Flexible Viruses: Structural Disorder in Viral Proteins (Wiley Series in Protein and Peptide Science)

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Protein intrinsic disorder and influenza virulence: the 1918 H1N1 and H5N1 viruses

Chemes, and Gonzalo de Prat-Gay. Biochemistry , 55 10 , Cell Biochemistry and Biophysics , 76 3 , Manuel Garcia-Moreno, Aino I.


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Unconventional RNA-binding proteins step into the virus-host battlefront. Erik D. Holmstrom, Daniel Nettels, Benjamin Schuler.

Journal of Molecular Biology , 16 , Christopher A. Das, Raymond S. Disordered epitopes as peptide vaccines. Peptide Science , 24 , e Biophysical Journal , 8 , Larisa V.

Background

Kordyukova, Eleonora V. Shtykova, Lyudmila A. Baratova, Dmitri I.

Svergun, Oleg V. Matrix proteins of enveloped viruses: a case study of Influenza A virus M1 protein. Journal of Biomolecular Structure and Dynamics , 71 , Monika Reuter, Detlev H. The nucleocapsid protein of hantaviruses: much more than a genome-wrapping protein. Virus Genes , 54 1 , A comprehensive assessment of long intrinsic protein disorder from the DisProt database. Bioinformatics , 34 3 , Journal of Physics: Condensed Matter , 30 2 , Vladimir N.

Molecular Biology and Evolution , 35 1 , Perturbed human sub-networks by Fusobacterium nucleatum candidate virulence proteins. Microbiome , 5 1 DOI: Intrinsic disorder is a common structural characteristic of RxLR effectors in oomycete pathogens. Fungal Biology , 11 , An NMR study on the intrinsically disordered core transactivation domain of human glucocorticoid receptor. BMB Reports , 50 10 , Yoshiki Shigemitsu, Hidekazu Hiroaki.

Common molecular pathogenesis of disease-related intrinsically disordered proteins revealed by NMR analysis. How order and disorder within paramyxoviral nucleoproteins and phosphoproteins orchestrate the molecular interplay of transcription and replication. Cellular and Molecular Life Sciences , 74 17 , Eric B. Gibbs, Erik C. Cook, Scott A. Application of NMR to studies of intrinsically disordered proteins. Archives of Biochemistry and Biophysics , , Hiroko Nishikawa, Masanori Hatakeyama.

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Toxins , 9 4 , How to Predict Disorder in a Protein of Interest. Rita Pancsa, Peter Tompa. Essential functions linked with structural disorder in organisms of minimal genome. Biology Direct , 11 1 DOI: Mitra Kheirabadi, Majid Taghdir. Is unphosphorylated Rex, as multifunctional protein of HTLV-1, a fully intrinsically disordered protein? An in silico study. Biochemistry and Biophysics Reports , 8 , Jordon Rahaman, Jessica Siltberg-Liberles. Genome Biology and Evolution , 8 11 , Bhargavi Jayaraman, Amber M. Smith, Jason D.

Structure, Phosphorylation, and Biological Function of the HIV-1 Specific Virus Protein U (Vpu)

Fernandes, Alan D. Oligomeric viral proteins: small in size, large in presence. Critical Reviews in Biochemistry and Molecular Biology , 51 5 , BMB Reports , 49 8 , Dal Young Kim, Josephine M. Mobley, Ilya Frolov, Elena I. PLOS Pathogens , 12 8 , e Makarov, N. Structure and noncanonical activities of coat proteins of helical plant viruses. Biochemistry Moscow , 81 , Antibody Recognition of Disordered Antigens. Structure , 24 1 , Thawatchai Chaijarasphong, Robert J. Nichols, Kaitlyn E.

Prions and Protein Misfolding

Kortright, Charlotte F. Nixon, Poh K. Teng, Luke M. Oltrogge, David F. Programmed Ribosomal Frameshifting Mediates Expression of the? Journal of Molecular Biology , 1 , To obtain the best experience, we recommend you use a more up to date browser or turn off compatibility mode in Internet Explorer. In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript.

A Nature Research Journal. GP functions in cellular attachment, endosomal entry, and membrane fusion to initiate infection, and is a key therapeutic target. Nevertheless, only about half of the GP molecule has yet been solved to atomic resolution, excluding the mucin-like and transmembrane domains, and some of the glycans. We show that the mucin-like domain covers the glycan cap and partially occludes the receptor binding sites prior to proteolytic cleavage. Our structure is also consistent with key antibody neutralisation sites on GP being accessible prior to proteolysis. Based on the findings of us and others, GP-mediated binding may create an angle of 18 degrees between the planes of viral and endosomal membranes.

Ebola viruses EBOVs cause periodic outbreaks of severe hemorrhagic disease 1. The recent deadly outbreak in West Africa — was the largest in history, with 28, cases and 11, deaths 2. EBOV has a striking, filamentous structure: the helical nucleocapsid acquires an envelope by budding from the plasma membrane, a process driven by the VP40 matrix protein.

Intrinsically disordered proteins - Wikipedia

The viral envelope contains spikes consisting of the glycoprotein GP trimer 3 , 4 , 5. This GP molecule achieves the combined functions of attachment to host cells, endosomal entry, and membrane fusion 6 , 7 , 8 , 9 , 10 , 11 , As a class I fusion protein, EBOV GP plays key roles in cellular attachment, and entry of the virus into host cells, and is a key target for immune and therapeutic approaches 13 , 14 , 15 , 16 , 17 , There is extensive glycosylation, particularly in the mucin-like domain.

Cathepsin cleavage of GP in the endsome is necessary for exposure of the NPC-1 binding site and subsequent fusion: binding to the receptor is thought to trigger fusion 13 , 14 , 17 , 20 , 21 , GP2 is bound to the viral envelope by the transmembrane domain and contains the fusion peptide which achieves membrane fusion 19 , 20 , 21 , 22 , 23 , 24 , The latter is the largest and most detailed structure of the EBOV GP described so far, however certain domains are still missing, due to the need to truncate the transmembrane and certain glycosylation sites in order to achieve crystallization.

The GP spike is the only surface protein in EBOVs, unlike some other enveloped viruses, for example paramyxoviruses, which have separate proteins that perform the viral attachment and fusion functions.

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In EBOV the GP is solely responsible for both of these functions and the presence of a single species of spike molecule simplifies analysis by cryo-electron microscopy and image processing. Previous structural investigations of the entire GP trimer have relied upon recombinant expression of truncated mutants without a transmembrane domain, or as smaller sub-domains of the GP molecule, or as artificial virus-like particles VLPs 15 , 16 , 18 , 24 , 26 , 27 , 28 , The structure presented in the current investigation is based solely on data from the entire glycosylated GP on the surface of EBOV, using virions purified from EBOV infection in cell culture, and not recombinant expressed versions of the GP spike.

These GP spike images were analysed using the single particle method only Fig. S1,S2 , as a comparison to structures previously obtained by us and others using tomographic methods. Discrepancies had been observed between the structures of the entire, untruncated EBOV GP determined using material produced with differing heterologous expression systems, and between structures obtained using alternative tomographic or single-particle three-dimensional image processing methods 4 , Due to safety concerns, the virus preparation was treated using paraformaldehyde crosslinking after centrifugation in a protocol that has previously been shown to preserve protein and lipid structures 4 , Ebola virions are flexible, and viral filaments are frequently curved when prepared in the frozen-hydrated state for cryo-electron microscopy Fig.

Therefore, regions of virions that were as straight as possible were selected for image processing Fig.