Presentation of antigenic sites from foot-and-mouth disease virus on the surface of baculovirus and in the membrane of infected cells

2000 ◽  
Vol 145 (9) ◽  
pp. 1815-1828 ◽  
Author(s):  
C. Tami ◽  
M. Farber ◽  
E. L. Palma ◽  
O. Taboga
Keyword(s):  
Disease Virus ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Antigenic Sites ◽  
Mouth Disease Virus ◽  
Foot And Mouth ◽  
Infected Cells

scholarly journals Impairment of the DeISGylation Activity of Foot-and-Mouth Disease Virus Lpro Causes Attenuation In Vitro and In Vivo

2020 ◽  
Vol 94 (13) ◽  
Author(s):  
Gisselle N. Medina ◽  
Paul Azzinaro ◽  
Elizabeth Ramirez-Medina ◽  
Joseph Gutkoska ◽  
Ying Fang ◽  
...  
Keyword(s):  
Disease Virus ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Type I ◽  
Mouth Disease Virus ◽  
Foot And Mouth ◽  
Infected Cells ◽  
Viral Attenuation

ABSTRACT Foot-and-mouth disease virus (FMDV) leader proteinase (Lpro) affects several pathways of the host innate immune response. Previous studies in bovine cells demonstrated that deletions (leaderless [LLV]) or point mutations in Lpro result in increased expression of interferon (IFN) and IFN-stimulated genes (ISGs), including, among others, the ubiquitin-like protein modifier ISG15 and the ubiquitin specific peptidase USP18. In addition to its conventional papain-like protease activity, Lpro acts as a deubiquitinase (DUB) and deISGylase. In this study, we identified a conserved residue in Lpro that is involved in its interaction with ISG15. Mutation W105A rendered Escherichia coli-expressed Lpro unable to cleave the synthetic substrate pro-ISG15 while preserving cellular eIF4G cleavage. Interestingly, mutant FMDV W105A was viable. Overexpression of ISG15 and the ISGylation machinery in porcine cells resulted in moderate inhibition of FMDV replication, along with a decrease of the overall state of ISGylation in wild-type (WT)-infected cells. In contrast, reduced deISGylation was observed upon infection with W105A and leaderless virus. Reduction in the levels of deubiquitination was also observed in cells infected with the FMDV LproW105A mutant. Surprisingly, similarly to WT, infection with W105A inhibited IFN/ISG expression despite displaying an attenuated phenotype in vivo in mice. Altogether, our studies indicate that abolishing/reducing the deISGylase/DUB activity of Lpro causes viral attenuation independently of its ability to block the expression of IFN and ISG mRNA. Furthermore, our studies highlight the potential of ISG15 to be developed as a novel biotherapeutic molecule against FMD. IMPORTANCE In this study, we identified an aromatic hydrophobic residue in foot-and-mouth disease virus (FMDV) leader proteinase (Lpro) (W105) that is involved in the interaction with ISG15. Mutation in Lpro W105 (A12-LproW105A) resulted in reduced deISGylation in vitro and in porcine-infected cells. Impaired deISGylase activity correlated with viral attenuation in vitro and in vivo and did not affect the ability of Lpro to block expression of type I interferon (IFN) and other IFN-stimulated genes. Moreover, overexpression of ISG15 resulted in the reduction of FMDV viral titers. Thus, our study highlights the potential use of Lpro mutants with modified deISGylase activity for development of live attenuated vaccine candidates, and ISG15 as a novel biotherapeutic against FMD.

