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Journal articles on the topic 'Human cytomegalovirus'

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Published: 4 June 2021
Last updated: 23 February 2023

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1

AbuBakar, S., I. Boldogh, and T. Albrecht. "Human cytomegalovirus." Archives of Virology 113-113, no. 3-4 (September 1990): 255–66. http://dx.doi.org/10.1007/bf01316678.

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2

Sutcliffe, Debra. "Human cytomegalovirus." British Journal of Midwifery 3, no. 12 (December 2, 1995): 665–68. http://dx.doi.org/10.12968/bjom.1995.3.12.665.

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3

Nachmani, Daphna, and Ofer Mandelboim. "Human cytomegalovirus miRNAs." Future Virology 6, no. 8 (August 2011): 909–16. http://dx.doi.org/10.2217/fvl.11.52.

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4

Britt, William J., and Michael Mach. "Human Cytomegalovirus Glycoproteins." Intervirology 39, no. 5-6 (1996): 401–12. http://dx.doi.org/10.1159/000150510.

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5

Stern-Ginossar, N., B. Weisburd, A. Michalski, V. T. K. Le, M. Y. Hein, S. X. Huang, M. Ma, et al. "Decoding Human Cytomegalovirus." Science 338, no. 6110 (November 22, 2012): 1088–93. http://dx.doi.org/10.1126/science.1227919.

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6

Sissons, J. G., and L. K. Borysiewicz. "Human cytomegalovirus infection." Thorax 44, no. 4 (April 1, 1989): 241–46. http://dx.doi.org/10.1136/thx.44.4.241.

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7

Landolfo, Santo, Marisa Gariglio, Giorgio Gribaudo, and David Lembo. "The human cytomegalovirus." Pharmacology & Therapeutics 98, no. 3 (June 2003): 269–97. http://dx.doi.org/10.1016/s0163-7258(03)00034-2.

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8

Revello, M. G., M. Furione, M. Zavattoni, and G. Gerna. "Human cytomegalovirus infection." Reviews in Medical Microbiology 5, no. 4 (October 1994): 265–76. http://dx.doi.org/10.1097/00013542-199410000-00006.

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9

Goodrum, Felicia, Katie Caviness, and Patricia Zagallo. "Human cytomegalovirus persistence." Cellular Microbiology 14, no. 5 (March 8, 2012): 644–55. http://dx.doi.org/10.1111/j.1462-5822.2012.01774.x.

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10

Strauss, Melvin. "Human cytomegalovirus labyrinthitis." American Journal of Otolaryngology 11, no. 5 (September 1990): 292–98. http://dx.doi.org/10.1016/0196-0709(90)90057-3.

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11

Heilbronn, R., I. Albrecht, S. Stephan, A. Bürkle, and H. zur Hausen. "Human cytomegalovirus induces JC virus DNA replication in human fibroblasts." Proceedings of the National Academy of Sciences 90, no. 23 (December 1, 1993): 11406–10. http://dx.doi.org/10.1073/pnas.90.23.11406.

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JC virus, a human papovavirus, is the causative agent of the demyelinating brain disease progressive multifocal leucoencephalopathy (PML). PML is a rare but fatal disease which develops as a complication of severe immunosuppression. Latent JC virus is harbored by many asymptomatic carriers and is transiently reactivated from the latent state upon immunosuppression. JC virus has a very restricted host range, with human glial cells being the only tissue in which it can replicate at reasonable efficiency. Evidence that latent human cytomegalovirus is harbored in the kidney similar to latent JC virus led to the speculation that during episodes of impaired immunocompetence, cytomegalovirus might serve as helper virus for JC virus replication in otherwise nonpermissive cells. We show here that cytomegalovirus infection indeed leads to considerable JC virus DNA replication in cultured human fibroblasts that are nonpermissive for the replication of JC virus alone. Cytomegalovirus-mediated JC virus replication is dependent on the JC virus origin of replication and T antigen. Ganciclovir-induced inhibition of cytomegalovirus replication is associated with a concomitant inhibition of JC virus replication. These results suggest that reactivation of cytomegalovirus during episodes of immunosuppression might lead to activation of latent JC virus, which would enhance the probability of subsequent PML development. Ganciclovir-induced repression of both cytomegalovirus and JC virus replication may form the rational basis for the development of an approach toward treatment or prevention of PML.
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12

