Unknown

Dataset Information

0

Aggregation Propensities of Herpes Simplex Virus-1 Proteins and Derived Peptides: An In Silico and In Vitro Analysis.


ABSTRACT: Recurrent infections of neurotropic herpes simplex virus-1 (HSV-1) have been implicated in etiology and pathology of Alzheimer's disease (AD). Although protein and peptide aggregation events are at the center of the AD pathophysiology, except a single study where a peptide derived from glycoprotein B of HSV-1 was reported to form ?-amyloid-like aggregates, similar investigations with the entire proteome of HSV-1 have not been attempted. In the current study, 70 HSV-1 proteins were screened using bioinformatics tools to identify aggregation-prone candidates. Thereafter, the 20S proteasome cleavage sites within the sequence of the selected proteins were determined using Pcleavage and NetChop algorithms, thereby mimicking a cellular proteasomal activity providing short peptides. Here, we report the biochemical characterization of a 28-residue-long peptide (HSV-1 gK208-235) derived from glycoprotein K of HSV-1. The peptide showed high aggregation propensity and homology to the C-terminus of A?1-42 peptide. The aggregates of gK208-235 peptide were characterized by the Congo red and Thioflavin T assays and Fourier transform infrared (FTIR) spectroscopy, and their spheroid oligomeric structure was established by atomic force microscopy (AFM). Furthermore, the aggregates demonstrated dose-dependent cytotoxicity to primary mouse splenocytes. The current findings hypothesize a mechanism by which HSV-1 may contribute to AD, which may be pursued further in the future.

SUBMITTER: Singh VK 

PROVIDER: S-EPMC7288601 | biostudies-literature | 2020 Jun

REPOSITORIES: biostudies-literature

altmetric image

Publications

Aggregation Propensities of Herpes Simplex Virus-1 Proteins and Derived Peptides: An <i>In Silico</i> and <i>In Vitro</i> Analysis.

Singh Vikas Kumar VK   Kumar Sandeep S   Tapryal Suman S  

ACS omega 20200526 22


Recurrent infections of neurotropic herpes simplex virus-1 (HSV-1) have been implicated in etiology and pathology of Alzheimer's disease (AD). Although protein and peptide aggregation events are at the center of the AD pathophysiology, except a single study where a peptide derived from glycoprotein B of HSV-1 was reported to form β-amyloid-like aggregates, similar investigations with the entire proteome of HSV-1 have not been attempted. In the current study, 70 HSV-1 proteins were screened using  ...[more]

Similar Datasets

| S-EPMC8157732 | biostudies-literature
| S-EPMC3489092 | biostudies-literature
| S-EPMC1472043 | biostudies-literature
| S-EPMC7168125 | biostudies-literature
| PRJNA338711 | ENA
| S-EPMC7172891 | biostudies-literature
2017-08-30 | GSE95716 | GEO
| S-EPMC2993110 | biostudies-literature
| S-EPMC556126 | biostudies-literature
2022-10-18 | GSE202363 | GEO