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Publication Abstract from PubMed

The capsid protein (CP) of Sesbania mosaic virus (SeMV, a T=3 plant virus) consists of a disordered N-terminal R-domain and an ordered S-domain. Removal of the R-domain results in the formation of T=1 particles. In the current study, the R-domain was replaced with unrelated polypeptides of similar lengths: the B-domain of Staphylococcus aureus SpA, and SeMV encoded polypeptides P8 and P10. The chimeric proteins contained T=3 or larger virus-like particles (VLPs) and could not be crystallized. The presence of metal ions during purification resulted in a large number of heterogeneous nucleoprotein complexes. N65-B (R domain replaced with B domain) could also be purified in a dimeric form. Its crystal structure revealed T=1 particles devoid of metal ions and the B-domain was disordered. However, the B-domain was functional in N65-B VLPs, suggesting possible biotechnological applications. These studies illustrate the importance of N-terminal residues, metal ions and robustness of the assembly process.

Structural studies on chimeric Sesbania mosaic virus coat protein: Revisiting SeMV assembly.,Gulati A, Murthy A, Abraham A, Mohan K, Natraj U, Savithri HS, Murthy MR Virology. 2015 Dec 17;489:34-43. doi: 10.1016/j.virol.2015.11.029. PMID:26704627^[1]

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