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Query: UNIPROT:P06889 (Mol)
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Normal human c-fgr cDNA clones were constructed by using normal peripheral blood mononuclear cell mRNA as a template. Nucleotide sequence analysis of two such clones revealed a 1,587-base-pair-long open reading frame which predicted the primary amino acid sequence of the c-fgr translational product. Homology of this protein with the v-fgr translational product stretched from codons 128 to 516, where 32 differences among 388 codons were observed. Sequence similarity with human c-src, c-yes, and fyn translational products began at amino acid position 76 of the predicted c-fgr protein and extended nearly to its C-terminus. In contrast, the stretch of 75 amino acids at the N-terminus demonstrated a greatly reduced degree of relatedness to these same proteins. To verify the deduced amino acid sequence, antibodies were prepared against peptides representing amino- and carboxy-terminal regions of the predicted c-fgr translational product. Both antibodies specifically recognized a 55-kilodalton protein expressed in COS-1 cells transfected with a c-fgr cDNA expression plasmid. Moreover, the same protein was immunoprecipitated from an Epstein-Barr virus-infected Burkitt's lymphoma cell line which expressed c-fgr mRNA but not in its uninfected fgr mRNA-negative counterpart. These findings identified the 55-kilodalton protein as the product of the human fgr protooncogene.
Mol Cell Biol 1988 Jan
PMID:Primary structure of the human fgr proto-oncogene product p55c-fgr. 327 68

The technology for the production of murine monoclonal antibodies has been refined enormously since its introduction in 1975. However, the technology for generating human monoclonal antibodies has only recently come into its own. In this review, three currently available approaches to the production of human monoclonal antibodies are described. These include the hybridoma technique, based on the fusion of antibody-producing human B lymphocytes with either mouse or human myeloma or lymphoblastoid cells; the EBV immortalization technique, based on the use of Epstein-Barr virus (EBV) to 'immortalize' antigen-specific human B lymphocytes; and the EBV-hybridoma technique, based on a combination of the first two methods. The EBV-hybridoma system retains the advantageous features of the other two systems while overcoming their pitfalls and may be the current method of choice for producing human monoclonal antibodies with a defined specificity.
Mol Cell Biochem 1984 Jun
PMID:Human monoclonal antibodies. 608 21

In order to provide a framework for understanding the molecular biology of Epstein-Barr virus (EBV), we are determining the DNA sequence of the virus and studying the organization of genes on the viral genome. In this paper we report the DNA sequence of the EcoRI C fragment of the B95-8 strain of EBV. The large (approximately 13.6 kb) deletion in this strain has been located by comparison with the DNA sequence of EBV isolated from Raji cells. The sequence has been analysed for possible protein coding regions and transcriptional control sites. At least eight large open reading frames are found, some of them associated with canonical promoter and polyadenylation sequences. The sequences of some of the encoded proteins suggest that they are membrane proteins. It is known that antibodies to major membrane glycoproteins of EBV can neutralize infection in tissue culture. A possible relationship between some of the encoded proteins and the major membrane glycoproteins of the virus is discussed.
Mol Biol Med 1983 Jul
PMID:Sequence analysis of the 17,166 base-pair EcoRI fragment C of B95-8 Epstein-Barr virus. 609 25

The DNA sequence of the BamHI fragments B and the contiguous portion of G extending from the BamHI site to the EcoRI site of the B95-8 strain of Epstein-Barr virus has been determined. The sequence has been analysed for possible protein coding regions and transcriptional control sites. At least eight large open reading frames were found. Several RNA polymerase II promoters have been identified in the BamHI-B fragments. RNAs transcribed from these promoters are substantially induced by treatment of B95-8 cells with 12-O-tetradecanoylphorbol-13-acetate. Phosphonoacetic acid reversed the stimulatory effect of 12-O-tetradecanoylphorbol-13-acetate on the transcription of these RNAs indicating that they are late RNAs.
Mol Biol Med 1983 Oct
PMID:DNA sequence and transcription of the BamHI fragment B region of B95-8 Epstein-Barr virus. 609 53

An analysis of the approximately 12,440 base-pair sequence of the EcoRI Dhet fragment isolated from the circular episomal form of the B95-8 strain of Epstein-Barr virus is presented. This fragment contains the covalently joined ends of the intracellular episomal form of the molecule. In the viral capsid the DNA is linear and the joining is mediated via the terminal repeated DNA. Four copies of tandem repeated DNA were present in this clone, three with a repeat size of 538 and one of 523. The positions of a number of possible protein coding regions and transcription signals are discussed. In particular a possible spliced coding region for an approximately 45,000 Mr protein expressed in latently infected transformed cells is proposed. The predicted protein sequence contains hydrophobic regions separated by charged amino acids reminiscent of a membrane protein.
Mol Biol Med 1983 Nov
PMID:DNA sequence analysis of the EcoRI Dhet fragment of B95-8 Epstein-Barr virus containing the terminal repeat sequences. 609 55

