Early Events of Virus-Cell Interaction in an Adenovirus System

Lonberg-Holm, K.; Philipson, Lennart

doi:10.1128/jvi.4.4.323-338.1969

Cited by 144 publications

(49 citation statements)

References 27 publications

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“…Previous results from DNAase I digestion studies suggested that the viral DNA, on entry into the nucleus, is released from its core proteins (11), a finding which should be reconsidered in the light of what is now known about protein-DNA interactions in chromatin. Even if the DNA is completely uncoated, it is unlikely that such a highly-charged molecule will exist free in the nucleus.…”

Section: Introductionmentioning

confidence: 96%

Parental adenovirus DNA accumulates in nucleosome-like structures in infected cells

Tate¹,

Philipson²

1979

Nucl Acids Res

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Micrococcal-nuclease digestion of adenovirus 2(ad 2) infected HeLa cell nuclei early after infection has been used to investigate the nucleoprotein nature of parental viral DNA. Viral DNA is more susceptible to nuclease digestion than cellular DNA. The pattern of digestion products changes as digestion proceeds from an indistinct pattern 1 hour post infection(pi) to a nucleosome-like pattern at 6 hours pi. The major differences between viral and cellular nucleoprotein products were i) a subnucleosome fraction from viral DNA and ii) the repeat size of DNA in viral nucleosomes was 165 base pairs and in cellular nucleosomes, 195 base pairs. Up to 50% viral DNA in nuclei 6 hours pi seems to be in nucleosome-like structures. Such patterns are not seen on digestion of partially-uncoated virus or isolated cores.

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Section: Introductionmentioning

confidence: 96%

Parental adenovirus DNA accumulates in nucleosome-like structures in infected cells

Tate¹,

Philipson²

1979

Nucl Acids Res

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“…During the early stages of infection, the virus undergoes stepwise dismantling, in part through the action of the virally encoded cysteine protease (Greber et al ., 1993; Russell and Kemp, 1995). Ultimately the viral nucleocapsid, still containing the hexon protein, docks at the nuclear pore complex (NPC) (Lonberg‐Holm and Philipson, 1969; Chardonnet and Dales, 1970; Greber et al ., 1993, 1997; Whittaker et al ., 2000). The particle undergoes further disassembly at the NPC, culminating with the translocation of the DNA into the nucleoplasm, where viral transcription and DNA replication take place (Greber et al ., 1993, 1996; Whittaker et al ., 2000).…”

Section: Introductionmentioning

confidence: 99%

Switch from capsid protein import to adenovirus assembly by cleavage of nuclear transport signals

et al. 2003

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Replication and assembly of adenovirus occurs in the nucleus of infected cells, requiring the nuclear import of all viral structural proteins. In this report we show that nuclear import of the major capsid protein, hexon, is mediated by protein VI, a structural protein located underneath the 12 vertices of the adenoviral capsid. Our data indicate that protein VI shuttles between the nucleus and the cytoplasm and that it links hexon to the nuclear import machinery via an importin a/b-dependent mechanism. Key nuclear import and export signals of protein VI are located in a short C-terminal segment, which is proteolytically removed during virus maturation. The removal of these C-terminal transport signals appears to trigger a functional transition in protein VI, from a role in supporting hexon nuclear import to a structural role in virus assembly.

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“…Penetration of the viral particles from endosomes into the cytosol occurs by acidtriggered lysis of the endosomal membrane, a reaction most likely mediated by the integrins and the penton base protein (Pastan et al, 1986;Wickham et al, 1994). Having thus entered the cytosol, the viral particles are next transported through the cytoplasm to the nuclear mem-brane, and attach to the cytosolic face of the nuclear pore complexes (Lonberg-Holm and Philipson, 1969;Chardonnet and Dales, 1970; Dales and Chardonnet, 1973;Greber et al, 1993). The DNA is released through the pore, and the viral capsid dissociates (Horwitz, 1990).…”

Section: Introductionmentioning

confidence: 99%

The role of the adenovirus protease on virus entry into cells.

et al. 1996

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Adenovirus uncoating is a stepwise process which culminates in the release of the viral DNA into the nucleus through the nuclear pore complexes and dissociation of the capsid. Using quantitative biochemical, immunochemical and morphological methods, we demonstrate that inhibitors of the cystine protease, L3/p23, located inside the capsid block the degradation of the capsid-stabilizing protein VI, and prevent virus uncoating at the nuclear membrane. There was no effect on virus internalization, fiber shedding and virus binding to the nuclear envelope. The viral enzyme (dormant in the extracellular virus) was activated by two separate signals, neither of which was sufficient alone; virus interaction with the integrin receptor (inhibited with RGD peptides) and re-entry of the virus particle into a reducing environment in the endosome or the cytosol. Incorrectly assembled mutant viruses that lack the functional protease (ts1) failed at releasing fibers and penetrating into the cytosol. The results indicated that L3/p23 is needed not only to assemble an entry-competent virus but also to disassemble the incoming virus. The EMBO Journal vol.15 no.8 pp.1766-1777, 1996 The role of the adenovirus protease in virus entry into cells Adenovirus uncoating is a stepwise process which culminates in the release of the viral DNA into the nucleus through the nuclear pore complexes and dissociation of the capsid. Using quantitative biochemical, immunochemical and morphological methods, we demonstrate that inhibitors of the cysteine protease, L3/ p23, located inside the capsid block the degradation of the capsid-stabilizing protein VI, and prevent virus uncoating at the nuclear membrane. There was no effect on virus internalization, fiber shedding and virus binding to the nuclear envelope. The viral enzyme (dormant in the extracellular virus) was activated by two separate signals, neither of which was sufficient alone; virus interaction with the integrin receptor (inhibited with RGD peptides) and re-entry of the virus particle into a reducing environment in the endosome or the cytosol. Incorrectly assembled mutant viruses that lack the functional protease (tsl) failed at releasing fibers and penetrating into the cytosol. The results indicated that L3/p23 is needed not only to assemble an entry-competent virus but also to disassemble the incoming virus.

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Early Events of Virus-Cell Interaction in an Adenovirus System

Cited by 144 publications

References 27 publications

Parental adenovirus DNA accumulates in nucleosome-like structures in infected cells

Parental adenovirus DNA accumulates in nucleosome-like structures in infected cells

Switch from capsid protein import to adenovirus assembly by cleavage of nuclear transport signals

The role of the adenovirus protease on virus entry into cells.

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