Quantitative Proteomics by Amino Acid Labeling in Foot-and-Mouth Disease Virus (FMDV)-Infected Cells

2012 ◽  
Vol 12 (1) ◽  
pp. 363-377 ◽  
Author(s):  
Yu Ye ◽  
Guangrong Yan ◽  
Yongwen Luo ◽  
Tiezhu Tong ◽  
Xiangtao Liu ◽  
...  
Keyword(s):  
Amino Acid ◽  
Disease Virus ◽  
Quantitative Proteomics ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Mouth Disease Virus ◽  
Foot And Mouth ◽  
Infected Cells ◽  
Amino Acid Labeling

scholarly journals Predicting antigenic sites on the foot-and-mouth disease virus capsid of the South African Territories types using virus neutralization data

2011 ◽  
Vol 92 (10) ◽  
pp. 2297-2309 ◽  
Author(s):  
F. F. Maree ◽  
B. Blignaut ◽  
J. J. Esterhuysen ◽  
T. A. P. de Beer ◽  
J. Theron ◽  
...  
Keyword(s):  
South African ◽  
Disease Virus ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Sub Saharan Africa ◽  
Antigenic Sites ◽  
Mouth Disease Virus ◽  
Virus Serotype ◽  
Antigenic Properties ◽  
Foot And Mouth

Foot-and-mouth disease virus (FMDV) outer capsid proteins 1B, 1C and 1D contribute to the virus serotype distribution and antigenic variants that exist within each of the seven serotypes. This study presents phylogenetic, genetic and antigenic analyses of South African Territories (SAT) serotypes prevalent in sub-Saharan Africa. Here, we show that the high levels of genetic diversity in the P1-coding region within the SAT serotypes are reflected in the antigenic properties of these viruses and therefore have implications for the selection of vaccine strains that would provide the best vaccine match against emerging viruses. Interestingly, although SAT1 and SAT2 viruses displayed similar genetic variation within each serotype (32 % variable amino acids), antigenic disparity, as measured by r1-values, was less pronounced for SAT1 viruses compared with SAT2 viruses within our dataset, emphasizing the high antigenic variation within the SAT2 serotype. Furthermore, we combined amino acid variation and the r1-values with crystallographic structural data and were able to predict areas on the surface of the FMD virion as antigenically relevant. These sites were mostly consistent with antigenic sites previously determined for types A, O and C using mAbs and escape mutant studies. Our methodology offers a quick alternative to determine antigenic relevant sites for FMDV field strains.

Activation of Porcine Natural Killer Cells and Lysis of Foot-and-Mouth Disease Virus Infected Cells

2009 ◽  
Vol 29 (3) ◽  
pp. 179-192 ◽  
Author(s):  
Felix N. Toka ◽  
Charles K. Nfon ◽  
Harry Dawson ◽  
D. Mark Estes ◽  
William T. Golde
Keyword(s):  
Natural Killer Cells ◽  
Natural Killer ◽  
Disease Virus ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Killer Cells ◽  
Mouth Disease Virus ◽  
Foot And Mouth ◽  
Infected Cells

scholarly journals Foot-and-Mouth Disease Virus Lacking the VP1 G-H Loop: The Mutant Spectrum Uncovers Interactions among Antigenic Sites for Fitness Gain

Virology ◽  
2001 ◽  
Vol 288 (2) ◽  
pp. 192-202 ◽  
Author(s):  
Eric Baranowski ◽  
Carmen M. Ruiz-Jarabo ◽  
Filip Lim ◽  
Esteban Domingo
Keyword(s):  
Disease Virus ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Antigenic Sites ◽  
Mouth Disease Virus ◽  
Foot And Mouth ◽  
Mutant Spectrum

scholarly journals Use of in Situ Hybridization for the Detection of Foot-and-Mouth Disease Virus in Cell Culture

1989 ◽  
Vol 1 (4) ◽  
pp. 329-332 ◽  
Author(s):  
Richard F. Meyer ◽  
Corrie C. Brown ◽  
Thomas W. Molitor ◽  
Vikram N. Vakharia
Keyword(s):  
Disease Virus ◽  
Detection System ◽  
Cdna Probe ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Rna Probes ◽  
Mouth Disease Virus ◽  
Foot And Mouth ◽  
Infected Cells

