Understanding the Folding Mediated Assembly of the Bacteriophage MS2 Coat Protein Dimers

2021 ◽  
Author(s):  
Digvijay Lalwani Prakash ◽  
Shachi Gosavi
Keyword(s):  
Coat Protein ◽  
Bacteriophage Ms2 ◽  
Protein Dimers

scholarly journals RNA Packing Specificity and Folding during Assembly of the Bacteriophage MS2

2008 ◽  
Vol 9 (3-4) ◽  
pp. 339-349 ◽  
Author(s):  
Ottar Rolfsson ◽  
Katerina Toropova ◽  
Victoria Morton ◽  
Simona Francese ◽  
Gabriella Basnak ◽  
...  
Keyword(s):  
Rna Structure ◽  
3D Structure ◽  
Viral Assembly ◽  
Genomic Rna ◽  
Stem Loop ◽  
Bacteriophage Ms2 ◽  
Protein Dimers ◽  
Phage Capsid ◽  
Type Phage ◽  
Viral Genomic Rna

Using a combination of biochemistry, mass spectrometry, NMR spectroscopy and cryo-electron microscopy (cryo-EM), we have been able to show that quasi-equivalent conformer switching in the coat protein (CP) of an RNA bacteriophage (MS2) is controlled by a sequence-specific RNA–protein interaction. The RNA component of this complex is an RNA stem-loop encompassing just 19 nts from the phage genomic RNA, which is 3569 nts in length. This binding results in the conversion of a CP dimer from a symmetrical conformation to an asymmetric one. Only when both symmetrical and asymmetrical dimers are present in solution is assembly of theT = 3 phage capsid efficient. This implies that the conformers, we have characterized by NMR correspond to the two distinct quasi-equivalent conformers seen in the 3D structure of the virion. An icosahedrally-averaged single particle cryo-EM reconstruction of the wild-type phage (to ∼9 Å resolution) has revealed icosahedrally ordered density encompassing up to 90% of the single-stranded RNA genome. The RNA is seen with a novel arrangement of two concentric shells, with connections between them along the 5-fold symmetry axes. RNA in the outer shell interacts with each of the 90 CP dimers in theT = 3 capsid and although the density is icosahedrally averaged, there appears to be a different average contact at the different quasi-equivalent protein dimers: precisely the result that would be expected if protein conformer switching is RNA-mediated throughout the assembly pathway. This unprecedented RNA structure provides new constraints for models of viral assembly and we describe experiments aimed at probing these. Together, these results suggest that viral genomic RNA folding is an important factor in efficient assembly, and further suggest that RNAs that could sequester viral CPs but not fold appropriately could act as potent inhibitors of viral assembly.

scholarly journals Correction to A Selection for Assembly Reveals That a Single Amino Acid Mutant of the Bacteriophage MS2 Coat Protein Forms a Smaller Virus-like Particle

Nano Letters ◽  
2016 ◽  
Vol 16 (12) ◽  
pp. 8034-8034 ◽  
Author(s):  
Michael A. Asensio ◽  
Norma M. Morella ◽  
Christopher M. Jakobson ◽  
Emily C. Hartman ◽  
Jeff E. Glasgow ◽  
...  
Keyword(s):  
Amino Acid ◽  
Coat Protein ◽  
Single Amino Acid ◽  
Bacteriophage Ms2 ◽  
Virus Like Particle ◽  
Selection For

Complexes of alfalfa mosaic virus RNA 4 with one and three coat protein dimers

Biochemistry ◽  
1980 ◽  
Vol 19 (23) ◽  
pp. 5255-5260 ◽  
Author(s):  
Corrie J. Houwing ◽  
E. M. J. Jaspars
Keyword(s):  
Coat Protein ◽  
Mosaic Virus ◽  
Alfalfa Mosaic Virus ◽  
Protein Dimers ◽  
Virus Rna

The coat protein of the RNA bacteriophage MS2

1967 ◽  
Vol 24 (1) ◽  
pp. 1-14 ◽  
Author(s):  
Jung-Yaw Lin ◽  
Chung M. Tsung ◽  
H. Fraenkel-Conrat
Keyword(s):  
Coat Protein ◽  
Bacteriophage Ms2

scholarly journals The structure of a plant-specific partitivirus capsid reveals a unique coat protein domain architecture with an intrinsically disordered protrusion

2021 ◽  
Vol 4 (1) ◽  
Author(s):  
Matthew Byrne ◽  
Aseem Kashyap ◽  
Lygie Esquirol ◽  
Neil Ranson ◽  
Frank Sainsbury
Keyword(s):  
Coat Protein ◽  
Domain Architecture ◽  
Plant Viruses ◽  
Protein Domain ◽  
Wild Plants ◽  
Structural Basis ◽  
Coat Proteins ◽  
Intrinsically Disordered ◽  
Binding Interface ◽  
Protein Dimers

AbstractPersistent plant viruses may be the most common viruses in wild plants. A growing body of evidence for mutualism between such viruses and their hosts, suggests that they play an important role in ecology and agriculture. Here we present the capsid structure of a plant-specific partitivirus, Pepper cryptic virus 1, at 2.9 Å resolution by Cryo-EM. Structural features, including the T = 1 arrangement of 60 coat protein dimers, are shared with fungal partitiviruses and the picobirnavirus lineage of dsRNA viruses. However, the topology of the capsid is markedly different with protrusions emanating from, and partly comprising, the binding interface of coat protein dimers. We show that a disordered region at the apex of the protrusion is not required for capsid assembly and represents a hypervariable site unique to, and characteristic of, the plant-specific partitiviruses. These results suggest a structural basis for the acquisition of additional functions by partitivirus coat proteins that enables mutualistic relationships with diverse plant hosts.

scholarly journals Bacteriophage MS2 Lysis Protein Does Not Require Coat Protein to Mediate Cell Lysis

1983 ◽  
Vol 153 (2) ◽  
pp. 1098-1100 ◽  
Author(s):  
Jack Coleman ◽  
Masayori Inouye ◽  
John Atkins
Keyword(s):  
Coat Protein ◽  
Cell Lysis ◽  
Bacteriophage Ms2 ◽  
Mediate Cell
Sign in / Sign up

Export Citation Format

Share Document