The role of post-translational modifications in parvovirus life cycle

Parvoviruses are a group of single-stranded DNA viruses that lack an envelope and are widely distributed in both vertebrates and invertebrates. When they infect a host cell, parvoviruses take over the cell’s translational machinery to support the viral genome replication and proteins synthesis, foll...

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Main Authors: Peng Liu, Liqin Yang
Format: Article
Language:English
Published: Frontiers Media S.A. 2025-07-01
Series:Frontiers in Veterinary Science
Subjects:
Online Access:https://www.frontiersin.org/articles/10.3389/fvets.2025.1634345/full
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author Peng Liu
Liqin Yang
author_facet Peng Liu
Liqin Yang
author_sort Peng Liu
collection DOAJ
description Parvoviruses are a group of single-stranded DNA viruses that lack an envelope and are widely distributed in both vertebrates and invertebrates. When they infect a host cell, parvoviruses take over the cell’s translational machinery to support the viral genome replication and proteins synthesis, following which viral proteins undergo various post-translational modifications (PTMs). Parvovirus non-structural (NS) and capsid proteins are modified by PTMs, including phosphorylation, ubiquitination, SUMOylation, and glycosylation. Phosphorylation of parvovirus mainly occurs on NS and capsid proteins, modulating the functions and activities of the NS protein and the assembly of the capsid protein. Ubiquitination and SUMOylation of parvoviral capsid proteins mainly affect intracellular trafficking during viral infection. Glycosylation of parvoviral capsid proteins is involved in the regulation of virion stability and infectivity. In this review, we summarize the PTMs of parvovirus proteins and discuss their impact on the viral life cycle, which will help in understanding viral replication and pathogenesis.
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spelling doaj-art-726199dcdbaf43988429ebcb458e7c232025-08-20T03:29:30ZengFrontiers Media S.A.Frontiers in Veterinary Science2297-17692025-07-011210.3389/fvets.2025.16343451634345The role of post-translational modifications in parvovirus life cyclePeng LiuLiqin YangParvoviruses are a group of single-stranded DNA viruses that lack an envelope and are widely distributed in both vertebrates and invertebrates. When they infect a host cell, parvoviruses take over the cell’s translational machinery to support the viral genome replication and proteins synthesis, following which viral proteins undergo various post-translational modifications (PTMs). Parvovirus non-structural (NS) and capsid proteins are modified by PTMs, including phosphorylation, ubiquitination, SUMOylation, and glycosylation. Phosphorylation of parvovirus mainly occurs on NS and capsid proteins, modulating the functions and activities of the NS protein and the assembly of the capsid protein. Ubiquitination and SUMOylation of parvoviral capsid proteins mainly affect intracellular trafficking during viral infection. Glycosylation of parvoviral capsid proteins is involved in the regulation of virion stability and infectivity. In this review, we summarize the PTMs of parvovirus proteins and discuss their impact on the viral life cycle, which will help in understanding viral replication and pathogenesis.https://www.frontiersin.org/articles/10.3389/fvets.2025.1634345/fullparvovirusphosphorylationubiquitinationSUMOylationglycosylation
spellingShingle Peng Liu
Liqin Yang
The role of post-translational modifications in parvovirus life cycle
Frontiers in Veterinary Science
parvovirus
phosphorylation
ubiquitination
SUMOylation
glycosylation
title The role of post-translational modifications in parvovirus life cycle
title_full The role of post-translational modifications in parvovirus life cycle
title_fullStr The role of post-translational modifications in parvovirus life cycle
title_full_unstemmed The role of post-translational modifications in parvovirus life cycle
title_short The role of post-translational modifications in parvovirus life cycle
title_sort role of post translational modifications in parvovirus life cycle
topic parvovirus
phosphorylation
ubiquitination
SUMOylation
glycosylation
url https://www.frontiersin.org/articles/10.3389/fvets.2025.1634345/full
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