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Peptide Scanning-assisted Identification of a Monoclonal Antibody-recognized Linear B-cell Epitope

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Tegument Protein pp150 Sequence-Specific Peptide Blocks Cytomegalovirus Infection.

Dipanwita Mitra¹, Mohammad H Hasan¹, John T Bates^1,2

¹Department of Microbiology and Immunology, University of Mississippi Medical Center, 2500 North State Street, Jackson, MS 39216, USA.

|November 27, 2021

Summary

A novel peptide inhibitor, pep-CR2, effectively targets human cytomegalovirus (HCMV) protein pp150, significantly reducing viral growth by disrupting capsid binding and nuclear egress. This peptide shows promise as a potential antiviral therapy.

Keywords:

CMV herpesviruses nuclear egress peptide therapy tegument

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Area of Science:

Virology
Structural Biology
Drug Discovery

Background:

Human cytomegalovirus (HCMV) tegument protein pp150 is crucial for viral maturation.
Previous research identified specific structural conformers of the pp150 N-terminus (pp150nt) involved in capsid stabilization.

Purpose of the Study:

To design and evaluate peptide inhibitors targeting the pp150nt-capsid interaction.
To investigate the antiviral efficacy and mechanism of action of novel pp150nt-targeting peptides.

Main Methods:

Peptide design based on atomic-level structural data of pp150nt.
In vitro antiviral assays to determine efficacy (IC50) and cell viability.
3D modeling to predict peptide-target interactions.
Cell-based assays to study viral protein localization and nuclear egress.

Main Results:

Peptide pep-CR2 demonstrated significant HCMV growth inhibition with an IC50 of 1.33 μM and no observed cytotoxicity.
3D modeling indicated pep-CR2 specifically disrupts the pp150-capsid binding interface.
Pre-treatment with pep-CR2 led to nuclear sequestration of pp150, inhibiting capsid loading and nuclear egress.
Pep-CR2 also showed inhibitory activity against mouse cytomegalovirus (MCMV) in cell culture.

Conclusions:

The CR2 region of pp150 is a viable target for peptide-based antiviral inhibitors.
Pep-CR2 represents a promising lead compound for developing novel HCMV and MCMV therapeutics.
Targeting the pp150-capsid interaction offers a new strategy for antiviral drug development.