Mapping and sequence of the gene encoding protein p37, A major structural protein of African swine fever virus

Virus Genes ◽  
1988 ◽  
Vol 1 (3) ◽  
pp. 291-303 ◽  
Author(s):  
C. L�pez-Ot�n ◽  
C. Sim�n ◽  
E. M�ndez ◽  
E. Vi�uela
Keyword(s):  
African Swine Fever Virus ◽  
African Swine Fever ◽  
Fever Virus ◽  
Structural Protein ◽  
Gene Encoding ◽  
Major Structural Protein ◽  
Encoding Protein

scholarly journals Mapping and Sequence of the Gene Encoding Protein pl7, a Major African Swine Fever Virus Structural Protein

Virology ◽  
1995 ◽  
Vol 206 (2) ◽  
pp. 1140-1144 ◽  
Author(s):  
Carmen Simón-Mateo ◽  
Jose Maria P. Freue ◽  
German Andrés ◽  
Carlos López-Otin ◽  
Eladio Viñuela
Keyword(s):  
African Swine Fever Virus ◽  
African Swine Fever ◽  
Fever Virus ◽  
Structural Protein ◽  
Gene Encoding ◽  
Encoding Protein

scholarly journals The Major Structural Protein of African Swine Fever Virus, p73, Is Packaged into Large Structures, Indicative of Viral Capsid or Matrix Precursors, on the Endoplasmic Reticulum

1998 ◽  
Vol 72 (6) ◽  
pp. 5215-5223 ◽  
Author(s):  
Christian Cobbold ◽  
Thomas Wileman
Keyword(s):  
Endoplasmic Reticulum ◽  
Complex Formation ◽  
Inner Core ◽  
African Swine Fever Virus ◽  
African Swine Fever ◽  
Fever Virus ◽  
In Vitro Translation ◽  
Structural Protein ◽  
Major Structural Protein ◽  
Outer Capsid

ABSTRACT African swine fever virus (ASFV) is a large enveloped DNA virus that shares the striking icosahedral symmetry of iridoviruses. To understand the mechanism of assembly of ASFV, we have been studying the biosynthesis and subcellular distribution of p73, the major structural protein of ASFV. Sucrose density sedimentation of lysates prepared from infected cells showed that newly synthesized p73 was incorporated into a complex with a size of 150 to 250 kDa. p73 synthesized by in vitro translation migrated at 70 kDa, suggesting that cellular and/or viral proteins are required for the formation of the 150- to 250-kDa complex. During a 2-h chase, approximately 50% of the newly synthesized pool of p73 bound to the endoplasmic reticulum (ER). During this period, the membrane-bound pool of p73, but not the cytosolic pool, formed large complexes of approximately 50,000 kDa. The complexes were formed via assembly intermediates, and the entire membrane-associated pool of p73 was incorporated into the 50,000-kDa complex within 2 h. The 50,000-kDa complexes containing p73 were also detected in virions secreted from cells. Immunoprecipitation of sucrose gradients with sera taken from hyperimmune pigs suggested that p73 was the major component of the 50,000-kDa complex. It is possible, therefore, that the complex contains between 600 and 700 copies of p73. The kinetics of complex formation and envelopment of p73 were similar, and complex formation and envelopment were both reversibly inhibited by cycloheximide, suggesting a functional link between complex assembly and ASFV envelopment. A protease protection assay detected 50,000-kDa complexes on the inside and outside of the membranes forming the viral envelope. The identification of a complex containing p73 beneath the envelope of ASFV suggests that p73 may be a component of the inner core shell or matrix of ASFV. The outer pool may represent p73 within the outer capsid layer of the virus. In summary, the data suggest that the assembly of the inner core matrix and outer capsid of ASFV takes place on the ER membrane during envelopment and that these structures are not preassembled in the cytosol.

scholarly journals African Swine Fever Virus pB119L Protein Is a Flavin Adenine Dinucleotide-Linked Sulfhydryl Oxidase

2006 ◽  
Vol 80 (7) ◽  
pp. 3157-3166 ◽  
Author(s):  
Irene Rodríguez ◽  
Modesto Redrejo-Rodríguez ◽  
Javier M. Rodríguez ◽  
Alí Alejo ◽  
José Salas ◽  
...  
Keyword(s):  
Disulfide Bonds ◽  
Flavin Adenine Dinucleotide ◽  
Virus Assembly ◽  
Nonstructural Protein ◽  
African Swine Fever Virus ◽  
African Swine Fever ◽  
Fever Virus ◽  
Structural Protein ◽  
Sulfhydryl Oxidase ◽  
Infected Cells

