Promoter analysis of an African Swine Fever Virus gene encoding a putative elongation factor

1995 ◽  
Vol 23 (1) ◽  
pp. 139S-139S ◽  
Author(s):  
PAULA R. YATES ◽  
LINDA K. DIXON ◽  
PHILIP. C. TURNER
Keyword(s):  
Promoter Analysis ◽  
African Swine Fever Virus ◽  
Elongation Factor ◽  
African Swine Fever ◽  
Fever Virus ◽  
Gene Encoding ◽  
Virus Gene

scholarly journals Structural comparisons of host and African swine fever virus dUTPases reveal new clues for inhibitor development

2020 ◽  
pp. jbc.RA120.014005
Author(s):  
Rui Liang ◽  
Gang Wang ◽  
Ding Zhang ◽  
Gang Ye ◽  
Mengxia Li ◽  
...  
Keyword(s):  
Active Sites ◽  
African Swine Fever Virus ◽  
African Swine Fever ◽  
Structural Diversity ◽  
Fever Virus ◽  
Gene Encoding ◽  
Inhibitor Development ◽  
Ligand Free ◽  
The Difference ◽  
Swine Diseases

African swine fever, caused by the African swine fever virus (ASFV), is among the most significant swine diseases. There are currently no effective treatments against ASFV. ASFV contains a gene encoding a dUTPase (E165R), which is required for viral replication in swine macrophages, making it an attractive target for inhibitor development. However, the full structural details of the ASFV dUTPase and those of the comparable swine enzyme are not available, limiting further insights. Herein, we determine the crystal structures of ASFV dUTPase and swine dUTPase in both their ligand-free and ligand-bound forms. We observe that the swine enzyme employs a classical dUTPase architecture made up of three-subunit active sites, whereas the ASFV enzyme employs a novel two-subunit active site. We then performed a comparative analysis of all dUTPase structures uploaded in PDB, which showed classic and non-classical types were mainly determined by the C-terminal β-strand orientation, and the difference was mainly related to the four amino acids behind motif IV. Thus, our study not only explains the reason for the structural diversity of dUTPase but also reveals how to predict dUTPase type, which may have implications for the dUTPase family. Finally, we tested two dUTPase inhibitors developed for the Plasmodium falciparum dUTPase against the swine and ASFV enzymes. One of these compounds inhibited the ASFV dUTPase at low micromolar concentrations (Kd=15.6μM) and with some selectivity (~2x) over swine dUTPase. In conclusion, our study expands our understanding of the dUTPase family and may aid in the development of specific ASFV inhibitors.

scholarly journals African swine fever virus gene j13L encodes a 25-27 kDa virion protein with variable numbers of amino acid repeats

1995 ◽  
Vol 76 (5) ◽  
pp. 1117-1127 ◽  
Author(s):  
H. Sun ◽  
S. C. Jacobs ◽  
G. L. Smith ◽  
L. K. Dixon ◽  
R. M. E. Parkhouse
Keyword(s):  
Amino Acid ◽  
African Swine Fever Virus ◽  
African Swine Fever ◽  
Fever Virus ◽  
Virion Protein ◽  
Virus Gene ◽  
Amino Acid Repeats

scholarly journals An African swine fever virus gene with similarity to the proto-oncogene bcl-2 and the Epstein-Barr virus gene BHRF1.

1993 ◽  
Vol 67 (7) ◽  
pp. 4391-4394 ◽  
Author(s):  
J G Neilan ◽  
Z Lu ◽  
C L Afonso ◽  
G F Kutish ◽  
M D Sussman ◽  
...  
Keyword(s):  
Epstein Barr Virus ◽  
African Swine Fever Virus ◽  
African Swine Fever ◽  
Fever Virus ◽  
Virus Gene ◽  
Barr Virus ◽  
Epstein Barr

scholarly journals An African swine fever virus gene with homology to DNA ligases

1992 ◽  
Vol 20 (11) ◽  
pp. 2667-2671 ◽  
Author(s):  
Jef M. Hammond ◽  
Shona M. Kerr ◽  
Geoffrey L. Smith ◽  
Linda K. Dixon
Keyword(s):  
African Swine Fever Virus ◽  
African Swine Fever ◽  
Fever Virus ◽  
Dna Ligases ◽  
Virus Gene

An African Swine Fever Virus Gene with Similarity to the T-Lymphocyte Surface Antigen CD2 Mediates Hemadsorption

