Human cytomegalovirus structural proteins

Spaete, Richard R.; Gehrz, Richard C.; Landini, Maria Paola

doi:10.1099/0022-1317-75-12-3287

Cited by 78 publications

(60 citation statements)

References 74 publications

(128 reference statements)

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“…Nine of these HCMV-encoded polypeptides (UL38, UL50, UL71, UL79, UL93, UL96, UL102, US23, and US24) are required for efficient virus growth in cultured fibroblasts (12,43). UL4, UL23, UL53, UL56, UL98a, and US28 have previously been reported to be associated with HCMV particles (1,6,7,10,37). Although peptides corresponding to these viral proteins were detected in our study, the peptides failed to meet the criteria, as outlined in Materials and Methods, for inclusion in our database.…”

Section: Resultsmentioning

confidence: 99%

Identification of Proteins in Human Cytomegalovirus (HCMV) Particles: the HCMV Proteome

Varnum

Streblow

Monroe

et al. 2004

J Virol

529

350

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Human cytomegalovirus (HCMV), a member of the herpesvirus family, is a large complex enveloped virus composed of both viral and cellular gene products. While the sequence of the HCMV genome has been known for over a decade, the full set of viral and cellular proteins that compose the HCMV virion are unknown. To approach this problem we have utilized gel-free two-dimensional capillary liquid chromatography-tandem mass spectrometry (MS/MS) and Fourier transform ion cyclotron resonance MS to identify and determine the relative abundances of viral and cellular proteins in purified HCMV AD169 virions and dense bodies. Analysis of the proteins from purified HCMV virion preparations has indicated that the particle contains significantly more viral proteins than previously known. In this study, we identified 71 HCMV-encoded proteins that included 12 proteins encoded by known viral open reading frames (ORFs) previously not associated with virions and 12 proteins from novel viral ORFs. Analysis of the relative abundance of HCMV proteins indicated that the predominant virion protein was the pp65 tegument protein and that gM rather than gB was the most abundant glycoprotein. We have also identified over 70 host cellular proteins in HCMV virions, which include cellular structural proteins, enzymes, and chaperones. In addition, analysis of HCMV dense bodies indicated that these viral particles are composed of 29 viral proteins with a reduced quantity of cellular proteins in comparison to HCMV virions. This study provides the first comprehensive quantitative analysis of the viral and cellular proteins that compose infectious particles of a large complex virus.

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Section: Resultsmentioning

confidence: 99%

Identification of Proteins in Human Cytomegalovirus (HCMV) Particles: the HCMV Proteome

Varnum

Streblow

Monroe

et al. 2004

J Virol

529

350

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“…This could be due to either weaker antigen presentation on the CMV-infected fibroblast cells, possibly by the mechanism of class I molecule down-regulation, [40][41][42][43][44] or the same T-cell repertoires being reactive with some of the 5 peptides. To test these possibilities, we established T-cell clones from limiting dilution culture of the bulk CTL line stimulated with anti-CD3 mAb, appropriate feeder cells, and IL-2.…”

Section: Recognition Of the 4 Pp65 Peptides By Single Cmv-specific CDmentioning

confidence: 99%

Efficient identification of HLA-A*2402–restricted cytomegalovirus-specific CD8+ T-cell epitopes by a computer algorithm and an enzyme-linked immunospot assay

Kuzushima

Hayashi

Kimura

et al. 2001

Blood

146

149

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“…Little is known about the organization and function of the HCMV tegument, although a large number of proteins have been assigned to it (Spaete et al, 1994). There is evidence that the tegument proteins of the input virus play an important role in viral gene regulation and modification of host cell metabolism during the initial stages of infection, but no experimental data are available for a possible function in the maturation or transport of virions.…”

Section: Introductionmentioning

confidence: 99%

Human cytomegalovirus late-phase maturation is blocked by stably expressed UL32 antisense mRNA in astrocytoma cells.

Meyer¹,

Ripalti

Landini³

et al. 1997

Journal of General Virology

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Human cytomegalovirus (HCMV) open reading frame UL32 codes for the basic phosphoprotein pp150 (ppUL32), an abundant constituent of the virion tegument. In order to study its potential role in the assembly and/or transport of progeny particles, astrocytoma cell lines (U373MG) were generated, stably expressing a 2n1 kb 5h fragment of UL32 in antisense orientation under the control of the HCMV major immediate early promoter. The steady-state level of the UL32 sense mRNA and pp150 synthesis were strongly reduced in infected antisense cell lines. Neither immediate early and early gene expression, nor viral DNA replication, was inhibited ; the expression of the late gene product gB (gpUL55) was also reduced, but mainly at the level of translation. Control experiments indicated that this dif-

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Human cytomegalovirus structural proteins

Cited by 78 publications

References 74 publications

Identification of Proteins in Human Cytomegalovirus (HCMV) Particles: the HCMV Proteome

Identification of Proteins in Human Cytomegalovirus (HCMV) Particles: the HCMV Proteome

Efficient identification of HLA-A*2402–restricted cytomegalovirus-specific CD8+ T-cell epitopes by a computer algorithm and an enzyme-linked immunospot assay

Human cytomegalovirus late-phase maturation is blocked by stably expressed UL32 antisense mRNA in astrocytoma cells.

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