B., Karl M. Johnson, Isabel J. King, et al. "Lassa Virus Hepatitis: a Study of Fatal Lassa Fever in Humans." American Journal of Tropical Medicine and Hygiene 35, no. 2 (1986): 401–7. http://dx.doi.org/10.4269/ajtmh.1986.35.401.

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Jahrling, Peter B., John D. Frame, Sheilda B. Smith, and Mark H. Monson. "Endemic Lassa fever in Liberia. III. Characterization of Lassa virus isolates." Transactions of the Royal Society of Tropical Medicine and Hygiene 79, no. 3 (1985): 374–79. http://dx.doi.org/10.1016/0035-9203(85)90386-4.

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Ibukun, Francis Ifedayo. "Inter-Lineage Variation of Lassa Virus Glycoprotein Epitopes: A Challenge to Lassa Virus Vaccine Development." Viruses 12, no. 4 (2020): 386. http://dx.doi.org/10.3390/v12040386.

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Lassa virus (LASV), which causes considerable morbidity and mortality annually, has a high genetic diversity across West Africa. LASV glycoprotein (GP) expresses this diversity, but most LASV vaccine candidates utilize only the Lineage IV LASV Josiah strain GP antigen as an immunogen and homologous challenge with Lineage IV LASV. In addition to the sequence variation amongst the LASV lineages, these lineages are also distinguished in their presentations. Inter-lineage variations within previously mapped B-cell and T-cell LASV GP epitopes and the breadth of protection in LASV vaccine/challenge studies were examined critically. Multiple alignments of the GP primary sequence of strains from each LASV lineage showed that LASV GP has diverging degrees of amino acid conservation within known epitopes among LASV lineages. Conformational B-cell epitopes spanning different sites in GP subunits were less impacted by LASV diversity. LASV GP diversity should influence the approach used for LASV vaccine design. Expression of LASV GP on viral vectors, especially in its prefusion configuration, has shown potential for protective LASV vaccines that can overcome LASV diversity. Advanced vaccine candidates should demonstrate efficacy against all LASV lineages for evidence of a pan-LASV vaccine.

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ter Meulen, Jan, Marlis Badusche, Kristiane Kuhnt, et al. "Characterization of Human CD4+ T-Cell Clones Recognizing Conserved and Variable Epitopes of the Lassa Virus Nucleoprotein." Journal of Virology 74, no. 5 (2000): 2186–92. http://dx.doi.org/10.1128/jvi.74.5.2186-2192.2000.

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ABSTRACT T cells must play the major role in controlling acute human Lassa virus infection, because patients recover from acute Lassa fever in the absence of a measurable neutralizing antibody response. T cells alone seem to protect animals from a lethal Lassa virus challenge, because after experimental vaccination no neutralizing antibodies are detectable. In order to study human T-cell reactivity to single Lassa virus proteins, the nucleoprotein (NP) of Lassa virus, strain Josiah, was cloned, expressed in Escherichia coli, and affinity purified. Peripheral blood mononuclear cells (PBMC) obtained from 8 of 13 healthy, Lassa virus antibody-positive individuals living in the Republic of Guinea, western Africa, were found to proliferate in response to the recombinant protein (proliferation index ≥10). PBMC obtained from one individual with a particularly high proliferative response were used to generate 50 NP-specific T-cell clones (TCC). For six of these the epitopes were mapped with overlapping synthetic peptides derived from the sequence of the NP. These CD4+TCC displayed high specific proliferation and produced mainly gamma interferon upon stimulation with NP. Because variation of up to 15% in the amino acid sequences of the structural proteins of naturally occurring Lassa virus variants has been observed, the reactivity of the TCC with peptides derived from the homologous epitopes of the Nigeria strain of Lassa virus and of the eastern Africa arenavirus Mopeia was tested. With the Nigeria strain of Lassa virus the levels of homology were 100% for two of these epitopes and 85% for three of them, whereas homology with the respective Mopeia epitopes ranged from 92 to 69%. Reactivity of the TCC with peptides derived from the variable epitopes of the Nigeria strain and of Mopeia was reduced or completely abolished. This report shows for the first time that seropositive individuals from areas of endemicity have very strong memory CD4+ T-cell responses against the NP of Lassa virus, which are partly strain specific and partly cross-reactive with other Lassa virus strains. Our findings may have important implications for the strategy of designing recombinant vaccines against this mainly T-cell-controlled human arenavirus infection.