Spoden, Gilles A., Katrin Besold, Steffi Krauter, Bodo Plachter, Nils Hanik, Andreas F. M. Kilbinger, Carsten Lambert, and Luise Florin. "Polyethylenimine Is a Strong Inhibitor of Human Papillomavirus and Cytomegalovirus Infection." Antimicrobial Agents and Chemotherapy 56, no. 1 (October 3, 2011): 75–82. http://dx.doi.org/10.1128/aac.05147-11.

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ABSTRACTPolyethylenimines are cationic polymers with potential as delivery vectors in gene therapy and with proven antimicrobial activity. However, the antiviral activity of polyethylenimines has not been addressed in detail thus far. We have studied the inhibitory effects of a linear 25-kDa polyethylenimine on infections with human papillomaviruses and human cytomegaloviruses. Preincubation of cells with polyethylenimine blocked primary attachment of both viruses to cells, resulting in a significant reduction of infection. In addition, the dissemination of human cytomegalovirus in culture cells was efficiently reduced by recurrent administration of polyethylenimine. Polyethylenimine concentrations required for inhibition of human papillomavirus and cytomegalovirus did not cause any cytotoxic effects. Polyethylenimines and their derivatives may thus be attractive molecules for the development of antiviral microbicides.
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13

McCormick, A. Louise, Christopher D. Meiering, Geoffrey B. Smith, and Edward S. Mocarski. "Mitochondrial Cell Death Suppressors Carried by Human and Murine Cytomegalovirus Confer Resistance to Proteasome Inhibitor-Induced Apoptosis." Journal of Virology 79, no. 19 (October 1, 2005): 12205–17. http://dx.doi.org/10.1128/jvi.79.19.12205-12217.2005.

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ABSTRACT Human cytomegalovirus carries a mitochondria-localized inhibitor of apoptosis (vMIA) that is conserved in primate cytomegaloviruses. We find that inactivating mutations within UL37x1, which encodes vMIA, do not substantially affect replication in TownevarATCC (Towne-BAC), a virus that carries a functional copy of the betaherpesvirus-conserved viral inhibitor of caspase 8 activation, the UL36 gene product. In Towne-BAC infection, vMIA reduces susceptibility of infected cells to intrinsic death induced by proteasome inhibition. vMIA is sufficient to confer resistance to proteasome inhibition when expressed independent of viral infection. Murine cytomegalovirus m38.5, whose position in the viral genome is analogous to UL37x1, exhibits mitochondrial association and functions in much the same manner as vMIA in inhibiting intrinsic cell death. This work suggests a common role for vMIA in rodent and primate cytomegaloviruses, modulating the threshold of virus-infected cells to intrinsic cell death.
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14

Smith, J. A., and G. S. Pari. "Human cytomegalovirus UL102 gene." Journal of virology 69, no. 3 (1995): 1734–40. http://dx.doi.org/10.1128/jvi.69.3.1734-1740.1995.

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15

Spaete, R. R., R. C. Gehrz, and M. P. Landini. "Human cytomegalovirus structural proteins." Journal of General Virology 75, no. 12 (December 1, 1994): 3287–308. http://dx.doi.org/10.1099/0022-1317-75-12-3287.

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16

Sissons, J. G. P., A. J. Carmichael, N. McKinney, J. H. Sinclair, and M. R. Wills. "Human cytomegalovirus and immunopathology." Springer Seminars in Immunopathology 24, no. 2 (November 1, 2002): 169–85. http://dx.doi.org/10.1007/s00281-002-0104-0.

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17

Rios, S. L., V. G. Baracho, KB A. Oliveira, and Prof Luiz Vicente Rizzo. "Therapies for human cytomegalovirus." Expert Opinion on Therapeutic Patents 17, no. 4 (April 2007): 407–18. http://dx.doi.org/10.1517/13543776.17.4.407.

