Inhibition of adenovirus DNA replication in vitro by autoimmune sera

Pruijn, Ger J. M.; Kusters, Hans G.; Meyling, F. H. J. Gmelig; Vliet, Peter C. van der

doi:10.1111/j.1432-1033.1986.tb09406.x

Cited by 11 publications

(14 citation statements)

References 31 publications

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“…In addition Pruijn et al [15] have reported that sera from patients suffering from autoimmune diseases can inhibit adenovirus DNA replication, suggesting a similar phenomenon. The similarities between viral proteins and myelin proteolipid may represent yet another case.…”

Section: Resultsmentioning

confidence: 90%

Analogous amino acid sequences in myelin proteolipid and viral proteins

1986

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Computer analysis of the intrinsic membrane protein, myelin proteolipid, shows strong sequence similarities between the putative extramembranc segments of the proteolipid protein and a number of viral proteins, several of which infect humans. These similarities are even more striking than those reported previously between viral proteins and the encephalitogenic myelin basic protein (MBP). These findings, along with other reports of molecular mimicry by viruses, suggest that immunological cross-reactions between virusinduced antibodies or T-cells and analogous antigenic determinants (epitopes) in myelin protcolipid could be involved in the pathophysiology of multiple sclerosis or post-infectious dcmyclinating syndromes. Proteolipid prolein Multiple sclerosis Viral protein Myelin basic protein Amino acid sequeneeSequence homology

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Section: Resultsmentioning

confidence: 90%

Analogous amino acid sequences in myelin proteolipid and viral proteins

1986

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“…We used an in vitro reconstituted replication assay to test whether vNFl and vNFlBD retain the functional properties of NFl purified from HeLa cells (Pruijn et al, 1986). 1, 5, 9, 13), 0.1 Id (lanes 2, 6, 10), 0.3 I1 (lanes 3, 7, 11, 14) and 1 Id (lanes 4, 8, 12, 15).…”

Section: Recombinant Vnf1 and Vnf1bd Stimulate Adenovirus Dna Replicamentioning

confidence: 99%

Amino-terminal domain of NF1 binds to DNA as a dimer and activates adenovirus DNA replication.

Gounari¹,

Francesco²,

Schmitt³

et al. 1990

The EMBO Journal

134

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NF1 is a DNA‐binding protein involved in initiation of adenovirus DNA replication as well as in modulating the rate of transcription initiation of genes containing the sequence TGGCA. We show here that recombinant NF1 expressed via vaccinia virus is transported into the nucleus and binds to its cognate sequences with the same specificity as NF1 purified from HeLa cells. Furthermore, the recombinant NF1 forms oligomers in solution and binds as a dimer to palindromic as well as half‐site sequences. NF1 expressed via vaccinia virus stimulates the initiation of adenovirus replication in vitro. The N‐terminal 240 amino acids of the protein are sufficient for full DNA‐binding activity as well as stimulation of adenovirus replication. By analysis of several NF1 mutants translated in vitro, we also define the minimal DNA‐binding domain and localize the region responsible for DNA binding on the N‐terminal and for oligomerization on the C‐terminal side of this domain.

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“…Mattaj and G.Tebb (pXLU2.5, containing a X laevis U2 snRNA gene and flanking sequences) (Mattaj et al, 1985 DEAE-cellulose and phosphocellulose chromatography as described (Pruijn et al, 1986a). During the purification procedure the NFE activity was monitored by the stimu- (Pruijn et al, 1986b). The reaction conditions for in vitro replication of Ad2 and Ad4 DNA were as described before (Pruijn et al, 1986a).…”

Section: The Different Affinity Of Nflli For Its Binding Sites In Ad2mentioning

confidence: 99%

Promoter and enhancer elements containing a conserved sequence motif are recognized by nuclear factor III, a protein stimulating adenovirus DNA replication.

et al. 1987

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Nuclear factor HI (NFI) is a protein from HeLa cells that stimulates the initiation of adenovirus type 2 (Ad2) DNA replication by binding to a specific nucleotide sequence in the orign, adjacent to the nuclear factor I recognition site. DNA sequences sharing a high degree of homology to the NFm binding site in Ad2 were found in a number of transcription regulatory elements, all containing the octanucleotide sequence ATGCAAAT. We have analysed the interaction between NF[II and the octamer-containing sequences in a histone H2B promoter, immunoglobulin light and heavy chain promoters, an immunoglobulin heavy chain enhancer, a U2 snRNA enhancer and the SV40 enhancer as well as Ad4. All sequences were recognized by NlI as indicated by gel retardation assays, DNase I footprinting and methylation protection experiments. A comparison of the relative binding affinities using competition assays indicated that mutations in the octanucleotide sequence reduced the binding affinity considerably. Small but signifit differences in affinity were also observed depending on the sequences bordering the conserved octanucleotide. The methylation protection patterns indicate that both major and minor groove contacts are involved in NFIII binding. The data suggest that NFEL could function both in adenovirus DNA replication and in the transcriptional control of several groups of genes sharing the octanucleotide sequence.

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Inhibition of adenovirus DNA replication in vitro by autoimmune sera

Cited by 11 publications

References 31 publications

Analogous amino acid sequences in myelin proteolipid and viral proteins

Analogous amino acid sequences in myelin proteolipid and viral proteins

Amino-terminal domain of NF1 binds to DNA as a dimer and activates adenovirus DNA replication.

Promoter and enhancer elements containing a conserved sequence motif are recognized by nuclear factor III, a protein stimulating adenovirus DNA replication.

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