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The Tanapoxvirus is a human, disease-causing virus for which little structural data about the proteome has been gathered. Using bioinformatics, several predictions were made about the structure and function of each of the 156 proteins that are expressed from the Tanapoxvirus genome. Predictions were made based upon the amino acid sequences of the proteins and their impact on folding the molecule into a well-defined structure, and based on the homology or similarity of a protein’s sequence to that of another protein. PHYRE and BLAST programs predicted which Tanapoxvirus protein structures are known, which can be confidently assigned a structure, and which have unknown structures. The data gathered has guided, and will continue to guide structural studies of the Tanapoxvirus proteome in Dr. Szymczyna’s laboratory.
One identified protein, 57L, was predicted to be a virion core protein, which is responsible for the assembly and maturation of viral progeny in host cells. The 57L gene sequence was isolated from the virus’ genome using recombinant technology and expressed with hopes of determining its structure and mechanism of function. Structural data from this protein could lead to a better understanding of the virus assembly and maturation. Such data could even lead to the design of antivirals that could halt the replication cycle of poxviruses.
Archer, Ethan, "Structure and Function Studies of Tanapoxvirus Proteins, With a Focus on 57L" (2016). Honors Theses. 2668.