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Schlie, Katrin, Anna Maisa, Fabian Freiberg, Allison Groseth, Thomas Strecker, and Wolfgang Garten. "Viral Protein Determinants of Lassa Virus Entry and Release from Polarized Epithelial Cells." Journal of Virology 84, no. 7 (2010): 3178–88. http://dx.doi.org/10.1128/jvi.02240-09.

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ABSTRACT The epithelium plays a key role in the spread of Lassa virus. Transmission from rodents to humans occurs mainly via inhalation or ingestion of droplets, dust, or food contaminated with rodent urine. Here, we investigated Lassa virus infection in cultured epithelial cells and subsequent release of progeny viruses. We show that Lassa virus enters polarized Madin-Darby canine kidney (MDCK) cells mainly via the basolateral route, consistent with the basolateral localization of the cellular Lassa virus receptor α-dystroglycan. In contrast, progeny virus was efficiently released from the apical cell surface. Further, we determined the roles of the glycoprotein, matrix protein, and nucleoprotein in directed release of nascent virus. To do this, a virus-like-particle assay was developed in polarized MDCK cells based on the finding that, when expressed individually, both the glycoprotein GP and matrix protein Z form virus-like particles. We show that GP determines the apical release of Lassa virus from epithelial cells, presumably by recruiting the matrix protein Z to the site of virus assembly, which is in turn essential for nucleocapsid incorporation into virions.

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Strecker, Thomas, Robert Eichler, Jan ter Meulen, et al. "Lassa Virus Z Protein Is a Matrix Protein Sufficient for the Release of Virus-Like Particles." Journal of Virology 77, no. 19 (2003): 10700–10705. http://dx.doi.org/10.1128/jvi.77.19.10700-10705.2003.

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ABSTRACT Lassa virus is an enveloped virus with glycoprotein spikes on its surface. It contains an RNA ambisense genome that encodes the glycoprotein precursor GP-C, the nucleoprotein NP, the polymerase L, and the Z protein. Here we demonstrate that the Lassa virus Z protein (i) is abundant in viral particles, (ii) is strongly membrane associated, (iii) is sufficient in the absence of all other viral proteins to release enveloped particles, and (iv) contains two late domains, PTAP and PPXY, necessary for the release of virus-like particles. Our data provide evidence that Z is the Lassa virus matrix protein that is the driving force for virus particle release.

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Müller, Stefanie, Robert Geffers, and Stephan Günther. "Analysis of gene expression in Lassa virus-infected HuH-7 cells." Journal of General Virology 88, no. 5 (2007): 1568–75. http://dx.doi.org/10.1099/vir.0.82529-0.

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The pathogenesis of Lassa fever is poorly understood. As the liver is a major target organ of Lassa virus, gene expression in Lassa virus-infected HuH-7 cells, a differentiated human hepatoma cell line, was studied. Cellular mRNA levels were measured at the late phase of acute infection, when virtually all cells expressed large amounts of nucleoprotein, and virus RNA concentration had reached >108 copies (ml supernatant)−1. Two types of transcription array were used: cDNA-based macroarrays with a set of 3500 genes (Atlas Human 1.2 arrays; Clontech) and oligonucleotide-based microarrays covering 18 400 transcripts (Human Genome U133A array; Affymetrix). Data analysis was based on statistical frameworks controlling the false-discovery rate. Atlas array data were considered relevant if they could be verified by U133A array or real-time RT-PCR. According to these criteria, there was no evidence for true changes in gene expression. Considering the precision of the U133A array and the number of replicates tested, potential expression changes due to Lassa virus infection are probably smaller than twofold. To substantiate the array data, beta interferon (IFN-β) gene expression was studied longitudinally in Lassa virus-infected HuH-7 and FRhK-4 cells by using real-time RT-PCR. IFN-β mRNA levels increased only twofold upon Lassa virus infection, although there was no evidence that the virus inhibited poly(I : C)-induced IFN-β gene expression. In conclusion, Lassa virus interferes only minimally with gene expression in HuH-7 cells and poorly induces IFN-β gene transcription.

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Russier, Marion, Delphine Pannetier, and Sylvain Baize. "Immune Responses and Lassa Virus Infection." Viruses 4, no. 11 (2012): 2766–85. http://dx.doi.org/10.3390/v4112766.

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Sironi, Manuela, and Juan C. de la Torre. "The chameleonic genetics of Lassa virus." Lancet Infectious Diseases 19, no. 12 (2019): 1276–77. http://dx.doi.org/10.1016/s1473-3099(19)30528-6.

