Abstract
Epstein-Barr virus nuclear antigen leader protein (EBNA-LP) is important for primary B-lymphocyte growth transformation. We now demonstrate that the W repeat-encoded domain of EBNA-LP significantly associates with proteins of the heat shock protein 70 family (hsp72/hsc73). hsp72/hsc73 may mediate the previously observed interaction between EBNA-LP and the retinoblastoma protein or p53.
MeSH Terms
Amino Acid Sequence
Antigens, Viral/biosynthesis,isolation & purification,metabolism
B-Lymphocytes/immunology,physiology,virology
Cell Line
DNA-Binding Proteins/biosynthesis,isolation & purification,metabolism
Electrophoresis, Polyacrylamide Gel
Epstein-Barr Virus Nuclear Antigens
Gene Expression
HSC70 Heat-Shock Proteins
HSP70 Heat-Shock Proteins
HSP72 Heat-Shock Proteins
Heat-Shock Proteins/chemistry,isolation & purification,metabolism
Humans
Lymphocyte Activation
Methionine/metabolism
Molecular Sequence Data
Protein Binding
Recombinant Proteins/biosynthesis,isolation & purification,metabolism
Retinoblastoma Protein/metabolism
Trans-Activators/isolation & purification,metabolism
Tumor Suppressor Protein p53/metabolism
Chemicals
Antigens, Viral
DNA-Binding Proteins
Epstein-Barr Virus Nuclear Antigens
HSC70 Heat-Shock Proteins
HSP70 Heat-Shock Proteins
HSP72 Heat-Shock Proteins
HSPA8 protein, human
Heat-Shock Proteins
Recombinant Proteins
Retinoblastoma Protein
Trans-Activators
Tumor Suppressor Protein p53
Methionine
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Mannick J B
Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, Massachusetts 02114, USA.
Tong X
Hemnes A
Kieff E
References (23)
23 references, click to expand
-
Monoclonal antibodies to Epstein-Barr virus-induced, transformation-associated cell surface antigens: binding patterns and effect upon virus-specific T-cell cytotoxicity.
Int J Cancer. 1982 Apr 15;29(4):373-81
PMID: 6282762
-
Common and divergent peptide binding specificities of hsp70 molecular chaperones.
J Biol Chem. 1994 Dec 2;269(48):30470-8
PMID: 7982963
-
Nucleotide sequences of mRNAs encoding Epstein-Barr virus nuclear proteins: a probable transcriptional initiation site.
Proc Natl Acad Sci U S A. 1986 Jul;83(14):5096-100
PMID: 3460083
-
Expression of human HSP70 during the synthetic phase of the cell cycle.
Proc Natl Acad Sci U S A. 1986 Dec;83(24):9517-21
PMID: 3540942
-
A bicistronic Epstein-Barr virus mRNA encodes two nuclear proteins in latently infected, growth-transformed lymphocytes.
J Virol. 1987 Apr;61(4):945-54
PMID: 3029429
-
Epstein-Barr virus gp350/220 binding to the B lymphocyte C3d receptor mediates adsorption, capping, and endocytosis.
Cell. 1987 Jul 17;50(2):203-13
PMID: 3036369
-
Immunological evidence for the association of p53 with a heat shock protein, hsc70, in p53-plus-ras-transformed cell lines.
Mol Cell Biol. 1987 Aug;7(8):2863-9
PMID: 3313006
-
Monoclonal and polyclonal antibodies against Epstein-Barr virus nuclear antigen 5 (EBNA-5) detect multiple protein species in Burkitt's lymphoma and lymphoblastoid cell lines.
J Virol. 1987 Dec;61(12):3870-8
PMID: 2824821
-
Purification of complexes of nuclear oncogene p53 with rat and Escherichia coli heat shock proteins: in vitro dissociation of hsc70 and dnaK from murine p53 by ATP.
Mol Cell Biol. 1988 Mar;8(3):1206-15
PMID: 3285177
-
Differential distribution of the adenovirus E1A proteins and colocalization of E1A with the 70-kilodalton cellular heat shock protein in infected cells.
J Virol. 1988 Nov;62(11):4153-66
PMID: 2971821
-
Cell cycle-dependent association of HSP70 with specific cellular proteins.
J Cell Biol. 1989 Feb;108(2):413-23
PMID: 2645297
-
Genetic analysis of immortalizing functions of Epstein-Barr virus in human B lymphocytes.
Nature. 1989 Aug 3;340(6232):393-7
PMID: 2547164
-
Association of a cellular heat shock protein with simian virus 40 large T antigen in transformed cells.
J Virol. 1989 Sep;63(9):3961-73
PMID: 2760986
-
Stress proteins, infection, and immune surveillance.
Cell. 1989 Oct 6;59(1):5-8
PMID: 2676194
-
Members of the 70-kilodalton heat shock protein family contain a highly conserved calmodulin-binding domain.
Mol Cell Biol. 1990 Mar;10(3):1234-8
PMID: 2154682
-
The v-rel oncogene product is complexed with cellular proteins including its proto-oncogene product and heat shock protein 70.
Virology. 1990 Mar;175(1):149-60
PMID: 2155506
-
Nuclear colocalization of cellular and viral myc proteins with HSP70 in myc-overexpressing cells.
J Virol. 1991 Feb;65(2):842-51
PMID: 1846202
-
Identification of cellular proteins that can interact specifically with the T/E1A-binding region of the retinoblastoma gene product.
Cell. 1991 Feb 8;64(3):521-32
PMID: 1825028
-
The Epstein-Barr virus nuclear protein encoded by the leader of the EBNA RNAs is important in B-lymphocyte transformation.
J Virol. 1991 Dec;65(12):6826-37
PMID: 1658376
-
The transport of proteins into the nucleus requires the 70-kilodalton heat shock protein or its cytosolic cognate.
Mol Cell Biol. 1992 May;12(5):2186-92
PMID: 1569948
-
Protein interaction of retinoblastoma gene product pRb110 with M(r) 73,000 heat shock cognate protein.
Cancer Res. 1993 Apr 1;53(7):1702-5
PMID: 8453645
-
EBNA-5, an Epstein-Barr virus-encoded nuclear antigen, binds to the retinoblastoma and p53 proteins.
Proc Natl Acad Sci U S A. 1993 Jun 15;90(12):5455-9
PMID: 8390666
-
Specific interaction between the p53 cellular tumour antigen and major heat shock proteins.
Nature. 1986 Mar 13-19;320(6058):182-4
PMID: 3513022