Adenovirus polypeptide IX revealed as capsid cement by difference images from electron microscopy and crystallography.

Furcinitti, Paul S.; Oostrum, Jan van; Burnett, Roger M.

doi:10.1002/j.1460-2075.1989.tb08528.x

Cited by 100 publications

(94 citation statements)

References 47 publications

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“…After endocytosis, the virus enters the cytosol encapsulated with in an endosomal membrane. As the endosome acidifies capsid proteins undergo conformational change (Seth, Willingham et al 1985;Furcinitti, van Oostrum et al 1989;Greber, Willetts et al 1993), where the virus partially disassembles, upsets the endosomal membrane and escapes into the cytoplasm (Graham, Smiley et al 1977).…”

Section: Infection Pathway Of Adenovirusmentioning

confidence: 99%

Evaluation of Cell-Penetrating Peptide/Adenovirus Particles for Transduction of CAR-Negative Cells

Nigatu

Vupputuri

Flynn

et al. 2013

Journal of Pharmaceutical Sciences

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Linear low‐density polyethylene (LLDPE), based on butene‐1 or hexene‐1, was irradiated with γ‐rays under vacuum or in the presence of air. The study focused on the influence of the dose rate and the γ‐dose on the thermal properties of LLDPE. Differential scanning calorimetry, thermogravimetric analysis (TGA), and TGA/FTIR techniques were used to address the thermal behavior as a result of γ‐irradiation. During this irradiation, competition between crosslinking and scission reactions, subsequent to oxidation reactions, occurred in the polymeric material, which strongly depends on the experimental conditions. A decrease of the crystallinity for γ‐irradiated samples was observed in particular for samples irradiated under vacuum. This observation may be explained by increased hindrance of segment mobility due to crosslinking reactions that prevent crystal growth. TGA investigations revealed an enhancement of the thermal stability for samples irradiated under vacuum but not for those irradiated in air. © 2006 Wiley Periodicals, Inc. J Appl Polym Sci 100: 2790–2795, 2006

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Section: Infection Pathway Of Adenovirusmentioning

confidence: 99%

Evaluation of Cell-Penetrating Peptide/Adenovirus Particles for Transduction of CAR-Negative Cells

Nigatu

Vupputuri

Flynn

et al. 2013

Journal of Pharmaceutical Sciences

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“…Protein VIII is located inside the shell and has a possible role in attaching the DNA to the capsid (Everitt et al, 1975;Stewart et al, 1993). The release of protein IX, a stabilizing factor important for the protection of the capsids against thermal denaturation (Colby and Shenk, 1981;Furcinitti et al, 1989), may weaken the capsid such that the DNA can finally escape from the shell.…”

Section: Other Dissociation Eventsmentioning

confidence: 99%

“…Each facette contains 12 hexons, the most abundant capsid protein (Burnett, 1985;Grutter and Franklin, 1974;Roberts et al, 1986). The facettes also contain three minor proteins, Illa, VIII, and IX (Furcinitti et al, 1989;Stewart et al, 1991Stewart et al, , 1993 that are thought to stabilize and link the facettes and connect them to the DNA. The peripentonal hexons are associated with protein VI, which links the inside surface of the capsid and the DNA (Stewart et al, 1993).…”

Section: Introductionmentioning

confidence: 99%

Stepwise dismantling of adenovirus 2 during entry into cells

Greber

Willetts

Webster

et al. 1993

Cell

745

726

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“…2A and 2A-like sequences have previously been used in biotechnology applications, but not in adenoviruses (reviewed by de Felipe et al, 2006). Protein IX is a small cement protein located between the hexons in the capsid of the adenovirus (Furcinitti et al, 1989). It is essential for the packaging of full-length viral genomes (Ghosh-Choudhury et al, 1987).…”

Section: Introductionmentioning

confidence: 99%

Expression of heterologous genes in oncolytic adenoviruses using picornaviral 2A sequences that trigger ribosome skipping

Funston

Kallioinen

Felipe

et al. 2008

Journal of General Virology

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Insertion of picornaviral 2A sequences into mRNAs causes ribosomes to skip formation of a peptide bond at the junction of the 2A and downstream sequences, leading to the production of two proteins from a single open reading frame. Adenoviral protein IX is a minor capsid protein that has been used to display foreign peptides on the surface of the capsid. We have used 2A sequences from the foot-and-mouth disease virus (FMDV) and porcine teschovirus 1 (PTV-1) to express protein IX (pIX) and green fluorescent protein (GFP) from pIX-2A-GFP fusion genes in an oncolytic virus derived from human adenovirus 5. GFP was efficiently expressed by constructs containing either 2A sequence. Peptide bond skipping was more efficient with the 58 aa FMDV sequence than with the 22 aa PTV-1 2A sequence, but the virus with the FMDV 2A sequence showed a reduction in plaque size, cytopathic effect, viral burst size and capsid stability. We conclude that ribosome skipping induced by 2A sequences is an effective strategy to express heterologous genes in adenoviruses; however, careful selection or optimization of the 2A sequence may be required if protein IX is used as the fusion partner. INTRODUCTIONReplication-competent oncolytic adenoviruses have been extensively tested in animals, and a virus lacking the E1B 55K gene was recently approved for cancer therapy in China (reviewed by Alemany, 2007). The main factor limiting widespread application of oncolytic adenoviruses is their low efficacy. Many groups have attempted to develop more active viruses, for example by inserting genes for toxic proteins or prodrug-activating enzymes (reviewed by Alemany, 2007). We and others have previously used internal ribosome entry sites (IRESs) to initiate the translation of prodrug-activating enzymes in adenoviruses but the results were disappointing (reviewed by de Felipe, 2002;Fuerer & Iggo, 2004;Lukashev et al., 2005). Ribosome skipping is a recently described mechanism that allows translation of multiple proteins from a single mRNA. It is based on the use of a picornaviral 2A sequence that causes the ribosome to continue translation after skipping the formation of one peptide bond. This process was first characterized in foot-and-mouth disease virus (FMDV) (Ryan & Drew, 1994). The process was originally termed 'cleavage' by analogy with the proteasemediated cleavages occurring at other sites in the FMDV polyprotein but this is misleading because the 'cleavage' results from failure to form a peptide bond during translation. Unlike reinitiation of translation by IRESs, skipping induced by 2A sequences gives approximately equal expression of the proteins upstream and downstream of the 2A site (de Felipe et al., 2006). 2A and 2A-like sequences have previously been used in biotechnology applications, but not in adenoviruses (reviewed by de Felipe et al., 2006). Protein IX is a small cement protein located between the hexons in the capsid of the adenovirus (Furcinitti et al., 1989). It is essential for the packaging of full-length viral genomes (Ghosh-Cho...

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Adenovirus polypeptide IX revealed as capsid cement by difference images from electron microscopy and crystallography.

Cited by 100 publications

References 47 publications

Evaluation of Cell-Penetrating Peptide/Adenovirus Particles for Transduction of CAR-Negative Cells

Evaluation of Cell-Penetrating Peptide/Adenovirus Particles for Transduction of CAR-Negative Cells

Stepwise dismantling of adenovirus 2 during entry into cells

Expression of heterologous genes in oncolytic adenoviruses using picornaviral 2A sequences that trigger ribosome skipping

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