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Baize, Sylvain. "Virus Lassa et cellules dendritiques myéloïdes." médecine/sciences 35, no. 8-9 (2019): 619–21. http://dx.doi.org/10.1051/medsci/2019122.

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Hurtley, S. M. "How Lassa virus breaks and enters." Science 344, no. 6191 (2014): 1476–77. http://dx.doi.org/10.1126/science.344.6191.1476-e.

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Tamrakar, Sushil B., and Charles N. Haas. "Dose-Response Model for Lassa Virus." Human and Ecological Risk Assessment: An International Journal 14, no. 4 (2008): 742–52. http://dx.doi.org/10.1080/10807030802235151.

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Tang-Huau, Tsing-Lee, H. Feldmann, and K. Rosenke. "Animal models for Lassa virus infection." Current Opinion in Virology 37 (August 2019): 112–17. http://dx.doi.org/10.1016/j.coviro.2019.07.005.

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ter Meulen, J., K. Koulemou, T. Wittekindt, et al. "Detection of Lassa Virus Antinucleoprotein Immunoglobulin G (IgG) and IgM Antibodies by a Simple Recombinant Immunoblot Assay for Field Use." Journal of Clinical Microbiology 36, no. 11 (1998): 3143–48. http://dx.doi.org/10.1128/jcm.36.11.3143-3148.1998.

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The nucleoprotein of Lassa virus, strain Josiah, was expressed inEscherichia coli as an N-terminally truncated, histidine-tagged recombinant protein. Following affinity purification the protein was completely denatured and spotted onto nitrocellulose membrane. A total of 1 μg of protein was applied for detection of Lassa virus antibodies (LVA) in a simple immunoblot assay. Specific anti-Lassa immunoglobulin M (IgM) antibodies could be detected by increasing the amount of protein to 5 μg. A panel of 913 serum specimens from regions in which Lassa virus was endemic and from regions in which Lassa virus was not endemic was used for evaluating the sensitivity and specificity of the LVA immunoblot in comparison to those of an indirect immunofluorescence (IIF) assay. The sera originated from field studies conducted in the Republic of Guinea (570 serum samples) and Liberia (99 serum samples), from inpatients of the clinical department of the Bernhard-Nocht-Institute, Hamburg, Germany (94 serum samples), and from healthy German blood donors (150 serum samples). In comparison to the IIF assay the LVA immunoblot assay had a specificity of 90.0 to 99.3%, depending on the origin of the specimens. The sensitivity was found to be highest for the Guinean samples (90.7%) and was lower for the Liberian samples (75%). Acute Lassa fever was diagnosed by PCR in 12 of 59 (20.3%) patients with fever of unknown origin (FUO) from the Republic of Guinea. On admission to the hospital, nine Lassa fever patients (75%) were reactive by the IgM immunoblot assay. One of the patients was infected with a new Lassa variant, which showed 10.4% variation on the amino acid level in comparison to the prototype strain of Lassa virus, Josiah. Seven PCR-negative patients were reactive by immunoblotting. The positive and negative predictive values of a single IgM immunoblot result for acute, PCR-confirmed Lassa fever were therefore 53.6 and 93.0%, respectively. Because of its high negative predictive value, a single IgM immunoblot result will be valuable for excluding acute Lassa fever for cases of FUO in areas where Lassa fever is endemic.

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Günther, Stephan, Boye Weisner, Andreas Roth, et al. "Lassa Fever Encephalopathy: Lassa Virus in Cerebrospinal Fluid but Not in Serum." Journal of Infectious Diseases 184, no. 3 (2001): 345–49. http://dx.doi.org/10.1086/322033.

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Fisher-Hoch, S. P., L. Hutwagner, B. Brown, and J. B. McCormick. "Effective Vaccine for Lassa Fever." Journal of Virology 74, no. 15 (2000): 6777–83. http://dx.doi.org/10.1128/jvi.74.15.6777-6783.2000.