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18

Stower, Hannah. "Human cytomegalovirus protein repertoire." Nature Reviews Genetics 14, no. 1 (December 18, 2012): 7. http://dx.doi.org/10.1038/nrg3401.

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19

Britt, William J., and Suresh Boppana. "Human cytomegalovirus virion proteins." Human Immunology 65, no. 5 (May 2004): 395–402. http://dx.doi.org/10.1016/j.humimm.2004.02.008.

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20

Pawelec, Graham, Evelyna Derhovanessian, Anis Larbi, Jan Strindhall, and Anders Wikby. "Cytomegalovirus and human immunosenescence." Reviews in Medical Virology 19, no. 1 (November 26, 2008): 47–56. http://dx.doi.org/10.1002/rmv.598.

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21

Foung, Steven K. H., Susan Perkins, Peggy Bradshaw, Judy Rowe, Linda B. Rabin, Gregory R. Reyes, and Evelyne T. Lennette. "Human Monoclonal Antibodies to Human Cytomegalovirus." Journal of Infectious Diseases 159, no. 3 (March 1989): 436–43. http://dx.doi.org/10.1093/infdis/159.3.436.

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22

Masuho, Y., Y. I. Matsumoto, T. Sugano, S. Fujinaga, and Y. Minamishima. "Human Monoclonal Antibodies Neutralizing Human Cytomegalovirus." Journal of General Virology 68, no. 5 (May 1, 1987): 1457–61. http://dx.doi.org/10.1099/0022-1317-68-5-1457.

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23

Wachsman, M., F. M. Hamzeh, H. Saito, and P. S. Lietman. "Anticytomegaloviral activity of methotrexate associated with preferential accumulation of drug by cytomegalovirus-infected cells." Antimicrobial Agents and Chemotherapy 40, no. 2 (February 1996): 433–36. http://dx.doi.org/10.1128/aac.40.2.433.

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We extend the observation that inhibitors of pyrimidine biosynthesis are active against human cytomegalovirus by demonstrating that methotrexate (MTX) has preferential activity against cytomegalovirus replication. The 50% and 90% inhibitory concentrations of MTX for inhibition of cytomegaloviral DNA replication at 3 days postinfection in MRC-5 cells were 0.05 and 0.2 microM, respectively. No cell toxicity was observed in uninfected confluent cells at the highest concentration tested (1 microM). Under similar conditions (3 days of treatment with 0.2 microM MTX), intracellular dTTP pools were diminished in cytomegalovirus-infected cells (87% decrease relative to untreated infected cells, P < 0.001) but were not reduced in uninfected cells. A potential explanation for the preferential antiviral effect of MTX was that human cytomegalovirus-infected cells preferentially accumulated MTX. Increased intracellular accumulation and increased polyglutamation of MTX were observed in cytomegalovirus-infected cells compared with uninfected cells. Increased uptake of [3H]MTX by cytomegalovirus-infected cells was first observed at 48 h postinfection, with threefold-higher accumulation within infected cells. By 96 h, accumulation had increased to approximately fourfold in comparison with uninfected cells. The uptake of [3H]MTX was saturable and was blocked by addition of unlabelled MTX. Intracellular MTX in infected cells was almost entirely in the polyglutamated form, as demonstrated by thin-layer chromatography, whereas intracellular MTX was almost exclusively in the parent form in uninfected cells.
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24

Halwachs-Baumann, G., M. Wilders-Truschnig, G. Desoye, T. Hahn, L. Kiesel, K. Klingel, P. Rieger, G. Jahn, and C. Sinzger. "Human Trophoblast Cells Are Permissive to the Complete Replicative Cycle of Human Cytomegalovirus." Journal of Virology 72, no. 9 (September 1, 1998): 7598–602. http://dx.doi.org/10.1128/jvi.72.9.7598-7602.1998.

