Protein Intrinsic Disorder Toolbox for Comparative Analysis of Viral Proteins

Overview

Journal BMC Genomics

Publisher Biomed Central

Specialty Genetics

Date 2008 Oct 10

PMID 18831795

Citations 28

Authors

Gerard Kian-Meng Goh

A Keith Dunker

Vladimir N Uversky

Affiliations

Soon will be listed here.

Abstract

To examine the usefulness of protein disorder predictions as a tool for the comparative analysis of viral proteins, a relational database has been constructed. The database includes proteins from influenza A and HIV-related viruses. Annotations include viral protein sequence, disorder prediction, structure, and function. Location of each protein within a virion, if known, is also denoted. Our analysis reveals a clear relationship between proximity to the RNA core and the percentage of predicted disordered residues for a set of influenza A virus proteins. Neuraminidases (NA) and hemagglutinin (HA) of major influenza A pandemics tend to pair in such a way that both proteins tend to be either ordered-ordered or disordered-disordered by prediction. This may be the result of these proteins evolving from being lipid-associated. High abundance of intrinsic disorder in envelope and matrix proteins from HIV-related viruses likely represents a mechanism where HIV virions can escape immune response despite the availability of antibodies for the HIV-related proteins. This exercise provides an example showing how the combined use of intrinsic disorder predictions and relational databases provides an improved understanding of the functional and structural behaviour of viral proteins.

Citing Articles

Evolution of Intrinsic Disorder in Protein Loops.

Mughal F, Caetano-Anolles G Life (Basel). 2023; 13(10).

PMID: 37895436 PMC: 10608553. DOI: 10.3390/life13102055.

Biomolecular condensates: insights into early and late steps of the HIV-1 replication cycle.

Di Nunzio F, Uversky V, Mouland A Retrovirology. 2023; 20(1):4.

PMID: 37029379 PMC: 10081342. DOI: 10.1186/s12977-023-00619-6.

Liquid-liquid phase separation of nucleocapsid proteins during SARS-CoV-2 and HIV-1 replication.

Chau B, Chen V, Cochrane A, Parent L, Mouland A Cell Rep. 2023; 42(1):111968.

PMID: 36640305 PMC: 9790868. DOI: 10.1016/j.celrep.2022.111968.

A Study on the Nature of SARS-CoV-2 Using the Shell Disorder Models: Reproducibility, Evolution, Spread, and Attenuation.

Goh G, Dunker A, Foster J, Uversky V Biomolecules. 2022; 12(10).

PMID: 36291562 PMC: 9599796. DOI: 10.3390/biom12101353.

Shell Disorder Models Detect That Omicron Has Harder Shells with Attenuation but Is Not a Descendant of the Wuhan-Hu-1 SARS-CoV-2.

Goh G, Dunker A, Foster J, Uversky V Biomolecules. 2022; 12(5).

PMID: 35625559 PMC: 9139003. DOI: 10.3390/biom12050631.

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