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ABSTRACT Lassa fever has been estimated to cause 5,000 deaths annually in West Africa. Recently, war in the zone where Lassa fever is hyperendemic has severely impeded control and treatment. Vaccination is the most viable control measure. There is no correlation between antibody levels and outcome in human patients, and inactivated vaccines produce high titers of antibodies to all viral proteins but do not prevent virus replication and death in nonhuman primates. Accordingly, we vaccinated 44 macaques with vaccinia virus-expressed Lassa virus structural proteins separately and in combination, with the object of inducing a predominantly TH1-type immune response. Following Lassa virus challenge, all unvaccinated animals died (0% survival). Nine of 10 animals vaccinated with all proteins survived (90% survival). Although no animals that received full-length glycoprotein alone had a high titer of antibody, 17 of 19 survived challenge (88%). In contrast, all animals vaccinated with nucleoprotein developed high titers of antibody but 12 of 15 died (20% survival). All animals vaccinated with single glycoproteins, G1 or G2, died, but all those that received both single glycoproteins (G1 plus G2) at separate sites survived, showing that both glycoproteins are independently important in protection. Neither group had demonstrable antibody levels prior to challenge. We demonstrate that in primates, immune responses to epitopes on both glycoproteins are required to protect against lethal challenge with Lassa virus without having untoward side effects and that this protection is likely to be primarily cell mediated. We show that an effective, safe vaccine against Lassa virus can and should be made and that its evaluation for human populations is a matter of humanitarian priority.

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Zapata, Juan, Sandra Medina-Moreno, Camila Guzmán-Cardozo, and Maria Salvato. "Improving the Breadth of the Host’s Immune Response to Lassa Virus." Pathogens 7, no. 4 (2018): 84. http://dx.doi.org/10.3390/pathogens7040084.

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In 2017, the global Coalition for Epidemic Preparedness (CEPI) declared Lassa virus disease to be one of the world’s foremost biothreats. In January 2018, World Health Organization experts met to address the Lassa biothreat. It was commonly recognized that the diversity of Lassa virus (LASV) isolated from West African patient samples was far greater than that of the Ebola isolates from the West African epidemic of 2013–2016. Thus, vaccines produced against Lassa virus disease face the added challenge that they must be broadly-protective against a wide variety of LASV. In this review, we discuss what is known about the immune response to Lassa infection. We also discuss the approaches used to make broadly-protective influenza vaccines and how they could be applied to developing broad vaccine coverage against LASV disease. Recent advances in AIDS research are also potentially applicable to the design of broadly-protective medical countermeasures against LASV disease.

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Kolawole, Daniel, Hayatu Raji, and Malachy Ifeanyi Okeke. "Phylogenetic and Mutational Analysis of Lassa Virus Strains Isolated in Nigeria: Proposal for an In Silico Study." JMIR Research Protocols 10, no. 3 (2021): e23015. http://dx.doi.org/10.2196/23015.

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Background In 2018, the total number of Lassa fever cases in Nigeria was significantly higher than that observed in previous years. Hence, studies had attempted to determine the underlying cause. However, reports using phylogenetic methods to analyze this finding ruled out the emergence of potentially more transmissible Lassa virus strains or an increase in human-to-human viral transmission as the cause underlying the increase in cases. Two years later, the situation seems even worse as the number of confirmed cases has reached an all-time high according to situational reports released by the Nigerian Center for Disease Control. Objective Considering the increasing trend of Lassa fever cases and related mortality, the major objective of this study is to map mutations within the genomes of Lassa virus isolates from 2018 and 2019 using the reference sequence available at the National Center for Biotechnology Information as a benchmark and compare them to the genomes of viruses isolated during 1969-2017. This study would also attempt to identify a viral marker gene for easier identification and grouping. Finally, the time-scaled evolution of Lassa virus in Nigeria will be reconstructed. Methods After collecting the sequence data of Lassa virus isolates, Bayesian phylogenetic trees, a sequence identity matrix, and a single nucleotide polymorphism matrix will be generated using BEAST (version 2.6.2), Base-By-Base, and DIVEIN (a web-based tool for variant calling), respectively. Results Mining and alignment of Lassa virus genome sequences have been completed, while mutational analysis and the reconstruction of time-scaled maximum clade credibility trees, congruence tests for inferred segments, and gene phylogeny analysis are ongoing. Conclusions The findings of this study would further the current knowledge of the evolutionary history of the Lassa virus in Nigeria and would document the mutations in Nigerian isolates from 1969 to 2019. International Registered Report Identifier (IRRID) DERR1-10.2196/23015

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Anderson, George P., Jinny L. Liu, Lisa C. Shriver-Lake, and Ellen R. Goldman. "Selection and Characterization of Single-Domain Antibodies for Detection of Lassa Nucleoprotein." Antibodies 9, no. 4 (2020): 71. http://dx.doi.org/10.3390/antib9040071.

