scholarly journals Expansion of host-cell tropism of foot-and-mouth disease virus despite replication in a constant environment

2004 ◽  
Vol 85 (8) ◽  
pp. 2289-2297 ◽  
Author(s):  
Carmen M. Ruiz-Jarabo ◽  
Nonia Pariente ◽  
Eric Baranowski ◽  
Mercedes Dávila ◽  
Gema Gómez-Mariano ◽  
...  
Keyword(s):  
Host Cell ◽  
Disease Virus ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Jurkat Cells ◽  
Virus Infectivity ◽  
Cell Tropism ◽  
Cellular Environment ◽  
Mouth Disease Virus ◽  
Foot And Mouth

Foot-and-mouth disease virus (FMDV) variants adapted to BHK-21 cells showed an expanded host-cell tropism that extended to primate and human cell lines. Virus replication in human HeLa and Jurkat cells has been documented by titration of virus infectivity, quantification of virus RNA, expression of a virus-specific non-structural antigen, and serial passage of virus in the cells. Parallel serial infections of human Jurkat cells with the same variant FMDVs indicates a strong stochastic component in the progression of infection. Chimeric viruses identified the capsid as a genomic region involved in tropism expansion. These results indicate that, contrary to theoretical predictions, replication of an RNA virus in a constant cellular environment may lead to expansion of cellular tropism, rather than to a more specialized infection of the cellular type to which the virus has been adapted.

scholarly journals Perturbations in the surface structure of A22 Iraq foot-and-mouth disease virus accompanying coupled changes in host cell specificity and antigenicity

Structure ◽  
1996 ◽  
Vol 4 (2) ◽  
pp. 135-145 ◽  
Author(s):  
Stephen Curry ◽  
Elizabeth Fry ◽  
Wendy Blakemore ◽  
Robin Abu Ghazaleh ◽  
Terry Jackson ◽  
...  
Keyword(s):  
Surface Structure ◽  
Host Cell ◽  
Disease Virus ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Cell Specificity ◽  
Mouth Disease Virus ◽  
Foot And Mouth

scholarly journals Host Cell Selection of Antigenic Variants of Foot-and-Mouth Disease Virus

1989 ◽  
Vol 70 (1) ◽  
pp. 45-57 ◽  
Author(s):  
C. Bolwell ◽  
A. L. Brown ◽  
P. V. Barnett ◽  
R. O. Campbell ◽  
B. E. Clarke ◽  
...  
Keyword(s):  
Host Cell ◽  
Disease Virus ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Cell Selection ◽  
Mouth Disease Virus ◽  
Foot And Mouth ◽  
Selection Of

scholarly journals Exploring IRES Region Accessibility by Interference of Foot-and-Mouth Disease Virus Infectivity

PLoS ONE ◽  
2012 ◽  
Vol 7 (7) ◽  
pp. e41382 ◽  
Author(s):  
Teodoro Fajardo ◽  
Maria Flora Rosas ◽  
Francisco Sobrino ◽  
Encarnacion Martinez-Salas
Keyword(s):  
Disease Virus ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Virus Infectivity ◽  
Mouth Disease Virus ◽  
Foot And Mouth

scholarly journals Foot-and-mouth disease virus protease 3C induces specific proteolytic cleavage of host cell histone H3.

1990 ◽  
Vol 64 (2) ◽  
pp. 748-756 ◽  
Author(s):  
M M Falk ◽  
P R Grigera ◽  
I E Bergmann ◽  
A Zibert ◽  
G Multhaup ◽  
...  
Keyword(s):  
Host Cell ◽  
Disease Virus ◽  
Histone H3 ◽  
Foot And Mouth Disease ◽  
Proteolytic Cleavage ◽  
Mouth Disease ◽  
Mouth Disease Virus ◽  
Foot And Mouth

scholarly journals Thermostability of the Foot-and-Mouth Disease Virus Capsid Is Modulated by Lethal and Viability-Restoring Compensatory Amino Acid Substitutions

2019 ◽  
Vol 93 (10) ◽  
Author(s):  
Silvia López-Argüello ◽  
Verónica Rincón ◽  
Alicia Rodríguez-Huete ◽  
Encarnación Martínez-Salas ◽  
Graham J. Belsham ◽  
...  
Keyword(s):  
Amino Acid ◽  
Disease Virus ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Virus Infectivity ◽  
Side Chains ◽  
Mouth Disease Virus ◽  
Foot And Mouth ◽  
Capsid Stability ◽  
The Relationship