The translational efficiency of cMyc mRNAs was assessed in a variety of cell lines: HeLa cells and Epstein-Barr virus-transformed lymphocytes, both of which contain only the germ line cMyc allele; Daudi, a Burkitt cell line containing a translocated cMyc gene with no apparent alteration; and P3HR-1, a Burkitt line in which the 5' end of the translocated cMyc gene has been altered by the chromosomal translocation. Translational efficiency was inferred by measuring the number of ribosomes associated with the cMyc mRNA, using a procedure by which individual polysomal fractions were analyzed by blot hybridization. Since polysome size is a function of the length of the translated sequence as well as the rate of initiation of protein synthesis, we also determined the number of ribosomes associated with a control mRNA (alpha tubulin) which codes for a protein of similar size to cMyc. We found that the cMyc mRNA was associated with a number of ribosomes comparable to that associated with alpha tubulin mRNA in all the cell lines tested.
Mol Cell Biol 1984 Oct
PMID:Translational efficiency of cMyc mRNA in Burkitt lymphoma cells. 609 51

Naturally developing human antibodies to the Epstein-Barr nuclear antigen recognize synthetic peptides containing sequences from the unusual glycine-alanine region of this protein. We tested antibody binding to a series of peptides of from five to 20 amino acids in length. Peptides as small as seven amino acids could bind but optimal results required chain lengths of 15. Binding was extremely sensitive to small changes in the length and sequence of the peptide, and also to the temp of the reaction. The changes can be ascribed to two factors: (1) deletion of the site of antigen binding and (2) loss of peptide secondary structure.
Mol Immunol 1984 Nov
PMID:The immune response to Epstein-Barr nuclear antigen: conformational and structural features of antibody binding to synthetic peptides. 609

Three new Epstein-Barr virus DNA populations have been isolated from the recently established Burkitt's lymphoma-derived cell lines, LY47, LY91 and BL8. Each of these lines carries one of the specific chromosome translocations associated with Burkitt's lymphoma but few if any other chromosomal abnormalities. An outline of their molecular organization, as determined by restriction enzyme analysis, is presented. Two of the isolates, LY47 and BL8, give patterns broadly similar to Epstein-Barr virus DNA molecules studied to date. The third, LY91, shows a highly unusual molecular organization, in particular within BamHI subfragments of the EcoRI A fragment, indicative of the presence of a major defective molecular species within this line. All three cell lines produce virions that are capable of transforming immature B-lymphocytes.
Mol Biol Med 1984 Apr
PMID:Molecular characterization of the Epstein-Barr virus DNA in three new Burkitt's lymphoma-derived cell lines. 609 62

Adenovirus (Ad) serotypes 2 and 5 synthesize large amounts of two low molecular weight RNAs designated virus-associated (VA) 1 and 2. Recently, genetic and biochemical approaches have been used to show that Ad2 VA1 RNA is required for efficient translation of viral mRNAs produced at late times after infection. Primate cells harboring the Epstein-Barr virus genome (EBV) synthesize large amounts of two low molecular weight RNAs: EBER1 and EBER2. Striking similarities of gene organization have been noted between the genes coding for Ad5 VA RNAs and the EBV EBERs [Rosa, M. D., Gottlieb, E., Lerner, M. R. & Steitz, J. A. (1981) Mol. Cell. Biol. 1, 785-796]. To examine whether the EBRs can functionally substitute for the VA RNAs for the lytic growth of Ad5, we have constructed an Ad5 substitution mutant in which the two VA RNA genes have been deleted and replaced by an EBV DNA segment coding for the two EBERs. The resulting Ad5 mutant synthesizes large amounts of the EBERs and is viable. Thus, two small RNAs of EBV origin, having primary and secondary structures different from those of the VA RNAs, can functionally substitute for the VA RNAs in the lytic growth of Ad5. These results are discussed in the context of mechanism of function of the VA RNAs.
...
PMID:Two small RNAs encoded by Epstein-Barr virus can functionally substitute for the virus-associated RNAs in the lytic growth of adenovirus 5. 630 49

An OKT3+T4+T8-DR+ lymphocyte line was developed from an Epstein-Barr virus (EBV) seropositive individual by repeated stimulation in vitro with autologous EBV-infected B cells. The T cell population designated E-44 was carried for eight months in the presence of Interleukin-2 and was repeatedly tested for cytotoxicity, proliferation and lymphokine production in response to the autologous and a panel of allogenic B cells. The E-44 cells lysed the autologous lymphoblastoid cell lines (LCL) and allogenic B cell lines sharing the DR6.1 major histocompatibility complex antigen with the lymphocyte donors. The EBV genome-negative lymphoma line BJAB and its two, infected in vitro, EBV-positive sublines were lysed with similar efficiencies. Autologous Staphylococcus aureus protein A (Prot-A) induced B, but not Phytohaemagglutinin (PHA)-induced T blasts were also lysed. It is likely that E-44 recognized an antigenic component derived from the fetal calf serum in association with class II determinants expressed on the B cells. Preincubation of E-44 cells with saturating amounts of OKT3 and Leu3a monoclonal antibodies abrogated the lytic effect on the autologous LCL. Cold target competition experiments demonstrated that, within, the population, the same cells reacted with the autologous Prot-A-induced blasts, the EBV-transformed LCL, and also with Daudi (an EBV genome-positive BL line). Although Daudi was the target which was lysed with the greatest efficiency, the avidity of interaction was highest with the autologous LCL because these cells competed best. Among the cells that were sensitive for the lytic effect, only the autologous LCL and Prot-A-induced B blasts triggered release of detectable amounts of Interleukin-2 and induced proliferation of the culture. The results suggest that the affinity of interaction with the target may be decisive for the triggering of the various T cell functions.
Mol Biol Med 1984 Aug
PMID:T lymphocyte culture established by repeated stimulation with the autologous lymphoblastoid line. MHC class II restricted interactions with B blasts. 644 79


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