Do Viral Proteins Possess Unique Features?

Xue, Bin; Williams, Robert W.; Oldfield, Christopher J.; Goh, Gerard Kian-Meng; Dunker, A. Keith; Uversky, Vladimir N.

doi:10.1002/9781118135570.ch1

Cited by 6 publications

(8 citation statements)

References 193 publications

(184 reference statements)

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“…The proportions of predicted continuous disordered segments are shown as a function of the length of the disordered region. Data were taken from ref .…”

Section: Prevalence Of Intrinsic Disorder In Viral Proteins As Unveil...mentioning

confidence: 99%

Structural Disorder in Viral Proteins

Xue¹,

et al. 2014

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“…The proportions of predicted continuous disordered segments are shown as a function of the length of the disordered region. Data were taken from ref .…”

Section: Prevalence Of Intrinsic Disorder In Viral Proteins As Unveil...mentioning

confidence: 99%

Structural Disorder in Viral Proteins

Xue¹,

et al. 2014

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“…Indeed, the high content of intrinsic disorder predicted in viruses agrees with a recent study which showed that viral proteins were significantly enriched in polar residues and depleted in hydrophobic residues compared with that of archaea and bacteria, 109 which correlates with their disorderedness. 110 , 111 The high intrinsic disorder in viral proteins is supposedly linked to important functional implications, helping the viruses to highjack various pathways of the host cells and/or to accommodate to their hostile habitats. 110 , 111 The roles of IDPs/IDRs in certain viral proteins upon viral infections have been explored but are not yet completely understood, including membrane-binding protein λN of bacteriophage, horde virus protein TGBp1, influenza virus nonstructural protein 2, basic protein δAg of hepatitis B virus, and human adenovirus type 5.…”

Section: Intrinsically Disordered Proteins In Sars-cov-2 Proteome And...mentioning

confidence: 99%

“… 110 , 111 The high intrinsic disorder in viral proteins is supposedly linked to important functional implications, helping the viruses to highjack various pathways of the host cells and/or to accommodate to their hostile habitats. 110 , 111 The roles of IDPs/IDRs in certain viral proteins upon viral infections have been explored but are not yet completely understood, including membrane-binding protein λN of bacteriophage, horde virus protein TGBp1, influenza virus nonstructural protein 2, basic protein δAg of hepatitis B virus, and human adenovirus type 5. 1 …”

Section: Intrinsically Disordered Proteins In Sars-cov-2 Proteome And...mentioning

confidence: 99%

Intrinsically Disordered Proteins: Perspective on COVID-19 Infection and Drug Discovery

Tenchov

Zhou

2022

ACS Infect. Dis.

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Since the beginning of the COVID-19 pandemic caused by SARS-CoV-2, millions of patients have been diagnosed and many of them have died from the disease worldwide. The identification of novel therapeutic targets are of utmost significance for prevention and treatment of COVID-19. SARS-CoV-2 is a single-stranded RNA virus with a 30 kb genome packaged into a membrane-enveloped virion, transcribing several tens of proteins. The belief that the amino acid sequence of proteins determines their 3D structure which, in turn, determines their function has been a central principle of molecular biology for a long time. Recently, it has been increasingly realized, however, that there is a large group of proteins that lack a fixed or ordered 3D structure, yet they exhibit important biological activities—so-called intrinsically disordered proteins and protein regions (IDPs/IDRs). Disordered regions in viral proteins are generally associated with viral infectivity and pathogenicity because they endow the viral proteins the ability to easily and promiscuously bind to host proteins; therefore, the proteome of SARS-CoV-2 has been thoroughly examined for intrinsic disorder. It has been recognized that, in fact, the SARS-CoV-2 proteome exhibits significant levels of structural order, with only the nucleocapsid (N) structural protein and two of the nonstructural proteins being highly disordered. The spike (S) protein of SARS-CoV-2 exhibits significant levels of structural order, yet its predicted percentage of intrinsic disorder is still higher than that of the spike protein of SARS-CoV. Noteworthy, however, even though IDPs/IDRs are not common in the SARS-CoV-2 proteome, the existing ones play major roles in the functioning and virulence of the virus and are thus promising drug targets for rational antiviral drug design. Presented here is a COVID-19 perspective on the intrinsically disordered proteins, summarizing recent results on the SARS-CoV-2 proteome disorder features, their physiological and pathological relevance, and their prominence as prospective drug target sites.

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“…Also, a remarkable discovery that tryptophan conformation and absolute stereochemistry could be determined from the signs of the tryptophan W3 ROA bands was made from ROA data on filamentous bacteriophages [33], further insight into this assignment being provided by later DFT calculations [63]. The importance of intrinsic disorder in viral coat proteins is being increasingly recognized, especially to facilitate rapid changes at almost all stages of their life cycle, with many functions attributed to disordered regions [101]. In fact the strong positive ∼1316 cm −1 band in the ROA spectrum of STMV (Fig.…”

Section: Virusesmentioning

confidence: 99%

The development of biomolecular Raman optical activity spectroscopy

Barron

2015

BSI

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Abstract. Following its first observation over 40 years ago, Raman optical activity (ROA), which may be measured as a small difference in the intensity of vibrational Raman scattering from chiral molecules in right-and left-circularly polarized incident light or, equivalently, the intensity of a small circularly polarized component in the scattered light using incident light of fixed polarization, has evolved into a powerful chiroptical spectroscopy for studying a large range of biomolecules in aqueous solution. The long and tortuous path leading to the first observations of ROA in biomolecules in 1989, in which the author was closely involved from the very beginning, is documented, followed by a survey of subsequent developments and applications up to the present day. Among other things, ROA provides information about motif and fold, as well as secondary structure, of proteins; solution structure of carbohydrates; polypeptide and carbohydrate structure of intact glycoproteins; new insight into structural elements present in unfolded protein sequences; and protein and nucleic acid structure of intact viruses. Quantum chemical simulations of observed Raman optical activity spectra provide the complete three-dimensional structure, together with information about conformational dynamics, of smaller biomolecules. Biomolecular ROA measurements are now routine thanks to a commercial instrument based on a novel design becoming available in 2004.

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Do Viral Proteins Possess Unique Features?

Abstract: Many proteins (or protein regions) are intrinsically disordered. They lack unique 3D structures in their native, functional states under physiological conditions

Cited by 6 publications

References 193 publications

Structural Disorder in Viral Proteins

Structural Disorder in Viral Proteins

Intrinsically Disordered Proteins: Perspective on COVID-19 Infection and Drug Discovery

The development of biomolecular Raman optical activity spectroscopy

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