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Relevant bibliographies by topics / FMDV Virulence Factor

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Journal articles

Academic literature on the topic 'FMDV Virulence Factor'

Author: Grafiati

Published: 3 June 2025

Last updated: 31 July 2025

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Journal articles on the topic "FMDV Virulence Factor"

1

Swaroop, Sarkar, V.V.S.Suryanarayana, and Shankar S.R.Madhan. "CLONING AND EXPRESSION OF LB-PROTEASE FROM CDNA CLONE OF FOOT-AND- MOUTH DISEASE VIRUS." International Journal of Research - Granthaalayah 5, no. 9SE (2017): 62–71. https://doi.org/10.5281/zenodo.1020885.

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Foot-and –Mouth disease virus (FMDV) is a positive sense RNA virus and the genome codes for single polyprotein. The FMDV L protein is located at the N terminus of the polyprotein and is the first gene product released from the nascent polyprotein. The leader L protease which is involved in pathogenesis has two known functions: (i) auto-catalytic removal from the N terminus of the viral polyprotein and (ii) cleavage of the p220 subunit of the eukaryotic initiation factor 4F complex, which helps to shut off host protein synthesis. To explore the role of L protease in FMDV pathogenesis we generat

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2

Hinton, Tracey M., Natalie Ross-Smith, Simone Warner, Graham J. Belsham, and Brendan S. Crabb. "Conservation of L and 3C proteinase activities across distantly related aphthoviruses." Journal of General Virology 83, no. 12 (2002): 3111–21. http://dx.doi.org/10.1099/0022-1317-83-12-3111.

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The foot-and-mouth disease virus (FMDV) leader (L) proteinase is an important virulence determinant in FMDV infections. It possesses two distinct catalytic activities: (i) C-terminal processing at the L/VP4 junction; and (ii) induction of the cleavage of translation initiation factor eIF4G, an event that inhibits cap-dependent translation in infected cells. The only other member of the Aphthovirus genus, equine rhinitis A virus (ERAV), also encodes an L protein, but this shares only 32% amino acid identity with its FMDV counterpart. Another more distantly related picornavirus, equine rhinitis

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3

Pereira, Elisa Dias, Thalison Rodrigues Moreira, Vanessa Rafaela Milhomem Cruz-Leite, et al. "Paracoccidioides lutzii Infects Galleria mellonella Employing Formamidase as a Virulence Factor." PLOS Neglected Tropical Diseases 18, no. 9 (2024): e0012452. http://dx.doi.org/10.1371/journal.pntd.0012452.

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The formamidase (FMD) enzyme plays an important role in fungal thriving by releasing a secondary nitrogen source as a product of its activity. In Paracoccidioides species, previous studies have demonstrated the upregulation of this enzyme in a wide range of starvation and infective-like conditions. However, Paracoccidioides lutzii formamidase has not yet been defined as a virulence factor. Here, by employing in vivo infections using an fmd-silenced strain in Galleria mellonella larvae model, we demonstrate the influence of formamidase in P. lutzii’s immune stimulation and pathogenicity. The fo

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4

Azzinaro, Paul A., Gisselle N. Medina, Devendra Rai, et al. "Mutation of FMDV Lpro H138 residue drives viral attenuation in cell culture and in vivo in swine." Frontiers in Veterinary Science 9 (October 31, 2022). http://dx.doi.org/10.3389/fvets.2022.1028077.

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The foot-and-mouth disease virus (FMDV) leader proteinase (Lpro) is a papain like protease that cleaves the viral polyprotein and several host factors affecting host cell translation and induction of innate immunity. Introduction of Lpro mutations ablating catalytic activity is not tolerated by the virus, however, complete coding sequence deletion or introduction of targeted amino acid substitutions can render viable progeny. In proof-of-concept studies, we have previously identified and characterized FMDV Lpro mutants that are attenuated in cell culture and in animals, while retaining their c

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5

Zhang, Xiangle, Pengfei Li, Wenzhe Chen, et al. "Impaired interferon response in senecavirus A infection and identification of 3C ^pro as an antagonist." Journal of Virology, June 13, 2024. http://dx.doi.org/10.1128/jvi.00585-24.

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ABSTRACT Senecavirus A (SVA), a picornavirus, causes vesicular diseases and epidemic transient neonatal losses in swine, resulting in a multifaceted economic impact on the swine industry. SVA counteracts host antiviral response through multiple strategies facilitatng viral infection and transmission. However, the mechanism of how SVA modulates interferon (IFN) response remains elusive. Here, we demonstrate that SVA 3C protease (3C pro ) blocks the transduction of Janus kinase-signal transducer and activator of transcription (JAK-STAT) signaling pathway to antagonize type I IFN response. Mechan

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