MINI REVIEW article
Front. Vet. Sci.
Sec. Veterinary Infectious Diseases
Volume 12 - 2025 | doi: 10.3389/fvets.2025.1634345
The role of posttranslational modifications in the parvovirus life cycle
Provisionally accepted- Guizhou University of Engineering Science, Bijie, China
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Parvoviruses are a group of single-stranded DNA viruses without envelope and widely distributed in both vertebrates and invertebrates. During viral infection, parvoviruses hijack the host cell's translational machinery to support the viral protein synthesis and replication, following which viral proteins undergo various posttranslational modifications (PTMs). Parvovirus nonstructural (NS) and capsid protein are modified by PTMs, including phosphorylation, ubiquitination, SUMOylation and glycosylation. The phosphorylation of parvovirus mainly occurs on NS and capsid protein, which modulates the NS protein's function and activities and capsid protein's assembly. Ubiquitination and SUMOylation of parvoviral capsid protein mainly affect the intracellular trafficking during viral infection. Glycosylation of parvoviral capsid protein involves in regulation of the stability of virion and infectivity. In this review, we summarize the PTMs of parvovirus proteins, as well as the impact of PTMs on viral life cycle that would be helpful in understanding the viral replication and pathogenesis.
Keywords: Parvovirus, Phosphorylation, Ubiquitination, Sumoylation, Glycosylation
Received: 24 May 2025; Accepted: 18 Jun 2025.
Copyright: © 2025 Liu and Yang. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
* Correspondence: Peng Liu, Guizhou University of Engineering Science, Bijie, China
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