Structural studies on chimeric Sesbania mosaic virus coat protein: Revisiting SeMV assembly

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. N Delta 65-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 N Delta 65-B VLPs, suggesting possible biotechnological applications. These studies illustrate the importance of N-terminal residues, metal ions and robustness of the assembly process. (C) 2015 Elsevier Inc. All rights reserved.

Counting zero kernel pairs over a finite field

Helmke et al. have recently given a formula for the number of reachable pairs of matrices over a finite field. We give a new and elementary proof of the same formula by solving the equivalent problem of determining the number of so called zero kernel pairs over a finite field. We show that the problem is, equivalent to certain other enumeration problems and outline a connection with some recent results of Guo and Yang on the natural density of rectangular unimodular matrices over F-qx]. We also propose a new conjecture on the density of unimodular matrix polynomials. (C) 2016 Elsevier Inc. All rights reserved.