Cytomegaloviruses (CMVs) have developed multiple diverse strategies to ensure their replicative success and to evade immune recognition. Given the fact that G protein-coupled receptors (GPCRs) are key regulators of numerous cellular processes and modify a variety of signaling pathways, it is not surprising that CMVs and other herpesviruses have hijacked mammalian GPCRs during their coevolution. Human cytomegalovirus (HCMV) encodes for four viral GPCR homologues (vGPCRs), termed US27, US28, UL33, and UL78. Although HCMV-encoded GPCRs were first described in 1990, the pivotal functions of these viral receptor proteins were detected only recently. Here, we summarize seminal knowledge on the functions of herpesviral vGPCRs with a focus on novel roles of cytomegalovirus-encoded vGPCRs for viral spread and the regulation of latency.
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Human cytomegalovirus (HCMV) encodes four viral Fc-gamma receptors (vFcγRs) that counteract antibody-mediated activation , but their role in infection and pathogenesis is unknown. To examine the function of vFcγRs in animal hosts closely related to humans, we identified and characterized vFcγRs encoded by rhesus CMV (RhCMV). We demonstrate that Rh05, Rh152/151 and Rh173 represent the complete set of RhCMV vFcγRs, each displaying functional similarities to their respective HCMV orthologs with respect to antagonizing host FcγR activation .
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Virology Laboratory, Shengjing Hospital of China Medical University, Shenyang, China.
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MRC-University of Glasgow Centre for Virus Research, Glasgow, United Kingdom.
Article Synopsis
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Functional Relevance of the Interaction between Human Cyclins and the Cytomegalovirus-Encoded CDK-Like Protein Kinase pUL97.
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Institute of Clinical and Molecular Virology, Friedrich-Alexander University of Erlangen-Nürnberg (FAU), 91054 Erlangen, Germany.
The replication of human cytomegalovirus (HCMV) is characterized by a complex network of virus-host interaction. This involves the regulatory viral protein kinase pUL97, which represents a viral cyclin-dependent kinase ortholog (vCDK) combining typical structural and functional features of host CDKs. Notably, pUL97 interacts with the three human cyclin types T1, H and B1, whereby the binding region of cyclin T1 and the region conferring oligomerization of pUL97 were both assigned to amino acids 231-280.
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Viruses
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Amsterdam Institute for Molecular and Life Sciences (AIMMS), Division of Medicinal Chemistry, Faculty of Sciences, Vrije Universiteit, De Boelelaan 1108, 1081 HZ Amsterdam, The Netherlands.
Human cytomegalovirus (HCMV) encodes four G protein-coupled receptor (GPCR) homologs. Three of these receptors, UL78, US27 and US28, are known for their roles in HCMV dissemination and latency. Despite importance of its rodent orthologs for viral replication and pathogenesis, such a function is not reported for the HCMV-encoded GPCR UL33.
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