ABSTRACTInfection by viruses depends on a balance between capsid stability and dynamics. This study investigated biologically and biotechnologically relevant aspects of the relationship in foot-and-mouth disease virus (FMDV) between capsid structure and thermostability and between thermostability and infectivity. In the FMDV capsid, a substantial number of amino acid side chains at the interfaces between pentameric subunits are charged at neutral pH. Here a mutational analysis revealed that the essential role for virus infection of most of the 8 tested charged groups is not related to substantial changes in capsid protein expression or processing or in capsid assembly or stability against a thermally induced dissociation into pentamers. However, the positively charged side chains of R2018 and H3141, located at the interpentamer interfaces close to the capsid 2-fold symmetry axes, were found to be critical both for virus infectivity and for keeping the capsid in a state of weak thermostability. A charge-restoring substitution (N2019H) that was repeatedly fixed during amplification of viral genomes carrying deleterious mutations reverted both the lethal and capsid-stabilizing effects of the substitution H3141A, leading to a double mutant virus with close to normal infectivity and thermolability. H3141A and other thermostabilizing substitutions had no detectable effect on capsid resistance to acid-induced dissociation into pentamers. The results suggest that FMDV infectivity requires limited local stability around the 2-fold axes at the interpentamer interfaces of the capsid. The implications for the mechanism of genome uncoating in FMDV and the development of thermostabilized vaccines against foot-and-mouth disease are discussed.IMPORTANCEThis study provides novel insights into the little-known structural determinants of the balance between thermal stability and instability in the capsid of foot-and-mouth disease virus and into the relationship between capsid stability and virus infectivity. The results provide new guidelines for the development of thermostabilized empty capsid-based recombinant vaccines against foot-and-mouth disease, one of the economically most important animal diseases worldwide.

scholarly journals Rapid Selection in Modified BHK-21 Cells of a Foot-and-Mouth Disease Virus Variant Showing Alterations in Cell Tropism

1998 ◽  
Vol 72 (12) ◽  
pp. 10171-10179 ◽  
Author(s):  
Cristina Escarmís ◽  
Elisa C. Carrillo ◽  
Marcela Ferrer ◽  
Juan F. García Arriaza ◽  
Nora Lopez ◽  
...  
Keyword(s):  
Amino Acid ◽  
Disease Virus ◽  
Chinese Hamster ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Single Infection ◽  
Cell Tropism ◽  
Nucleotide Substitutions ◽  
Mouth Disease Virus ◽  
Foot And Mouth

ABSTRACT With persistent foot-and-mouth disease virus (FMDV) in BHK-21 cells, there is coevolution of the cells and the resident virus; the virulence of the virus for the parental BHK-21 cells is gradually increased, and the cells become partially resistant to FMDV. Here we report that variants of FMDV C3Arg/85 were selected in a single infection of partially resistant BHK-21 cells (termed BHK-Rb cells). Indirect immunofluorescence showed that the BHK-Rb cell population was heterogeneous with regard to susceptibility to C3Arg/85 infection. Infection of BHK-Rb cells with C3Arg/85 resulted in an early phase of partial cytopathology which was followed at 6 to 10 days postinfection by the shedding of mutant FMDVs, termed C3-Rb. The selected C3-Rb variants showed increased virulence for BHK-21 cells, were able to overcome the resistance of modified BHK-21 cells to infection, and had acquired the ability to bind heparin and to infect wild-type Chinese hamster ovary (CHO) cells. A comparison of the genomic sequences of the parental and modified viruses revealed only two amino acid differences, located at the surface of the particle, at the fivefold axis of the viral capsid (Asp-9→Ala in VP3 and either Gly-110→Arg or His-108→Arg in VP1). The same phenotypic and genotypic modifications occurred in a highly reproducible manner; they were seen in a number of independent infections of BHK-Rb cells with viral preparation C3Arg/85 or with clones derived from it. Neither amino acid substitutions in other structural or nonstructural proteins nor nucleotide substitutions in regulatory regions were found. These results prove that infection of partially permissive cells can promote the rapid selection of virus variants that show alterations in cell tropism and are highly virulent for the same cells.

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