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ABSTRACT Human trophoblast cells were permissively infected by human cytomegalovirus. The kinetics of viral immediate-early, early, and late gene expression was clearly delayed compared to that in fibroblasts. Productive infection was unequivocally proven by the detection of virion particles, infectious virus in trophoblast culture supernatant, and cell-to-cell spread of cytomegalovirus from infected trophoblasts to uninfected fibroblasts. These observations indicate that infected trophoblasts may be involved in maternofetal transmission of human cytomegalovirus.
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25

Flores-Martínez, Yulia Alejandra, Vu Thuy Khanh Le-Trilling, and Mirko Trilling. "Nedd8-Activating Enzyme Is a Druggable Host Dependency Factor of Human and Mouse Cytomegalovirus." Viruses 13, no. 8 (August 14, 2021): 1610. http://dx.doi.org/10.3390/v13081610.

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Human cytomegalovirus causes diseases in individuals with insufficient immunity. Cytomegaloviruses exploit the ubiquitin proteasome pathway to manipulate the proteome of infected cells. The proteasome degrades ubiquitinated proteins. The family of cullin RING ubiquitin ligases (CRL) regulates the stability of numerous important proteins. If the cullin within the CRL is modified with Nedd8 (“neddylated”), the CRL is enzymatically active, while CRLs lacking Nedd8 modifications are inactive. The Nedd8-activating enzyme (NAE) is indispensable for neddylation. By binding to NAE and inhibiting neddylation, the drug MLN4924 (pevonedistat) causes CRL inactivation and stabilization of CRL target proteins. We showed that MLN4924 elicits potent antiviral activity against cytomegaloviruses, suggesting that NAE might be a druggable host dependency factor (HDF). However, MLN4924 is a nucleoside analog related to AMP, and the antiviral activity of MLN4924 may have been influenced by off-target effects in addition to NAE inhibition. To test if NAE is indeed an HDF, we assessed the novel NAE inhibitor TAS4464 and observed potent antiviral activity against mouse and human cytomegalovirus. Additionally, we raised an MLN4924-resistant cell clone and showed that MLN4924 as well as TAS4464 lose their antiviral activity in these cells. Our results indicate that NAE, the neddylation process, and CRLs are druggable HDFs of cytomegaloviruses.
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26

Michaels, Marian G., Donald J. Alcendor, Kirsten St. George, Charles R. Rinaldo, Jr., Garth D. Ehrlich, Michael J. Becich, and Gary S. Hayward. "Distinguishing Baboon Cytomegalovirus from Human Cytomegalovirus: Importance for Xenotransplantation." Journal of Infectious Diseases 176, no. 6 (December 1997): 1476–83. http://dx.doi.org/10.1086/514144.

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27

Grey, Finn, Andy Antoniewicz, Edwards Allen, Julie Saugstad, Andy McShea, James C. Carrington, and Jay Nelson. "Identification and Characterization of Human Cytomegalovirus-Encoded MicroRNAs." Journal of Virology 79, no. 18 (September 15, 2005): 12095–99. http://dx.doi.org/10.1128/jvi.79.18.12095-12099.2005.

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ABSTRACT MicroRNAs (miRNAs) are an extensive class of noncoding genes that regulate gene expression through posttranscriptional repression. Given the potential for large viral genomes to encode these transcripts, we examined the human cytomegalovirus AD169 genome for miRNAs using a bioinformatics approach. We identified 406 potential stem-loops, of which 110 were conserved between chimpanzee cytomegalovirus and several strains of human cytomegalovirus. Of these conserved stem-loops, 13 exhibited a significant score using the MiRscan algorithm. Examination of total RNA from human cytomegalovirus-infected cells demonstrated that 5 of the 13 predicted miRNAs were expressed during infection. These studies demonstrate that human cytomegalovirus encodes multiple conserved miRNAs and suggest that human cytomegalovirus may utilize an miRNA strategy to regulate cellular and viral gene function.
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28

MO, Mahjoob. "Seroprevalence of Human Cytomegalovirus Infection among HIV Patients in Khartoum State." Open Access Journal of Microbiology & Biotechnology 4, no. 2 (2019): 1–4. http://dx.doi.org/10.23880/oajmb-16000145.

