Initiation of DNA replication in mammalian cells and its inhibition by reovirus infection

Hand, Roger; Tamm, Igor

doi:10.1016/0022-2836(74)90339-8

Cited by 100 publications

(51 citation statements)

References 21 publications

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“…The majority of virus stocks had particle/PFU ratios between 150 and 650, which is consistent with previously reported values for reovirus (18,29). Despite some sample-to-sample variation, only the ⌬IDR1 virus had a significantly higher particle/PFU ratio than WT virus (Student's t test, P Ͻ 0.01).…”

Section: Construction and Characterization Of Reovirus 1 Length And Fsupporting

confidence: 89%

Optimum Length and Flexibility of Reovirus Attachment Protein σ1 Are Required for Efficient Viral Infection

Bokiej

Ogden

Ikizler

et al. 2012

J Virol

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Reovirus attachment protein σ1 is an elongated trimer with head-and-tail morphology that engages cell-surface carbohydrate and junctional adhesion molecule A (JAM-A). The σ1 protein is comprised of three domains partitioned by two flexible linkers termed interdomain regions (IDRs). To determine the importance of σ1 length and flexibility at different stages of reovirus infection, we generated viruses with mutant σ1 molecules of altered length and flexibility and tested these viruses for the capacity to bind the cell surface, internalize, uncoat, induce protein synthesis, assemble, and replicate. We reduced the length of the α-helical σ1 tail to engineer mutants L1 and L2 and deleted midpoint and head-proximal σ1 IDRs to generate ΔIDR1 and ΔIDR2 mutant viruses, respectively. Decreasing length or flexibility of σ1 resulted in delayed reovirus infection and reduced viral titers. L1, L2, and ΔIDR1 viruses but not ΔIDR2 virus displayed reduced cell attachment, but altering σ1 length or flexibility did not diminish the efficiency of virion internalization. Replication of ΔIDR2 virus was hindered at a postdisassembly step. Differences between wild-type and σ1 mutant viruses were not attributable to alterations in σ1 folding, as determined by experiments assessing engagement of cell-surface carbohydrate and JAM-A by the length and IDR mutant viruses. However, ΔIDR1 virus harbored substantially less σ1 on the outer capsid. Taken together, these data suggest that σ1 length is required for reovirus binding to cells. In contrast, IDR1 is required for stable σ1 encapsidation, and IDR2 is required for a postuncoating replication step. Thus, the structural architecture of σ1 is required for efficient reovirus infection of host cells.

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Section: Construction and Characterization Of Reovirus 1 Length And Fsupporting

confidence: 89%

Optimum Length and Flexibility of Reovirus Attachment Protein σ1 Are Required for Efficient Viral Infection

Bokiej

Ogden

Ikizler

et al. 2012

J Virol

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“…Frequency histograms for intertrack distances were distinctly skewed to the right, to the values of longer intertrack distances (Fig. 2), as has been observed before for other cell systems (1,6,14). A similar distribution was also obtained in a previous analysis of the same BALB/c 3T3 cell line (20).…”

supporting

confidence: 86%

No activation of new initiation points for deoxyribonucleic acid replication in BALB/c 3T3 cells transformed by Kirsten sarcoma virus.

Oppenheim¹,

Horowitz²

1981

Mol. Cell. Biol.

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“…As described before (1,7,8,15), the distribution of intertrack distances was clearly not Gaussian (Fig. 3).…”

Section: Resultssupporting

confidence: 60%

Initiation points for cellular deoxyribonucleic acid replication in human lymphoid cells converted by Epstein-Barr virus.

Oppenheim¹,

Shlomai²,

Ben‐Bassat³

1981

Mol. Cell. Biol.

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Initiation of DNA replication in mammalian cells and its inhibition by reovirus infection

Cited by 100 publications

References 21 publications

Optimum Length and Flexibility of Reovirus Attachment Protein σ1 Are Required for Efficient Viral Infection

Optimum Length and Flexibility of Reovirus Attachment Protein σ1 Are Required for Efficient Viral Infection

No activation of new initiation points for deoxyribonucleic acid replication in BALB/c 3T3 cells transformed by Kirsten sarcoma virus.

Initiation points for cellular deoxyribonucleic acid replication in human lymphoid cells converted by Epstein-Barr virus.

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