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Lassa virus is the etiologic agent of Lassa fever, an acute and often fatal illness endemic to West Africa. It is important to develop new reagents applicable either for the specific diagnosis or as improved therapeutics for the treatment of Lassa fever. Here, we describe the development and initial testing of llama-derived single-domain antibodies that are specific for the Lassa virus nucleoprotein. Four sequence families based on complementarity-determining region (CDR) homology were identified by phage-based enzyme-linked immunosorbent assays, however, the highest affinity clones all belonged to the same sequence family which possess a second disulfide bond between Framework 2 and CDR3. The affinity and thermal stability were evaluated for each clone. A MagPlex-based homogeneous sandwich immunoassay for Lassa virus-like particles was also demonstrated to show their potential for further development as diagnostic reagents.

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Lee, Andrew M., Justin Cruite, Megan J. Welch, Brian Sullivan, and Michael B. A. Oldstone. "Pathogenesis of Lassa fever virus infection: I. Susceptibility of mice to recombinant Lassa Gp/LCMV chimeric virus." Virology 442, no. 2 (2013): 114–21. http://dx.doi.org/10.1016/j.virol.2013.04.010.

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Bausch, D. G., P. E. Rollin, A. H. Demby, et al. "Diagnosis and Clinical Virology of Lassa Fever as Evaluated by Enzyme-Linked Immunosorbent Assay, Indirect Fluorescent-Antibody Test, and Virus Isolation." Journal of Clinical Microbiology 38, no. 7 (2000): 2670–77. http://dx.doi.org/10.1128/jcm.38.7.2670-2677.2000.

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The Lassa virus (an arenavirus) is found in West Africa, where it sometimes causes a severe hemorrhagic illness called Lassa fever. Laboratory diagnosis has traditionally been by the indirect fluorescent-antibody (IFA) test. However, enzyme-linked immunosorbent assays (ELISAs) for Lassa virus antigen and immunoglobulin M (IgM) and G (IgG) antibodies have been developed that are thought to be more sensitive and specific. We compared ELISA and IFA testing on sera from 305 suspected cases of Lassa fever by using virus isolation with a positive reverse transcription-PCR (RT-PCR) test as the “gold standard.” Virus isolation and RT-PCR were positive on 50 (16%) of the 305 suspected cases. Taken together, Lassa virus antigen and IgM ELISAs were 88% (95% confidence interval [CI], 77 to 95%) sensitive and 90% (95% CI, 88 to 91%) specific for acute infection. Due to the stringent gold standard used, these likely represent underestimates. Diagnosis could often be made on a single serum specimen. Antigen detection was particularly useful in providing early diagnosis as well as prognostic information. Level of antigenemia varied inversely with survival. Detection by ELISA of IgG antibody early in the course of illness helped rule out acute Lassa virus infection. The presence of IFA during both acute and convalescent stages of infection, as well as significant interobserver variation in reading the slides, made interpretation difficult. However, the assay provided useful prognostic information, the presence of IFA early in the course of illness correlating with death. The high sensitivity and specificity, capability for early diagnosis, and prognostic value of the ELISAs make them the diagnostic tests of choice for the detection of Lassa fever.

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Lukashevich, Igor S., Jean Patterson, Ricardo Carrion, et al. "A Live Attenuated Vaccine for Lassa Fever Made by Reassortment of Lassa and Mopeia Viruses." Journal of Virology 79, no. 22 (2005): 13934–42. http://dx.doi.org/10.1128/jvi.79.22.13934-13942.2005.

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ABSTRACT Lassa virus (LASV) and Mopeia virus (MOPV) are closely related Old World arenaviruses that can exchange genomic segments (reassort) during coinfection. Clone ML29, selected from a library of MOPV/LASV (MOP/LAS) reassortants, encodes the major antigens (nucleocapsid and glycoprotein) of LASV and the RNA polymerase and zinc-binding protein of MOPV. Replication of ML29 was attenuated in guinea pigs and nonhuman primates. In murine adoptive-transfer experiments, as little as 150 PFU of ML29 induced protective cell-mediated immunity. All strain 13 guinea pigs vaccinated with clone ML29 survived at least 70 days after LASV challenge without either disease signs or histological lesions. Rhesus macaques inoculated with clone ML29 developed primary virus-specific T cells capable of secreting gamma interferon in response to homologous MOP/LAS and heterologous MOPV and lymphocytic choriomeningitis virus. Detailed examination of two rhesus macaques infected with this MOPV/LAS reassortant revealed no histological lesions or disease signs. Thus, ML29 is a promising attenuated vaccine candidate for Lassa fever.