Virology ◽  
1994 ◽  
Vol 199 (2) ◽  
pp. 463-468 ◽  
Author(s):  
M.V. Borca ◽  
G.F. Kutish ◽  
C.L. Afonso ◽  
P. Irusta ◽  
C. Carrillo ◽  
...  
Keyword(s):  
Surface Antigen ◽  
T Lymphocyte ◽  
African Swine Fever Virus ◽  
African Swine Fever ◽  
Fever Virus ◽  
Virus Gene ◽  
Lymphocyte Surface

scholarly journals Functionality and Cell Anchorage Dependence of the African Swine Fever Virus Gene A179L, a Viralbcl-2 Homolog, in Insect Cells

1998 ◽  
Vol 72 (12) ◽  
pp. 10227-10233 ◽  
Author(s):  
Alejandro Brun ◽  
Fernando Rodríguez ◽  
José M. Escribano ◽  
Covadonga Alonso
Keyword(s):  
Cell Survival ◽  
Intracellular Signaling ◽  
Insect Cells ◽  
African Swine Fever Virus ◽  
African Swine Fever ◽  
Fever Virus ◽  
Virus Gene ◽  
Mammalian Cell Lines ◽  
Extracellular Matrix Components ◽  
Baculovirus Infection

ABSTRACT The African swine fever virus gene A179L has been shown to be a functional member of the ced9/bcl-2 family of apoptosis inhibitors in mammalian cell lines. In this work we have expressed the A179L gene product (p21) under the control of the baculovirus polyhedrin promoter using a baculovirus system. Expression of the A179L gene neither altered the baculovirus replication phenotype nor delayed the shutoff of cellular protein synthesis, but it extended the survival of the infected insect cells to very late times postinfection. The increase in cell survival rates correlated with a marked apoptosis reduction after baculovirus infection. Interestingly, prevention of apoptosis was observed when recombinant baculovirus infections were carried out in monolayer cell cultures but not when cells were infected in suspension, suggesting a cell anchorage dependence for p21 function in insect cells. Cell survival was enhanced under optimal conditions of cell attachment and cell-to-cell contact as provided by extracellular matrix components or poly-d-lysine. Since it was observed that cytoskeleton organization varied depending on culture conditions of insect cells (grown in monolayer versus grown in suspension), these results suggested that A179L might regulate apoptosis in insect cells only when the cytoskeletal support of intracellular signaling is maintained upon cell adhesion. Thus, cell shape and cytoskeleton status might allow variations in intracellular transduction of signals related to cell survival in virus-infected cells.

scholarly journals An African swine fever virus gene with a similarity to eukaryotic RNA polymerase subunit 6

1993 ◽  
Vol 21 (12) ◽  
pp. 2940-2940 ◽  
Author(s):  
Z. Lu ◽  
G.F. Kutish ◽  
M.D. Sussman ◽  
D.L. Rock
Keyword(s):  
Rna Polymerase ◽  
African Swine Fever Virus ◽  
African Swine Fever ◽  
Fever Virus ◽  
Virus Gene

scholarly journals Inducible Gene Expression from African Swine Fever Virus Recombinants: Analysis of the Major Capsid Protein p72

1998 ◽  
Vol 72 (4) ◽  
pp. 3185-3195 ◽  
Author(s):  
Ramón García-Escudero ◽  
Germán Andrés ◽  
Fernando Almazán ◽  
Eladio Viñuela
Keyword(s):  
Capsid Protein ◽  
Major Capsid Protein ◽  
African Swine Fever Virus ◽  
Expression System ◽  
African Swine Fever ◽  
Firefly Luciferase ◽  
Fever Virus ◽  
Gene Encoding ◽  
Iptg Induction ◽  
Dense Membrane

ABSTRACT A method to study the function of individual African swine fever virus (ASFV) gene products utilizing the Escherichia coli lac repressor-operator system has been developed. Recombinant viruses containing both the lacI gene encoding thelac repressor and a strong virus late promoter modified by the insertion of one or two copies of the lac operator sequence at various positions were constructed. The ability of each modified promoter to regulate expression of the firefly luciferase gene was assayed in the presence and in the absence of the inducer isopropyl β-d-thiogalactoside (IPTG). Induction and repression of gene activity were dependent on the position(s) of the operator(s) with respect to the promoter and on the number of operators inserted. The ability of this system to regulate the expression of ASFV genes was analyzed by constructing a recombinant virus inducibly expressing the major capsid protein p72. Electron microscopy analysis revealed that under nonpermissive conditions, electron-dense membrane-like structures accumulated in the viral factories and capsid formation was inhibited. Induction of p72 expression allowed the progressive building of the capsid on these structures, leading to assembly of ASFV particles. The results of this report demonstrate that the transferred inducible expression system is a powerful tool for analyzing the function of ASFV genes.

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