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Results: 7

1.
Fig 7

Fig 7. From: Reduced Infectivity of Adenovirus Type 5 Particles and Degradation of Entering Viral Genomes Associated with Incomplete Processing of the Preterminal Protein.

Ad5 and Hr6 genomes do not associate with late endosomes. HFFs were infected with 100 PFU/cell Ad5 or Hr6 for the periods indicated or mock infected (M), and viral genomes were visualized as described in the legend to Fig. 6. Late endosomes, some of which are indicated by orange arrows, and microtubules were stained with mouse anti-Rab and rat anti-β-tubulin-antibodies as described in Materials and Methods.

Sayuri E. Kato, et al. J Virol. 2012 December;86(24):13554-13565.
2.
Fig 6

Fig 6. From: Reduced Infectivity of Adenovirus Type 5 Particles and Degradation of Entering Viral Genomes Associated with Incomplete Processing of the Preterminal Protein.

Visualization of viral genomes during the initial period of Ad5 and Hr6 infection. HFFs were infected with 100 PFU/cell Ad5 or Hr6 for the periods indicated as described in Materials and Methods or mock infected (M), and viral genomes were visualized by immunofluorescence using an anti-protein VII polyclonal antibody (42). Nuclei were stained with DAPI (blue). Z stack projections of representative fields are shown.

Sayuri E. Kato, et al. J Virol. 2012 December;86(24):13554-13565.
3.
Fig 4

Fig 4. From: Reduced Infectivity of Adenovirus Type 5 Particles and Degradation of Entering Viral Genomes Associated with Incomplete Processing of the Preterminal Protein.

Differences between the sequences of the Ad5 and Hr6 genomes. The horizontal line at the top represents the Ad5 genome in kilobase pairs. The fold coverage (FC) of sequence reads used to assemble the sequences of Ad5 and Hr6 DNA as described in Materials and Methods is indicated below. The black lines represent silent mutations detected in the Ad5 genome compared to the reference sequence or in Hr6 compared to the Ad5 sequence (see the text). The Hr6 mutations shown in blue and red indicate the previously described E1B 55-kDa coding sequence mutations (103) and newly discovered mutations in the preTP and fiber genes that introduce substitutions, respectively.

Sayuri E. Kato, et al. J Virol. 2012 December;86(24):13554-13565.
4.
Fig 1

Fig 1. From: Reduced Infectivity of Adenovirus Type 5 Particles and Degradation of Entering Viral Genomes Associated with Incomplete Processing of the Preterminal Protein.

Defects in the accumulation of viral DNA in proliferating SAECs, NHBECs, and HFFs infected with Hr6. Proliferating cells were infected with 30 PFU/cell Ad5 or Hr6, and DNA was isolated from cells harvested 2, 18, 24, and 30 h after infection. Viral DNA was quantified by real-time PCR as described in Materials and Methods. Relative concentrations of viral DNA were calculated as the increase in concentration at each time point over the value measured at 2 h after infection. Results represent the average of two independent experiments, and error bars represent the standard deviation.

Sayuri E. Kato, et al. J Virol. 2012 December;86(24):13554-13565.
5.
Fig 3

Fig 3. From: Reduced Infectivity of Adenovirus Type 5 Particles and Degradation of Entering Viral Genomes Associated with Incomplete Processing of the Preterminal Protein.

Intracellular degradation of viral DNA in Hr6-infected cells. (A) Cells were infected with 30 PFU/cell Ad5 or Hr6. DNA was purified from nuclei isolated from cells harvested at the times indicated, and viral DNA concentrations were determined by quantitative PCR as described in Materials and Methods. The values, which were corrected for the cellular GADPH DNA concentrations determined in parallel, are expressed relative to that measured at 2 h p.i. and represent the average of two independent experiments. Error bars show standard deviations. (B) The 2- to 18-h data from the experiments shown in panel B are replotted with an expanded y axis. (C) Cells were infected with equivalent numbers of Ad5 or Hr6 genomes, and intranuclear viral DNA concentrations were measured at the times indicated as described above for panel A. The corrected values, which are shown in arbitrary units, represent the mean of two independent experiments, and error bars show the standard deviations.

Sayuri E. Kato, et al. J Virol. 2012 December;86(24):13554-13565.
6.
Fig 5

Fig 5. From: Reduced Infectivity of Adenovirus Type 5 Particles and Degradation of Entering Viral Genomes Associated with Incomplete Processing of the Preterminal Protein.

Comparison of TP precursors in Ad5 and Hr6 virus particles. (A) The preTP is depicted to scale by the rectangle, with the precursor-specific and mature TP sequences shown in white and gray, respectively. The vertical arrows at the top indicate the sites at which preTP is cleaved by the viral L3 protease, and the arrow at the bottom shows the position of the G315V substitution in Hr6 preTP (77, 98). The epitopes recognized by the 5E3 (residues 184 to 200) and 11FH (residues 608 to 671) anti-preTP MAbs (99) are indicated by the bars below the protein. (B) Equal concentrations of proteins recovered from Ad5 and Hr6 particles, purified from equal number of infectious units as described in Materials and Methods, were examined by immunoblotting with the MAbs against protein V and preTP indicated at the top. 5E3 (long) indicates longer exposure of the blot shown to the left. The positions of molecular mass markers (sizes are in kilodaltons) are indicated at the left, and those of iTP, TP, and protein V are at the right.

Sayuri E. Kato, et al. J Virol. 2012 December;86(24):13554-13565.
7.
Fig 2

Fig 2. From: Reduced Infectivity of Adenovirus Type 5 Particles and Degradation of Entering Viral Genomes Associated with Incomplete Processing of the Preterminal Protein.

The E1B 55-kDa protein is not required for the synthesis of E2 proteins or the formation of replication centers. (A) Proliferating normal human cells were infected with Ad5 or Hr6 or mock infected and harvested after the periods indicated. Total cell lysates were examined by immunoblotting as described in Materials and Methods, with anti-E2 DBP MAb B6 and an anti-β-actin antibody. (B) Proliferating HFFs were infected with Ad5 or Hr6 or mock infected and processed for immunofluorescence 24 h after infection, as described in Materials and Methods. The viral E2 DBP was detected with the B6 antibody and cyanine 5-labeled anti-mouse IgG and is shown false colored in green. Nuclei were stained with DAPI (blue). Expanded, ring-like replication centers and dot-like structures are indicated by the orange and white arrows, respectively. These two types of replication centers were quantified in Ad5- and Hr6-infected HFFs (C) and NHBECs (D). Shortly after the onset of viral DNA synthesis, between 100 and 200 cells were analyzed for those in which the DBP was present only in small, dot-like structures (Small foci) or present in both these foci and large, ring-like structures (Large rings).

Sayuri E. Kato, et al. J Virol. 2012 December;86(24):13554-13565.

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