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Background: Human Cytomegalovirus (HCMV) is one of the opportunistic infections associated with significantly high morbidity and mortality among patients living with immunodeficiency syndrome. CMV has been reported to enhance HIV replication and accelerate the progre ssion of HIV infection to AIDS. Aim: The aim of this study was to determine the prevalence of HCMV among HIV patients in Khartoum State, Sudan, during the period April to July 2018. Methods: The study was carried out in Khartoum State, Sudan. A total of 9 2 HIV sero - positive cases were included. HCMV IgG and IgM antibodies were detected using Enzyme Linked Immune Sorbent Assay. Results: Among 92 HIV positive samples, 91 (99%) were found positive for HCMV - IgG while 3 samples (3.2%) were positive for HCMV - I gM. Conclusion: In Sudan, the existence of HCMV in patients with HIV infection was confirmed by using ELISA. These findings indicate that CMV is hyper-endemic in HIV seropositive patients in Khartoum, Sudan.
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29

Davison, Andrew J., Parvis Akter, Charles Cunningham, Aidan Dolan, Clare Addison, Derrick J. Dargan, Aycan F. Hassan-Walker, Vincent C. Emery, Paul D. Griffiths, and Gavin W. G. Wilkinson. "Homology between the human cytomegalovirus RL11 gene family and human adenovirus E3 genes." Journal of General Virology 84, no. 3 (March 1, 2003): 657–63. http://dx.doi.org/10.1099/vir.0.18856-0.

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A significant proportion of the human cytomegalovirus (HCMV) genome comprises 12 multigene families that probably arose by gene duplication. One, the RL11 family, contains 12 members, most of which are predicted to encode membrane glycoproteins. Comparisons of sequences near the left end of the genome in several HCMV strains revealed two adjacent open reading frames that potentially encode related proteins: RL6, which is hypervariable, and RL5A, which has not been recognized previously. These genes potentially encode a domain that is the hallmark of proteins encoded by the RL11 family, and thus constitute two new members. A homologous domain is also present in a subset of human adenovirus E3 membrane glycoproteins. Evolution of genes specifying the shared domain in cytomegaloviruses and adenoviruses is characterized by extensive divergence, gene duplication and selective sequence loss. These features prompt speculation about the roles of these genes in the two virus families.
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30

DUAN, Tao, Xiao-Fang WANG, Shu-Yuan XIAO, Shu-Yan GU, and Mi-Fang LIANG. "Recombinant Human IgG antibodies against Human Cytomegalovirus." Biomedical and Environmental Sciences 21, no. 5 (October 2008): 372–80. http://dx.doi.org/10.1016/s0895-3988(08)60057-4.

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31

Isomura, Hiroki. "Basic Research for Human Cytomegalovirus." Kitakanto Medical Journal 62, no. 4 (2012): 429–30. http://dx.doi.org/10.2974/kmj.62.429.

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32

Butler, Lynn M., Mensur Dzabic, Frank Bakker, Belghis Davoudi, Hannah Jeffery, Piotr Religa, Krzysztof Bojakowski, Koon-Chu Yaiw, Afsar Rahbar, and Cecilia Söderberg-Naucler. "Human Cytomegalovirus Inhibits Erythropoietin Production." Journal of the American Society of Nephrology 25, no. 8 (April 10, 2014): 1669–78. http://dx.doi.org/10.1681/asn.2013101125.

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33

Halenius, Anne, and Hartmut Hengel. "Human Cytomegalovirus and Autoimmune Disease." BioMed Research International 2014 (2014): 1–15. http://dx.doi.org/10.1155/2014/472978.

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Human cytomegalovirus (HCMV) represents a prototypic pathogenic member of theβ-subgroup of the herpesvirus family. A range of HCMV features like its lytic replication in multiple tissues, the lifelong persistence through periods of latency and intermitting reactivation, the extraordinary large proteome, and extensive manipulation of adaptive and innate immunity make HCMV a high profile candidate for involvement in autoimmune disorders. We surveyed the available literature for reports on HCMV association with onset or exacerbation of autoimmune disease. A causative linkage between HCMV and systemic lupus erythematosus (SLE), systemic sclerosis (SSc), diabetes mellitus type 1, and rheumatoid arthritis (RA) is suggested by the literature. However, a clear association of HCMV seroprevalence and disease could not be established, leaving the question open whether HCMV could play a coresponsible role for onset of disease. For convincing conclusions population-based prospective studies must be performed in the future. Specific immunopathogenic mechanisms by which HCMV could contribute to the course of autoimmune disease have been suggested, for example, molecular mimicry by UL94 in SSc and UL83/pp65 in SLE patients, as well as aggravation of joint inflammation by induction and expansion of CD4+/CD28− T-cells in RA patients. Further studies are needed to validate these findings and to lay the grounds for targeted therapeutic intervention.
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34

