Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
3429412 | Virus Research | 2010 | 5 Pages |
Abstract
Protein A33 is a type II membrane protein present in the outer envelope of extracellular as well as cell-associated Vaccinia virus particles. A33 has been implicated in mediating cell-to-cell virus spread in an antibody-resistant manner. Here, using state-of-the-art structure prediction methods and structural modeling, we show that A33 has most likely evolved from a C-type lectin-like protein. Comparison of the three-dimensional A33 model to the X-ray structures of distant cellular homologues revealed that A33 retained the key residues required for adopting the C-type lectin-like fold. Our results provide insights into the structure and origin of protein A33.
Keywords
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Immunology and Microbiology
Virology
Authors
Mart Krupovič, Virginija Cvirkaitė-Krupovič, Dennis H. Bamford,