3p0s

Publication Abstract from PubMed

Bombyx mori densovirus 1 (BmDNV-1), a major pathogen of silk worms, causes significant losses to the silk industry. The structure of recombinant BmDNV-1 virus-like particle has been determined to 3.1 A resolution using X-ray crystallography. It is the first near-atomic resolution structure of a virus-like particle within the genus Iteravirus. The particles consist of 60 copies of the 55 kDa VP3 coat protein. The capsid protein has a beta-barrel "jelly roll" fold similar to that found in many diverse icosahedral viruses including archaea, bacterial, plant and animal viruses as well as other parvoviruses. Most of the surface loops have little structural resemblance to other known parvoviral capsid proteins. In contrast to vertebrate parvoviruses, the N-terminal beta-strand of the BmDNV-1 VP3 is positioned relative to the neighboring twofold related subunit in a "domain swapped" conformation, similar to other invertebrate parvoviruses, suggesting domain-swapping is an evolutionary conserved structural feature of the Densovirinae.

Structure of Bombyx mori Densovirus 1, a Silkworm Pathogen.,Kaufmann B, El-Far M, Plevka P, Bowman VD, Li Y, Tijssen P, Rossmann MG J Virol. 2011 Mar 2. PMID:21367906^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.