Plotkin, Stanley A. "Preventing Infection by Human Cytomegalovirus." Journal of Infectious Diseases 221, Supplement_1 (March 5, 2020): S123—S127. http://dx.doi.org/10.1093/infdis/jiz448.

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Abstract The way to a successful vaccine against human cytomegalovirus is hampered by the peculiar biology of this infection. However, some candidate vaccines have been shown to protect seronegative women and transplant recipients, and we should know soon whether they can prevent congenital infection.
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35

Rawlinson, W. D., and B. G. Barrell. "Spliced transcripts of human cytomegalovirus." Journal of Virology 67, no. 9 (1993): 5502–13. http://dx.doi.org/10.1128/jvi.67.9.5502-5513.1993.

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36

Zhu, Yuao, Lili Huang, and David G. Anders. "Human Cytomegalovirus oriLyt Sequence Requirements." Journal of Virology 72, no. 6 (June 1, 1998): 4989–96. http://dx.doi.org/10.1128/jvi.72.6.4989-4996.1998.

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ABSTRACT The mechanisms of action and regulation of the human cytomegalovirus (HCMV) lytic-phase DNA replicator, oriLyt, which spans more than 2 kbp in a structurally complex region near the middle of the unique long region (UL), are not understood. Because oriLyt is thought to be essential for promoting initiation of lytic DNA synthesis and may participate in regulating the switch between lytic and latent phases, we undertook a mutational study to better define its sequence requirements. Kanr gene cassette insertions located an oriLyt core region between nucleotides (nt) 91751 and 93299 that is necessary but not sufficient for replicator activity in transient assays. In contrast, insertions into auxiliary regions flanking either side of this core—also required for significant replicator activity—had little effect. To search for essential components within the core region, we made a series of overlapping, roughly 200-bp deletions, and qualitatively and quantitatively assessed the abilities of the resulting constructs to mediate replication. All but one of these deletions produced a significant (i.e., greater than twofold) loss of activity, arguing that sequences across this entire region contribute to replicator function. However, two particularly critical segments separated by a dispensable region, here called essential regions I and II, were identified. Within essential region I, which overlaps the previously identified early transcript SRT, two adjacent but nonoverlapping, roughly 200-bp deletions abolished detectable replication. No single element or motif from the left half of essential region I was found to be essential. Thus, essential region I probably promotes replication through the cooperation of multiple elements. However, four small deletions in the right half of essential region I, which included or lay adjacent to the conserved 31-nt oligopyrimidine tract (referred to as the Y block), abolished or virtually abolished oriLyt activity. Together, these results identify candidate oriLyt sequences within which molecular interactions essential for initiation oforiLyt-mediated DNA synthesis are likely to occur.
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37

Plotkin, Stanley A., and Suresh B. Boppana. "Vaccination against the human cytomegalovirus." Vaccine 37, no. 50 (November 2019): 7437–42. http://dx.doi.org/10.1016/j.vaccine.2018.02.089.

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38

Müller, Gerhard A., Norbert Braun, Hermann Einsele, and Claudia A. Müller. "Human Cytomegalovirus Infection in Transplantation." Nephron 64, no. 3 (1993): 343–53. http://dx.doi.org/10.1159/000187352.

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39

Yen-Lieberman, Belinda. "Diagnosis of human cytomegalovirus disease." Clinical Microbiology Newsletter 22, no. 14 (July 2000): 105–9. http://dx.doi.org/10.1016/s0196-4399(00)80001-x.