ABSTRACT Protein pB119L of African swine fever virus belongs to the Erv1p/Alrp family of sulfhydryl oxidases and has been described as a late nonstructural protein required for correct virus assembly. To further our knowledge of the function of protein pB119L during the virus life cycle, we have investigated whether this protein possesses sulfhydryl oxidase activity, using a purified recombinant protein. We show that the purified protein contains bound flavin adenine dinucleotide and is capable of catalyzing the formation of disulfide bonds both in a protein substrate and in the small molecule dithiothreitol, the catalytic activity being comparable to that of the Erv1p protein. Furthermore, protein pB119L contains the cysteines of its active-site motif CXXC, predominantly in an oxidized state, and forms noncovalently bound dimers in infected cells. We also show in coimmunoprecipitation experiments that protein pB119L interacts with the viral protein pA151R, which contains a CXXC motif similar to that present in thioredoxins. Protein pA151R, in turn, was found to interact with the viral structural protein pE248R, which contains disulfide bridges and belongs to a class of myristoylated proteins related to vaccinia virus L1R, one of the substrates of the redox pathway encoded by this virus. These results suggest the existence in African swine fever virus of a system for the formation of disulfide bonds constituted at least by proteins pB119L and pA151R and identify protein pE248R as a possible final substrate of this pathway.

scholarly journals African Swine Fever Virus Structural Protein pE120R Is Essential for Virus Transport from Assembly Sites to Plasma Membrane but Not for Infectivity

2001 ◽  
Vol 75 (15) ◽  
pp. 6758-6768 ◽  
Author(s):  
Germán Andrés ◽  
Ramón Garcı́a-Escudero ◽  
Eladio Viñuela ◽  
Marı́a L. Salas ◽  
Javier M. Rodrı́guez
Keyword(s):  
Plasma Membrane ◽  
African Swine Fever Virus ◽  
Growth Curves ◽  
African Swine Fever ◽  
Fever Virus ◽  
Virus Yield ◽  
Virus Infectivity ◽  
Structural Protein ◽  
Virus Growth ◽  
Extracellular Virus

ABSTRACT This report examines the role of African swine fever virus (ASFV) structural protein pE120R in virus replication. Immunoelectron microscopy revealed that protein pE120R localizes at the surface of the intracellular virions. Consistent with this, coimmunoprecipitation assays showed that protein pE120R binds to the major capsid protein p72. Moreover, it was found that, in cells infected with an ASFV recombinant that inducibly expresses protein p72, the incorporation of pE120R into the virus particle is dependent on p72 expression. Protein pE120R was also studied using an ASFV recombinant in which E120R gene expression is regulated by the Escherichia coli lacrepressor-operator system. In the absence of inducer, pE120R expression was reduced about 100-fold compared to that obtained with the parental virus or the recombinant virus grown under permissive conditions. One-step virus growth curves showed that, under conditions that repress pE120R expression, the titer of intracellular progeny was similar to the total virus yield obtained under permissive conditions, whereas the extracellular virus yield was about 100-fold lower than in control infections. Immunofluorescence and electron microscopy demonstrated that, under restrictive conditions, intracellular mature virions are properly assembled but remain confined to the replication areas. Altogether, these results indicate that pE120R is necessary for virus dissemination but not for virus infectivity. The data also suggest that protein pE120R might be involved in the microtubule-mediated transport of ASFV particles from the viral factories to the plasma membrane.

scholarly journals Characterization of the African Swine Fever Virus Structural Protein p14.5: A DNA Binding Protein

Virology ◽  
1997 ◽  
Vol 229 (1) ◽  
pp. 201-211 ◽  
Author(s):  
Luisa Martinez-Pomares ◽  
Carmen Simon-Mateo ◽  
Carlos Lopez-Otin ◽  
Eladio Viñuela
Keyword(s):  
Dna Binding ◽  
African Swine Fever Virus ◽  
Binding Protein ◽  
African Swine Fever ◽  
Dna Binding Protein ◽  
Fever Virus ◽  
Structural Protein

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
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