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The human pathogen mumps virus, like all paramyxoviruses, encodes a polymerase responsible for virally directed RNA synthesis. The template for the polymerase is the nucleocapsid, a filamentous protein-RNA complex harbouring the viral genome. Interaction of the polymerase and the nucleocapsid is mediated by a small domain tethered to the end of the P protein, one of the polymerase subunits. We report the X-ray crystal structure of this region of mumps virus P (the nucleocapsid binding domain, or NBD, amino acids 343-391). The mumps P NBD forms a compact bundle of three α-helices within the crystal, a fold apparently conserved across the Paramyxovirinae. In solution, however, the domain exists in the molten globule state. This is demonstrated through application of differential scanning calorimetry, circular dichroism spectroscopy, NMR spectroscopy, and dynamic light scattering. While the mumps P NBD is compact, and has persistent secondary structure, it lacks a well-defined tertiary structure under normal solution conditions. It can, however, be induced to fold by addition of a stabilizing methylamine cosolute. The domain provides a rare example of a molten globule that can be crystallized. The structure that is stabilized in the crystal represents the fully folded state of the domain, which must be transiently realized during binding to the viral nucleocapsid. While the intermolecular forces that govern the polymerase-nucleocapsid interaction appear to be different in measles, mumps and Sendai viruses, for each of these viruses, polymerase translocation involves the coupled binding and folding of protein domains. In all cases we suggest this will result in a weak-affinity protein complex with a short lifetime, which allows the polymerase to take rapid steps forward.
Rubulavirus, X-ray crystallography, Molten globule, TMAO
Structure of the nucleocapsid-binding domain from the mumps virus polymerase; An example of protein folding induced by crystallization
Richard L. Kingston,1,* Leslie S. Gay,2 Walter S. Baase,2 and Brian W. Matthews2
2009 Jun 9
In a mature and infectious retroviral particle, the capsid protein (CA) forms a shell surrounding the genomic RNA and the replicative machinery of the virus. The irregular nature of this capsid shell precludes direct atomic resolution structural analysis. CA hexamers and pentamers are the fundamental building blocks of the capsid, however the pentameric state, in particular, remains poorly characterized. We have developed an efficient in vitro protocol for studying the assembly of Rous sarcoma virus (RSV) CA that involves mild acidification and produces structures modeling the authentic viral capsid. These structures include regular spherical particles with T = 1 icosahedral symmetry, built from CA pentamers alone. These particles were subject to cryoelectron microscopy (cryo-EM) and image processing, and a pseudo-atomic model of the icosahedron was created by docking atomic structures of the constituent CA domains into the cryo-EM-derived three-dimensional density map. The N-terminal domain (NTD) of CA forms pentameric turrets, which decorate the surface of the icosahedron, while the C-terminal domain (CTD) of CA is positioned underneath, linking the pentamers. Biophysical analysis of the icosahedral particle preparation reveals that CA monomers and icosahedra are the only detectable species and that these exist in reversible equilibrium at pH 5. These same acidic conditions are known to promote formation of a RSV CA CTD dimer, present within the icosahedral particle, which facilitates capsid assembly. The results are consistent with a model in which RSV CA assembly is a nucleation-limited process driven by very weak protein-protein interactions.
Biophysics, Electron Microscopy (EM), Protein Self-assembly, Retrovirus, Virus Assembly, Capsid Protein, Rous Sarcoma Virus
Proton-driven Assembly of the Rous Sarcoma Virus Capsid Protein Results in the Formation of Icosahedral Particles
Jae-Kyung Hyun,1 Mazdak Radjainia, Richard L. Kingston,2 and Alok K. Mitra3
2010 May 14
The propagule pressure hypothesis asserts that the number of individuals released is the key determinant of whether an introduction will succeed or not. It remains to be shown whether propagule pressure is more important than either species-level or site-level factors in determining the fate of an introduction. Studies claiming to show that propagule pressure is the primary determinant of introduction success must assume that the historical record as reported by secondary sources is complete and accurate. Here, examine a widely introduced game bird, the Chukar (Alectoris chukar), to the USA. We compare the records reported by two secondary sources (Long, 1981; Lever, 1987) to those in a primary source (Christensen, 1970) and to a recent study by Sol et al. (2012). Numerous inconsistencies exist in the records reported by Sol et al. (2012), Long (1981) and Lever (1987) when compared to the primary record of Christensen (1970). As reported by Christensen (1970), very large numbers of Chukars were released unsuccessfully in some states. Our results strongly imply that factors other than sheer numbers are more important. Site-to-site differences are the most likely explanation for the variation in success.
Chukar Partridge, Alectoris chukar, Propagule pressure, Introduced birds
Inconsistencies among secondary sources of Chukar Partridge (Alectoris chukar) introductions to the United States
Michael P. Moulton,corresponding author1 Wendell P. Cropper, Jr,2 and Andrew J. Broz1