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40

Stevenson, K., and J. C. M. Macnab. "Cervical carcinoma and human cytomegalovirus." Biomedicine & Pharmacotherapy 43, no. 3 (January 1989): 173–76. http://dx.doi.org/10.1016/0753-3322(89)90211-4.

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41

Vanarsdall, Adam L., and David C. Johnson. "Human cytomegalovirus entry into cells." Current Opinion in Virology 2, no. 1 (February 2012): 37–42. http://dx.doi.org/10.1016/j.coviro.2012.01.001.

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42

Langhoff, Erik, and Robert E. Siegel. "Pneumonitis in human cytomegalovirus infection." Current Infectious Disease Reports 8, no. 3 (June 2006): 222–30. http://dx.doi.org/10.1007/s11908-006-0063-z.

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43

Kalejta, Robert F. "Tegument Proteins of Human Cytomegalovirus." Microbiology and Molecular Biology Reviews 72, no. 2 (June 2008): 249–65. http://dx.doi.org/10.1128/mmbr.00040-07.

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SUMMARY Human cytomegalovirus (HCMV) is a common, medically relevant human herpesvirus. The tegument layer of herpesvirus virions lies between the genome-containing capsids and the viral envelope. Proteins within the tegument layer of herpesviruses are released into the cell upon entry when the viral envelope fuses with the cell membrane. These proteins are fully formed and active and control viral entry, gene expression, and immune evasion. Most tegument proteins accumulate to high levels during later stages of infection, when they direct the assembly and egress of progeny virions. Thus, viral tegument proteins play critical roles at the very earliest and very last steps of the HCMV lytic replication cycle. This review summarizes HCMV tegument composition and structure as well as the known and speculated functions of viral tegument proteins. Important directions for future investigation and the challenges that lie ahead are identified and discussed.
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44

Machesky, Nicholas J., Guojuan Zhang, Bindu Raghavan, Pete Zimmerman, Samuel L. Kelly, Alfred H. Merrill, W. James Waldman, James R. Van Brocklyn, and Joanne Trgovcich. "Human Cytomegalovirus Regulates Bioactive Sphingolipids." Journal of Biological Chemistry 283, no. 38 (July 20, 2008): 26148–60. http://dx.doi.org/10.1074/jbc.m710181200.

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Gatherer, D., S. Seirafian, C. Cunningham, M. Holton, D. J. Dargan, K. Baluchova, R. D. Hector, et al. "High-resolution human cytomegalovirus transcriptome." Proceedings of the National Academy of Sciences 108, no. 49 (November 22, 2011): 19755–60. http://dx.doi.org/10.1073/pnas.1115861108.

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Popović, Milan, Katarina Smiljanić, Branislava Dobutović, Tatiana Syrovets, Thomas Simmet, and Esma R. Isenović. "Human cytomegalovirus infection and atherothrombosis." Journal of Thrombosis and Thrombolysis 33, no. 2 (December 13, 2011): 160–72. http://dx.doi.org/10.1007/s11239-011-0662-x.

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Grce, M., L. Magdić, and K. Pavelic. "Human cytomegalovirus in cervical cancerogenesis." Journal of Cancer Research and Clinical Oncology 121, S1 (January 1995): S19. http://dx.doi.org/10.1007/bf02559829.

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Poole, Emma, and John Sinclair. "Sleepless latency of human cytomegalovirus." Medical Microbiology and Immunology 204, no. 3 (March 14, 2015): 421–29. http://dx.doi.org/10.1007/s00430-015-0401-6.

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Wilkinson, Gavin W. G., Andrew J. Davison, Peter Tomasec, Ceri A. Fielding, Rebecca Aicheler, Isa Murrell, Sepher Seirafian, et al. "Human cytomegalovirus: taking the strain." Medical Microbiology and Immunology 204, no. 3 (April 17, 2015): 273–84. http://dx.doi.org/10.1007/s00430-015-0411-4.

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Michelson, Susan. "Consequences of human cytomegalovirus mimicry." Human Immunology 65, no. 5 (May 2004): 465–75. http://dx.doi.org/10.1016/j.humimm.2004.02.002.

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