Interaction between viral proteins and hosts and its disturbance in the cellular responses to ionising radiation.
OBJECTIVE
Human malignant tumours are frequently found to be infected with a variety of viruses. The interaction of virus-encoded proteins with host cells proteins is highlighted in connection with the effect of viral proteins on DNA damage signalling and its impact on the sensitivity of cancer cells to ionising radiation.


CONCLUSIONS
The interaction of virus-encoded proteins with host cells not only plays an important role in viral infection and the consequential pathogenesis, but may also have an influence on the response of infected cancers to radiotherapy or chemotherapy. A series of viral proteins have already been demonstrated to interact with host proteins that are associated with cellular responses to DNA double-strand breaks, including DNA repair, apoptosis and cell cycle checkpoints, and this interaction results in mislocalisation, degradation, inactivation or activation of these host proteins. Some others directly or indirectly regulate the transcriptional level of a number of host genes or post-transcriptional modification of host proteins responding to ionising radiation, which leads to accumulation or downregulation of these gene products. These interactions between viral proteins and the hosts contribute to some extent to altered cellular radiosensitivity. Fully and accurately understanding the biological significance of viral infection to radiation will promote the future development of individualised strategies of cancer radiotherapy.
Zhou
Ping-Kun
PK
The Department of Radiation Toxicology and Oncology, Beijing Institute of Radiation Medicine, Beijing, P. R. China. zhoupk@nic.bmi.ac.cn
Sun
Yi
Y
An
Jing
J
D000818:Animals; D017209:Apoptosis / Q000528:radiation effects; D064007:Ataxia Telangiectasia Mutated Proteins; D002453:Cell Cycle; D018797:Cell Cycle Proteins / Q000378:metabolism; D064447:Checkpoint Kinase 2; D004249:DNA Damage; D004260:DNA Repair; D004268:DNA-Binding Proteins / Q000378:metabolism / Q000502:physiology; D004720:Endonucleases / Q000502:physiology; D006657:Histones / Q000378:metabolism; D006801:Humans; D009369:Neoplasms / Q000532:radiotherapy* / Q000821:virology; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism; D011836:Radiation Tolerance; D015398:Signal Transduction; D025521:Tumor Suppressor Proteins / Q000378:metabolism; D014764:Viral Proteins / Q000502:physiology*
D018797:Cell Cycle Proteins; D004268:DNA-Binding Proteins; C468783:H2AX protein, human; D006657:Histones; D025521:Tumor Suppressor Proteins; D014764:Viral Proteins; D064447:Checkpoint Kinase 2; C576324:ATM protein, human; D064007:Ataxia Telangiectasia Mutated Proteins; C578634:CHEK2 protein, human; D017346:Protein Serine-Threonine Kinases; C071447:ERCC1 protein, human; D004720:Endonucleases