A newest report says that African swine fever, a highly contagious hemorrhagic disease of pigs, has broken out in Chernihiv region, putting at risk large pig populations.
 
African swine fever, which is caused by the African swine fever virus (ASFV), is a deadly disease affecting pigs. Currently, there is no published treatment or vaccine for the disease. Mortality rates may be as high as 100%. But it is an economically important disease that it is becoming a threat to the swine industry worldwide.

Now a team consisting of researchers from Fudan University and Georgia State University have found that a protein of ASFV has a unique structure that has not been seen in related proteins in other organisms. The unique structure may be a new target for the prevention and treatment of ASF.

Jianhua Gan, who led the study, and the team focused on an enzyme that helps synthesize DNA, the ASFV DNA Polymerase X (AsfvPolX). AsfvPolX plays a role in the DNA repair process of the ASFV virus genome. Viral replication is partially dependent on the function of AsfvPolX. A better understanding of how AsfvPolX works may help design drugs to combat the virus. Now, in their paper in PLoS Biology, Gan and colleagues described the structure of the enzyme in detail.

The researchers discovered that unlike the homologous proteins, AsfvPolX has several unique structural features including a 5'-P binding pocket, a His115-Arg127 platform, and hydrophobic residues Val120 and Leu123, which can all influence the function of the enzyem. The most important feature is a special binding pocket. Blocking the binding pocket with therapeutics may inhibit AsfvPolX activity and thus impair the DNA repair process of the viral genome, the researchers assumed. Collectively, the study provide a molecule basis for the design and development of new drugs against ASFV.

ASFV is a large, enveloped, double-stranded DNA virus and is the only member of the Asfarviridae family. The virus does not affect humans. ASFV DNA Polymerase X (AsfvPolX) is the most distinctive DNA polymerase identified to date. Now this study offers new insights into the structure of the enzyme, providing information for rational drug design to help combat ASFV in the future. Besides, CusAb offers AsfvPolX related proteins and other products such as Recombinant CD9.

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