Point mutations in the herpes simplex virus type 1 Vmw110 RING finger helix affect activation of gene expression, viral growth, and interaction with PML-containing nuclear structures

Herpes simplex virus type 1 immediate-early protein Vmw110 (also known as ICP0) has been implicated in the control of the balance between the lytic and latent states, but the precise mechanisms by which it exerts its effects are unknown. Vmw110 includes a characteristic zinc binding domain, termed the C3HC4 domain or RING finger, which is essential for its function. The solution structure of a related herpesvirus RING finger domain suggested that an amphipathic alpha helix might be an important functional component of the RING finger. In this paper, we show that the equivalent region of Vmw110 is important for virus growth in tissue culture and for the normal interaction of Vmw110 with nuclear structures which include the PML protein.

[1]  P. Freemont,et al.  The solution structure of the RING finger domain from the acute promyelocytic leukaemia proto‐oncoprotein PML. , 1995, The EMBO journal.

[2]  R. Everett,et al.  HSV‐1 IE protein Vmw110 causes redistribution of PML. , 1994, The EMBO journal.

[3]  R. Everett,et al.  The nuclear location of PML, a cellular member of the C3HC4 zinc-binding domain protein family, is rearranged during herpes simplex virus infection by the C3HC4 viral protein ICP0. , 1994, The Journal of general virology.

[4]  B. Luisi,et al.  Structure of the C3HC4 domain by 1H-nuclear magnetic resonance spectroscopy. A new structural class of zinc-finger. , 1994, Journal of molecular biology.

[5]  N. Stuurman,et al.  The t(15;17) translocation alters a nuclear body in a retinoic acid‐reversible fashion. , 1994, The EMBO journal.

[6]  P. Desai,et al.  The RR1 Gene of Herpes Simplex Virus Type 1 Is Uniquely trans Activated by ICP0 during Infection , 1994, Journal of virology.

[7]  Maria Carmo-Fonseca,et al.  Retinoic acid regulates aberrant nuclear localization of PML-RARα in acute promyelocytic leukemia cells , 1994, Cell.

[8]  R. Evans,et al.  A novel macromolecular structure is a target of the promyelocyte-retinoic acid receptor oncoprotein , 1994, Cell.

[9]  B. Luisi,et al.  A novel arrangement of zinc-binding residues and secondary structure in the C3HC4 motif of an alpha herpes virus protein family. , 1993, Journal of molecular biology.

[10]  G. Maul,et al.  Modification of discrete nuclear domains induced by herpes simplex virus type 1 immediate early gene 1 product (ICP0). , 1993, The Journal of general virology.

[11]  R. Everett,et al.  A truncated form of herpes simplex virus type 1 immediate-early protein Vmw110 is expressed in a cell type dependent manner. , 1993, Virology.

[12]  P. Schaffer,et al.  The herpes simplex virus type 1 regulatory protein ICP0 enhances virus replication during acute infection and reactivation from latency , 1993, Journal of virology.

[13]  P. Desai,et al.  The RR1 gene of herpes simplex virus type 1 is uniquely trans activated by ICP0 during infection , 1993 .

[14]  D. McGeoch,et al.  Emerging functions of alphaherpesvirus genes , 1993 .

[15]  T. Block,et al.  The latency-associated transcripts of herpes simplex virus: RNA in search of function. , 1992, Virology.

[16]  B. Humbel,et al.  A monoclonal antibody recognizing nuclear matrix-associated nuclear bodies. , 1992, Journal of cell science.

[17]  P. Chambon,et al.  Structure, localization and transcriptional properties of two classes of retinoic acid receptor alpha fusion proteins in acute promyelocytic leukemia (APL): structural similarities with a new family of oncoproteins. , 1992, The EMBO journal.

[18]  N. Stow,et al.  A herpes simplex virus type 1 mutant containing a deletion within immediate early gene 1 is latency-competent in mice. , 1989, The Journal of general virology.

[19]  R. Everett,et al.  Herpes simplex virus type 1 immediate-early protein Vmw110 reactivates latent herpes simplex virus type 2 in an in vitro latency system , 1989, Journal of virology.

[20]  R. Everett.  Construction and characterization of herpes simplex virus type 1 mutants with defined lesions in immediate early gene 1. , 1989, The Journal of general virology.

[21]  K. Tyler,et al.  Immediate-early regulatory gene mutants define different stages in the establishment and reactivation of herpes simplex virus latency , 1989, Journal of virology.

[22]  R. Everett.  Analysis of the functional domains of herpes simplex virus type 1 immediate-early polypeptide Vmw110. , 1988, Journal of molecular biology.

[23]  C. M. Preston,et al.  Herpes simplex virus genes involved in latency in vitro. , 1987, The Journal of general virology.

[24]  J. Northrop,et al.  Lipofection: a highly efficient, lipid-mediated DNA-transfection procedure. , 1987, Proceedings of the National Academy of Sciences of the United States of America.

[25]  R. Everett.  A detailed mutational analysis of Vmw110, a trans‐acting transcriptional activator encoded by herpes simplex virus type 1. , 1987, The EMBO journal.

[26]  R. Everett.  The regulation of transcription of viral and cellular genes by herpesvirus immediate-early gene products (review). , 1987, Anticancer research.

[27]  P. Schaffer,et al.  Deletion mutants in the gene encoding the herpes simplex virus type 1 immediate-early protein ICP0 exhibit impaired growth in cell culture , 1987, Journal of virology.

[28]  N. Stow,et al.  Isolation and characterization of a herpes simplex virus type 1 mutant containing a deletion within the gene encoding the immediate early polypeptide Vmw110. , 1986, The Journal of general virology.

[29]  R. Everett.  Functional and genetic analysis of the role of Vmw110 in herpes simplex virus replication , 1991 .