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Studies on the bovine herpesvirus 1 US3 protein kinase (BHV-1pUS3)

  • The pUS3, a serine/threonine protein kinase that is conserved in Alphaherpesvirinae may play an important in phosphorylation and regulation of the activities of viral and cellular proteins. It has also been proposed that pUS3 affects virulence. Whereas many studies of the pUS3 functions of HSV-1 and PrV, a closely related homolog of BHV-1 have supported these assumptions, the role of BHV-1pUS3 is not yet fully understood so far. The aims of this study therefore were to investigate the functions of BHV-1pUS3 for virus replication in cultured cells, effect on apoptosis and identification of protein interactions with cellular proteins and addressed the function of the aminoterminal region by generating a short isoform of BHV-1pUS3 which corresponds in size to the natural short isoforms of PrVpUS3 and HSV-1pUS3. Results of the study are briefly summarized here: -BHV-1pUS3 is, although not essential, beneficial for infectious replication of BHV-1 in-vitro. It also supports direct cell-to-cell spread of BHV-1/Aus12 and prevents the formation of electron dense aggregates with embedded capsids in nuclei of BHV-1 infected cells, a phenotype that may affect nuclear egress of BHV-1 nucleocapsids. -The protein, independent from other BHV-1 encoded functions, located mainly to the nuclei of cells. -In contrast to functions of pUS3 in PrV and HSV-1, the protein of BHV-1 has no anti-apoptotic activity. -Biologically active BHV-1pUS3 physically interacts with the cellular SET protein and overexpression of SET, independent from the expression of the protein, inhibits productive BHV-1 replication in a dose dependent manner. -The aminoterminal 101 amino acids of the protein are dispensable for all in-vitro functions tested whereas kinase activity is required.
  • The pUS3, a serine/threonine protein kinase that is conserved in Alphaherpesvirinae may play an important in phosphorylation and regulation of the activities of viral and cellular proteins. It has also been proposed that pUS3 affects virulence. Whereas many studies of the pUS3 functions of HSV-1 and PrV, a closely related homolog of BHV-1 have supported these assumptions, the role of BHV-1pUS3 is not yet fully understood so far. The aims of this study therefore were to investigate the functions of BHV-1pUS3 for virus replication in cultured cells, effect on apoptosis and identification of protein interactions with cellular proteins and addressed the function of the aminoterminal region by generating a short isoform of BHV-1pUS3 which corresponds in size to the natural short isoforms of PrVpUS3 and HSV-1pUS3. Results of the study are briefly summarized here: -BHV-1pUS3 is, although not essential, beneficial for infectious replication of BHV-1 in-vitro. It also supports direct cell-to-cell spread of BHV-1/Aus12 and prevents the formation of electron dense aggregates with embedded capsids in nuclei of BHV-1 infected cells, a phenotype that may affect nuclear egress of BHV-1 nucleocapsids. -The protein, independent from other BHV-1 encoded functions, located mainly to the nuclei of cells. -In contrast to functions of pUS3 in PrV and HSV-1, the protein of BHV-1 has no anti-apoptotic activity. -Biologically active BHV-1pUS3 physically interacts with the cellular SET protein and overexpression of SET, independent from the expression of the protein, inhibits productive BHV-1 replication in a dose dependent manner. -The aminoterminal 101 amino acids of the protein are dispensable for all in-vitro functions tested whereas kinase activity is required.

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Metadaten
Author: Quang Minh Luu
URN:urn:nbn:de:gbv:9-000936-4
Title Additional (English):Studies on the bovine herpesvirus 1 US3 protein kinase (BHV-1pUS3)
Title Additional (German):Untersuchungen zur bovinen Herpesvirus 1 US3 Proteinkinase (BHV-1pUS3)
Advisor:Prof. Dr. rer. nat G√ľnther M. Keil, Prof. Dr. Dr. h.c. Thomas C. Mettenleiter
Document Type:Doctoral Thesis
Language:English
Date of Publication (online):2011/03/14
Granting Institution:Ernst-Moritz-Arndt-Universität, Mathematisch-Naturwissenschaftliche Fakultät (bis 31.05.2018)
Date of final exam:2011/03/09
Release Date:2011/03/14
Tag:apoptosis, point mutation, protein interaction, viral replication
GND Keyword:protein kinase
Faculties:Universit√§tsmedizin / Friedrich-Loeffler-Institut f√ľr Medizinische Mikrobiologie
DDC class:500 Naturwissenschaften und Mathematik / 570 Biowissenschaften; Biologie