Superimposition of Viral Protein Structures: A Means to Decipher the Phylogenies of Viruses.
Viruses
; 12(10)2020 10 09.
Article
in English
| MEDLINE | ID: covidwho-906169
ABSTRACT
Superimposition of protein structures is key in unravelling structural homology across proteins whose sequence similarity is lost. Structural comparison provides insights into protein function and evolution. Here, we review some of the original findings and thoughts that have led to the current established structure-based phylogeny of viruses starting from the original observation that the major capsid proteins of plant and animal viruses possess similar folds, to the idea that each virus has an innate "self". This latter idea fueled the conceptualization of the PRD1-adenovirus lineage whose members possess a major capsid protein (innate "self") with a double jelly roll fold. Based on this approach, long-range viral evolutionary relationships can be detected allowing the virosphere to be classified in four structure-based lineages. However, this process is not without its challenges or limitations. As an example of these hurdles, we finally touch on the difficulty of establishing structural "self" traits for enveloped viruses showcasing the coronaviruses but also the power of structure-based analysis in the understanding of emerging viruses.
Keywords
Full text:
Available
Collection:
International databases
Database:
MEDLINE
Main subject:
Rhinovirus
/
Adenoviridae
/
Protein Structure, Tertiary
/
Coronavirus
/
Capsid Proteins
Type of study:
Observational study
/
Prognostic study
Language:
English
Year:
2020
Document Type:
Article
Affiliation country:
V12101146
Similar
MEDLINE
...
LILACS
LIS