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Clegg, J. C. S., and G. Lloyd. "VACCINIA RECOMBINANT EXPRESSING LASSA-VIRUS INTERNAL NUCLEOCAPSID PROTEIN PROTECTS GUINEAPIGS AGAINST LASSA FEVER." Lancet 330, no. 8552 (1987): 186–88. http://dx.doi.org/10.1016/s0140-6736(87)90767-7.

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Gunther, Stephan. "Imported Lassa Fever in Germany: Molecular Characterization of a New Lassa Virus Strain." Emerging Infectious Diseases 6, no. 5 (2000): 466–76. http://dx.doi.org/10.3201/eid0605.000504.

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Loureiro, María, Alejandra D’Antuono, and Nora López. "Virus–Host Interactions Involved in Lassa Virus Entry and Genome Replication." Pathogens 8, no. 1 (2019): 17. http://dx.doi.org/10.3390/pathogens8010017.

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Lassa virus (LASV) is the causative agent of Lassa fever, a human hemorrhagic disease associated with high mortality and morbidity rates, particularly prevalent in West Africa. Over the past few years, a significant amount of novel information has been provided on cellular factors that are determinant elements playing a role in arenavirus multiplication. In this review, we focus on host proteins that intersect with the initial steps of the LASV replication cycle: virus entry and genome replication. A better understanding of relevant virus–host interactions essential for sustaining these critical steps may help to identify possible targets for the rational design of novel therapeutic approaches against LASV and other arenaviruses that cause severe human disease.

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Salvato, Maria S., Arban Domi, Camila Guzmán-Cardozo, et al. "A Single Dose of Modified Vaccinia Ankara Expressing Lassa Virus-like Particles Protects Mice from Lethal Intra-cerebral Virus Challenge." Pathogens 8, no. 3 (2019): 133. http://dx.doi.org/10.3390/pathogens8030133.

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Lassa fever surpasses Ebola, Marburg, and all other hemorrhagic fevers except Dengue in its public health impact. Caused by Lassa virus (LASV), the disease is a scourge on populations in endemic areas of West Africa, where reported incidence is higher. Here, we report construction, characterization, and preclinical efficacy of a novel recombinant vaccine candidate GEO-LM01. Constructed in the Modified Vaccinia Ankara (MVA) vector, GEO-LM01 expresses the glycoprotein precursor (GPC) and zinc-binding matrix protein (Z) from the prototype Josiah strain lineage IV. When expressed together, GP and Z form Virus-Like Particles (VLPs) in cell culture. Immunogenicity and efficacy of GEO-LM01 was tested in a mouse challenge model. A single intramuscular dose of GEO-LM01 protected 100% of CBA/J mice challenged with a lethal dose of ML29, a Mopeia/Lassa reassortant virus, delivered directly into the brain. In contrast, all control animals died within one week. The vaccine induced low levels of antibodies but Lassa-specific CD4+ and CD8+ T cell responses. This is the first report showing that a single dose of a replication-deficient MVA vector can confer full protection against a lethal challenge with ML29 virus.

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Olayemi, Ayodeji, and Elisabeth Fichet-Calvet. "Systematics, Ecology, and Host Switching: Attributes Affecting Emergence of the Lassa Virus in Rodents across Western Africa." Viruses 12, no. 3 (2020): 312. http://dx.doi.org/10.3390/v12030312.

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Ever since it was established that rodents serve as reservoirs of the zoonotic Lassa virus (LASV), scientists have sought to answer the questions: which populations of rodents carry the virus? How do fluctuations in LASV prevalence and rodent abundance influence Lassa fever outbreaks in humans? What does it take for the virus to adopt additional rodent hosts, proliferating what already are devastating cycles of rodent-to-human transmission? In this review, we examine key aspects of research involving the biology of rodents that affect their role as LASV reservoirs, including phylogeography, demography, virus evolution, and host switching. We discuss how this knowledge can help control Lassa fever and suggest further areas for investigation.

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Whitmer, Shannon L. M., Thomas Strecker, Daniel Cadar, et al. "New Lineage of Lassa Virus, Togo, 2016." Emerging Infectious Diseases 24, no. 3 (2018): 599–602. http://dx.doi.org/10.3201/eid2403.171905.

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Journal articles on the topic 'Virus de Lassa'

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