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Human herpesvirus portal proteins: Structure, function, and antiviral prospects
Ellyn M Kornfeind1, Robert J Visalli1
1Department of Biomedical Sciences, Mercer University School of Medicine, Savannah, GA, USA.
Reviews in Medical Virology
|March 25, 2018
Summary
Herpesviruses and bacteriophages share a conserved DNA packaging mechanism involving portal proteins. Targeting these essential viral proteins offers a promising strategy for developing new antiviral therapies.
Area of Science:
- Virology
- Structural Biology
- Biochemistry
Background:
- Herpesviruses (Herpesvirales) and tailed bacteriophages (Caudovirales) utilize a conserved mechanism for dsDNA genome packaging.
- While phage portal protein mechanisms are well-understood, herpesvirus portal protein structure and function (e.g., HSV-1, CMV, VZV, HHV-8) are increasingly elucidated.
- This process involves virus-encoded terminase cleavage of dsDNA concatamers and packaging into procapsids via a portal vertex.
Purpose of the Study:
- To review the structure and function of herpesvirus portal proteins.
- To highlight conserved mechanisms between herpesviruses and bacteriophages.
- To explore the potential of targeting portal proteins for novel antiviral drug development.
Main Methods:
- Comparative analysis of structural and functional data from herpesvirus and bacteriophage portal proteins.
- Review of existing literature on viral genome packaging and portal protein mechanisms.
- Examination of preclinical studies on small molecule inhibitors targeting portal proteins.
Main Results:
- Despite low primary sequence similarity, phage and herpesvirus portal proteins share conserved secondary and tertiary structures.
- Portal proteins are essential for viral DNA packaging and subsequent release during infection.
- Preclinical studies demonstrate that inhibiting portal protein function can prevent viral replication.
Conclusions:
- Herpesvirus and bacteriophage portal proteins, though diverse in sequence, share conserved structures and essential functions in DNA packaging.
- Targeting these conserved portal proteins represents a viable strategy for developing novel antiviral agents against herpesviruses.
- Further research into portal protein structure-function relationships can accelerate the development of specific DNA encapsidation inhibitors.
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