Biotinylated complementary DNA (cDNA) and RNA probes were prepared from a specific and highly conserved section of the foot-and-mouth disease virus (FMDV) genome coding for the RNA-dependent RNA polymerase. Hybridization was conducted on FMDV-infected, bovine enterovirus (BEV)-infected, and noninfected swine kidney cell cultures. The detection system utilized the enzyme system streptavidin-alkaline phosphatase, the substrate phosphate, and the chromogen nitroblue tetrazolium. Intense cytoplasmic granular staining was present at 2 and 4 hr postinfection (hpi), with less staining observed at 24 hpi. The staining was specific for FMDV, as indicated by a lack of staining of noninfected cells and BEV-infected cells. With the RNA probe, positive cells were detected up to the highest viral dilution assayed, which was approximately 96 TCID50. The cDNA probe was slightly less sensitive, detecting positive cells at lo-fold lower dilutions. This technique could prove useful in the diagnosis of foot-and-mouth disease in animals or in the detection of FMDV in biologics submitted for importation.

scholarly journals Analysis of neutralizing antigenic sites on the surface of type A12 foot-and-mouth disease virus.

1989 ◽  
Vol 63 (5) ◽  
pp. 2143-2151 ◽  
Author(s):  
B Baxt ◽  
V Vakharia ◽  
D M Moore ◽  
A J Franke ◽  
D O Morgan
Keyword(s):  
Disease Virus ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Antigenic Sites ◽  
Mouth Disease Virus ◽  
Foot And Mouth

scholarly journals Mapping of antigenic sites of foot-and-mouth disease virus serotype Asia 1 and relationships with sites described in other serotypes

2013 ◽  
Vol 94 (3) ◽  
pp. 559-569 ◽  
Author(s):  
Santina Grazioli ◽  
Francesca Fallacara ◽  
Emiliana Brocchi
Keyword(s):  
Disease Virus ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Antigenic Structure ◽  
Antigenic Sites ◽  
Fmdv Serotype ◽  
Fmdv Serotypes ◽  
Mouth Disease Virus ◽  
Foot And Mouth ◽  
Serotype Asia 1

Knowledge of the antigenic structure of foot-and-mouth disease virus (FMDV) has relevance in the development of diagnostic assays, in the evaluation of the antigenic variability and in the selection of appropriate vaccine strains. Antigenic sites have been investigated only in FMDVs of serotypes O, A and C, while it would be valuable to extend studies also to other serotypes. This paper reports the identification of antigenic sites involved in virus neutralization in the FMDV serotype Asia 1 by using a new panel of mAbs and their relation with sites described in other serotypes is discussed. Out of 24 mAbs raised against the FMDV serotype Asia 1, 10 neutralize viral infectivity and were used to select FMDV mutants resistant to neutralization. On the basis of their reactivity profile with virus mutants, the 10 neutralizing mAbs were clustered in four groups corresponding to four independent antigenic sites. By comparing the amino acid sequence of the parental virus and of virus mutants, the amino acids crucial for the four sites were mapped at the following positions: VP1 140–142, VP2 67–79, VP3 58/59 and VP3 218. Three of the four neutralizing sites identified and mapped on FMDV serotype Asia 1 correspond structurally and functionally to analogous sites described in FMDV serotypes O, A and C, enforcing the evidence that these are dominant antigenic sites in the FMDV structure. The fourth site, located at the C terminus of VP3, is a new independent site, described for the first time in FMDV.

scholarly journals The Foot-and-Mouth Disease Virus cis-Acting Replication Element (cre) Can Be Complemented in trans within Infected Cells

2003 ◽  
Vol 77 (3) ◽  
pp. 2243-2246 ◽  
Author(s):  
Laurence Tiley ◽  
Andrew M. Q. King ◽  
Graham J. Belsham
Keyword(s):  
Disease Virus ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Temperature Sensitive ◽  
Stem Loop ◽  
Cis Acting ◽  
Stem Loop Structure ◽  
Mouth Disease Virus ◽  
Foot And Mouth ◽  
Infected Cells

ABSTRACT A temperature-sensitive (ts) mutation was identified within the 5′-untranslated region of foot-and-mouth disease virus (FMDV) RNA. The mutation destabilizes a stem-loop structure recently identified as a cis-acting replication element (cre). Genetic analyses indicated that the ts defect in virus replication could be complemented. Thus, the FMDV cre can function in trans. It is suggested that the cre be renamed a 3B-uridylylation site (bus).

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