Role of Jumonji C-domain containing protein 6 (JMJD6) in infectivity of foot-and-mouth disease virus

Lawrence, Paul; Rai, Devendra; Conderino, Joseph S.; Uddowla, Sabena; Rieder, Elizabeth

doi:10.1016/j.virol.2016.02.005

Cited by 24 publications

(30 citation statements)

References 66 publications

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“…Residue 95 is located at the interface between two VP1 proteins at the fivefold axis of the virus particle and interacts with the C-terminus of the Jumonji C-domain containing protein 6 (JMJD6) [52,64]. A substitution of glutamic acid with lysine at this position allows the virus to infect cells in culture in an integrin-and HS-independent manner [30,52,64].…”

Section: Virus Protein Vp1mentioning

confidence: 99%

Cell culture propagation of foot-and-mouth disease virus: adaptive amino acid substitutions in structural proteins and their functional implications

Dill

Eschbaumer

2019

Virus Genes

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Foot-and-mouth disease is endemic in livestock in large parts of Africa and Asia, where it is an important driver of food insecurity and a major obstacle to agricultural development and the international trade in animal products. Virtually all commercially available vaccines are inactivated whole-virus vaccines produced in cell culture, but the adaptation of a field isolate of the virus to growth in culture is laborious and time-consuming. This is of particular concern for the development of vaccines to newly emerging virus lineages, where long lead times from virus isolate to vaccine can delay the implementation of effective control programs. High antigen yields in production cells are also necessary to make vaccines affordable for less developed countries in endemic areas. Therefore, a rational approach to cell culture adaptation that combines prior knowledge of common adaptive mutations and reverse genetics techniques is urgently required. This review provides an overview of amino acid exchanges in the viral capsid proteins in the context of adaptation to cell culture.

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Section: Virus Protein Vp1mentioning

confidence: 99%

Cell culture propagation of foot-and-mouth disease virus: adaptive amino acid substitutions in structural proteins and their functional implications

Dill

Eschbaumer

2019

Virus Genes

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“…This assumption is supported through studies using an A 24 Cruzeiro mutant (A-SIR #42) that harbors the same E95K change in VP1 [ 17 ]. Further studies revealed this amino acid change to be responsible for utilizing Jumonji C-domain containing protein 6 to infect cells in an integrin- and HS-independent way [ 43 ]. Indeed, in the present study, A 24 -2P was the only mutant capable of infecting CHO677 cells, which do neither have surface integrins nor HS.…”

Section: Discussionmentioning

confidence: 99%

Influence of cell type and cell culture media on the propagation of foot-and-mouth disease virus with regard to vaccine quality

Dill

Hoffmann

Zimmer

et al. 2018

Virol J

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BackgroundSuspension culture of BHK cells allows large-scale virus propagation and cost-efficient vaccine production, while the shift to animal-component-free cell culture media without serum is beneficial for the quality and downstream processing of the product. Foot-and-mouth disease virus is still endemic in many parts of the world and high-quality vaccines are essential for the eradication of this highly contagious and economically devastating disease.MethodsChanges to the viral genome sequence during passaging in an adherent and a suspension cell culture system were compared and the impact of amino acid substitutions on receptor tropism, antigenicity and particle stability was examined. Virus production in suspension cells in animal-component-free media and in serum-containing media as well as in adherent cells in serum-containing media was compared. Infection kinetics were determined and the yield of intact viral particles was estimated in all systems using sucrose density gradient centrifugation.ResultsCapsid protein sequence alterations were serotype-specific, but varied between cell lines. But The A24-2P virus variant had expanded its receptor tropism, but virus neutralization tests found no changes in the antigenic profile in comparison to the original viruses. There were no differences in viral titer between a suspension and an adherent cell culture system, independent of the type of media used. Also, the usage of a serum-free suspension culture system promoted viral growth and allowed an earlier harvest. For serotype O isolates, no differences were seen in the yield of 146S particles. Serotype A preparations revealed a decreased yield of 146S particles in suspension cells independent of the culture media.ConclusionThe selective pressure of the available surface receptors in different cell culture systems may be responsible for alterations in the capsid coding sequence of culture-grown virus. Important vaccine potency characteristics such as viral titer and the neutralization profile were unaffected, but the 146S particle yield differed for one of the tested serotypes.Electronic supplementary materialThe online version of this article (10.1186/s12985-018-0956-0) contains supplementary material, which is available to authorized users.

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“…Sequencing of the viral particles isolated from vesicular fluid and tissue samples of these animals confirmed no alterations in the capsid sequence, showing that the JMJD6-FMDV mutant virus was indeed causing the clinical disease. The authors also postulate that differences in the degree of virulence based on the route of inoculation could be due to the non-accessibility of the key components of the third receptor pathway by aerosol route of inoculation [66,67]. …”

Section: Jmjd6 and Virusesmentioning

confidence: 99%

Bifunctional Enzyme JMJD6 Contributes to Multiple Disease Pathogenesis: New Twist on the Old Story

et al. 2017

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Jumonji domain-containing protein 6 (JMJD6) is a non-heme Fe(II) 2-oxoglutarate (2OG)-dependent oxygenase with arginine demethylase and lysyl hydroxylase activities. Its initial discovery as a dispensable phosphatidylserine receptor (PSR) in the cell membrane of macrophages for phagocytosis was squashed by newer studies which revealed its nuclear localization and bifunctional enzymatic activity. Though its interaction with several nuclear and cytoplasmic target proteins has been demonstrated, the exact mechanisms and clinical significance of these various biologic interplays are not yet well established. Recent investigations have shed the light on the multiple pathways by which JMJD6 can regulate cell proliferation and cause tumorigenesis. Clinically, JMJD6 has been associated with more aggressive and metastatic disease, poorer prognosis, and lower overall survival rates—particularly in lung colon and oral cancers. JMJD6 is a novel biomarker for predicting future disease outcomes and is a target for new therapeutic treatments in future studies. Aberrant expression and dysregulation of JMJD6 are implicated in various other processes such as impaired T-cell proliferation and maturation, inoculation, and virulence of foot-and-mouth disease virus (FMDV), and impaired methylation of innate immunity factor. This article reviews the association of JMJD6 with various pathological processes—particularly, its role in tumorigenesis and virological interactions.

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Role of Jumonji C-domain containing protein 6 (JMJD6) in infectivity of foot-and-mouth disease virus

Cited by 24 publications

References 66 publications

Cell culture propagation of foot-and-mouth disease virus: adaptive amino acid substitutions in structural proteins and their functional implications

Cell culture propagation of foot-and-mouth disease virus: adaptive amino acid substitutions in structural proteins and their functional implications

Influence of cell type and cell culture media on the propagation of foot-and-mouth disease virus with regard to vaccine quality

Bifunctional Enzyme JMJD6 Contributes to Multiple Disease Pathogenesis: New Twist on the Old Story

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