MYH9: A key protein involved in tumor progression and virus-related diseases

Liu, Qing; Cheng, Chao; Huang, Jiyu; Yan, Weiwei; Wen, Yinhao; Liu, Zhen; Zhou, Beixian; Guo, Suiqun; Fang, Weiyi

doi:10.1016/j.biopha.2023.116118

Cited by 9 publications

(1 citation statement)

References 142 publications

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“…In contrast, after 24 hpi, the infected RHTiB cells showed increased activity of cytoskeletal proteins such as MYH9 and PLEKHH2 76 . MYH9 has been identified as a receptor for the herpes simplex virus 1 and EBV 77 and serves as a co-receptor in the entry process of SARS-CoV-2 78 . Additionally, MYH9 is essential for the cellular entry of infectious pancreatic necrosis virus 79 and the replication of porcine reproductive and respiratory syndrome virus 80 .…”

Section: Discussionmentioning

confidence: 99%

Proteomic and phosphoproteomic profilings reveal distinct cellular responses during Tilapinevirus tilapiae entry and replication

Lertwanakarn,

Khemthong,

Setthawong

et al. 2024

Preprint

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Tilapia lake virus (TiLV) poses a significant threat to global tilapia aquaculture, as it causes high mortality rates and severe economic losses. Nevertheless, the molecular mechanisms of TiLV–host interactions remain poorly understood. We investigated the proteomic and phosphoproteomic changes in E-11 and RHTiB cell lines following TiLV infection. Using mass spectrometry-based analyses, we identified substantial alterations in protein expression and phosphorylation states, highlighted distinct cell line responses. In E-11 cells, TiLV infection suppressed the proteins involved in the Janus kinase–signal transducer and activators of transcription and Fas-associated death domain protein–tumor necrosis factor receptor associated factor pathways, leading to the activation of nucleotide oligomerization domain signaling and cellular apoptosis. The TiLV-infected RHTiB cells showed suppression of the host cellular metabolism through a reduction in protein phosphatase to facilitate early viral entry, while later stages of infection involved increased activity of myosin heavy chain 9 and enhanced host immune responses via the phosphorylation of ribosomal protein L17 and GTPase immunity-associated protein family member 7. These findings suggest that TiLV employs different strategies to manipulate host cellular pathways depending on the cell type. Further studies are essential to validate these findings and ultimately facilitate the development of effective antiviral strategies.

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