Map position and nucleotide sequence of the gene for the large structural phosphoprotein of human cytomegalovirus

Jahn, Gerhard; Kouzarides, Tony; Mach, Michael; Scholl, B C; Plachter, Bodo; Traupe, B; Preddie, E.; Satchwell, Sandra C.; Fleckenstein, Bernhard; Barrell, Bart

doi:10.1128/jvi.61.5.1358-1367.1987

Cited by 103 publications

(47 citation statements)

References 45 publications

(48 reference statements)

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“…While neither of these properties clearly identifies this protein as being the MCMV homolog of the HCMV UL82 protein, they are both properties of matrix proteins of HCMV. Additionally, M83 is a true late protein, as are all known HCMV matrix components other than UL83 (10,16,26,40,44,63). These properties of M83 support its putative identification.…”

Section: Discussionmentioning

confidence: 74%

Identification, analysis, and evolutionary relationships of the putative murine cytomegalovirus homologs of the human cytomegalovirus UL82 (pp71) and UL83 (pp65) matrix phosphoproteins

Cranmer

Clark

Morello

et al. 1996

J Virol

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We have identified three open reading frames (ORFs) in murine cytomegalovirus (MCMV), designated M82, M83, and M84, which likely encode homologs of the human cytomegalovirus (HCMV) UL82 and UL83 matrix phosphoproteins. These ORFs, in the HindIII C fragment of MCMV, are colinear with the UL82, UL83, and UL84 ORFs of HCMV. M82 encodes a 598-amino-acid (aa) protein with homology to UL82, M83 encodes an 809-aa protein with homology to UL82 and UL83, and M84 encodes a 587-aa protein with homology to UL83 and UL84. Analysis of transcription by Northern (RNA) blotting indicated that the M82 and M83 ORFs are transcribed as 2.2-and 5-kb mRNAs, respectively, at 24 to 48 h postinfection (p.i.), while M84 is transcribed as a 6.9-kb mRNA only at 8 h p.i. All transcripts appear to terminate at the same position 3 of the M82 ORF. Of the products of the three ORFs, only M83 is strongly recognized by hyperimmune mouse serum. The M83 protein is a virion-associated phosphoprotein with an apparent molecular mass of 125 kDa. In MCMV-infected cells, it is detectable by Western blotting (immunoblotting) only at 48 h p.i. in the absence of phosphonoacetic acid, consistent with late gene expression. The M83 ORF is also expressed at high levels in cells infected by a recombinant vaccinia virus and yields a protein which is serologically cross-reactive and comigrates with the authentic MCMV protein in sodium dodecyl sulfate-polyacrylamide gel electrophoresis.

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Section: Discussionmentioning

confidence: 74%

Identification, analysis, and evolutionary relationships of the putative murine cytomegalovirus homologs of the human cytomegalovirus UL82 (pp71) and UL83 (pp65) matrix phosphoproteins

Cranmer

Clark

Morello

et al. 1996

J Virol

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“…(PR-AP), UL86 (MCP) UL99 (pp28), and UL115 (gL), as well as leaky late (␥ 1 ) expression of UL55 (gB), in addition to UL91 and UL92 themselves. It seems likely all of these act via UL87, given its relationship to gammaherpesvirus late TBP with specificity for TATT (48,49), the sequence that also characterizes HCMV true late promoters (27,29,33,37,39,41). In HSV-1, the late gene expression is also controlled by a small, TATA box-proximal region: however, regulation does not involve novel TATT sequences, at least based on the characterized ␥ 2 gC promoter (40).…”

Section: Discussionmentioning

confidence: 99%

“…True late gene regulation in HCMV (35,38,39), like HSV-1 (40) is controlled by a small, TATA box-proximal region. An unusual, TATT sequence predominates in HCMV ␥ 2 genes (27,29,33,37,39,41).…”

mentioning

confidence: 99%

Transcription of True Late (γ2) Cytomegalovirus Genes Requires UL92 Function That Is Conserved among Beta- and Gammaherpesviruses

Omoto

Mocarski

2014

J Virol

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Human cytomegalovirus-encoded UL92 plays an essential role in viral replication that has not been resolved. We show here that this gene controls the accumulation of true late (γ2) viral transcripts, a property shared with several other recently evaluated genes (UL79, UL87, UL91, and UL95) conserved among beta- and gammaherpesviruses. When the UL92 mutant virus was evaluated, function was fully complemented by either the natural protein or the homologous Rh127 protein from rhesus cytomegalovirus. N-terminal epitope-tagged UL92 protein is functional, follows complex early-late expression kinetics, and localizes in the nucleus within viral replication compartments. UL92 severely impacts the late (72-h postinfection) expression of nine genes encoding virion proteins (UL32, UL55, UL73, UL75, UL80, UL86, UL99, and UL115), as well as UL91 and itself, but does not influence the levels of UL44, UL82, or UL83 accumulation. Although viral DNA is made at normal levels, viral capsid accumulation in the nucleus is severely compromised in UL92 mutant virus-infected cells, and mature virions are not observed in the cytoplasm. Taken together, UL92 is a key regulator of late viral gene expression, apparently functioning with four other beta- or gammaherpesvirus gene products in a pattern that appears reminiscent of gene regulation in T4 DNA bacteriophage.

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“…Group 2 peptides were synthesized because they are present in other highly hydrophilic regions of ppl50 and are suggested to be immunodominant epitopes (3). Among group 1 peptides, two series of peptides were made with a leucine or a serine at position 1037, according to the published ppl50 nucleotide sequence (3) and the sequencing of the Dl recombinant protein (6, 12), respectively. on August 31, 2020 by guest http://jcm.asm.org/…”

Section: Discussionmentioning

confidence: 99%

Human cytomegalovirus structural proteins: immune reaction against pp150 synthetic peptides

et al. 1991

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In the present study, several peptides of the major structural antigen (ppl50) of human cytomegalovirus (CMV) have been chemically synthesized and tested by a modified slot blotting procedure for their ability to bind CMV-specific immunoglobulin G (IgG) and IgM present in human sera. The sequences of the peptides were deduced on the basis of either (i) their presence in a fusion protein already known to be frequently recognized by human antibody or (ii) their high content of hydrophilic amino acids as deduced from the published nucleotide sequence. An important IgM-binding epitope was found to be located in the last 38 amino acids at the carboxy terminus of the molecule. This region reacts with anti-CMV IgM present in the great majority (83.3%) of IgM-positive human sera, and adsorption experiments have shown that IgM titers to the entire ppl50 decrease 25 to 50% in most sera previously absorbed with this region. The overall results obtained endorse the continued synthesis of other sequences in order to define a group of peptides sensitive and specific enough to replace the virus and infected cells as an antigenic substrate in the serological evaluation of anti-CMV antibody.

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Map position and nucleotide sequence of the gene for the large structural phosphoprotein of human cytomegalovirus

Cited by 103 publications

References 45 publications

Identification, analysis, and evolutionary relationships of the putative murine cytomegalovirus homologs of the human cytomegalovirus UL82 (pp71) and UL83 (pp65) matrix phosphoproteins

Identification, analysis, and evolutionary relationships of the putative murine cytomegalovirus homologs of the human cytomegalovirus UL82 (pp71) and UL83 (pp65) matrix phosphoproteins

Transcription of True Late (γ2) Cytomegalovirus Genes Requires UL92 Function That Is Conserved among Beta- and Gammaherpesviruses

Human cytomegalovirus structural proteins: immune reaction against pp150 synthetic peptides

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