The Architecture of Adenoviruses

Nermut, M. V.

doi:10.1007/978-1-4684-7935-5_2

Cited by 22 publications

(28 citation statements)

References 62 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…After DOC treatment, viral DNA is partially uncoated and only associated with core proteins V and VII, making the DNA accessible to the environment (in particular to nucleases), whereas in intact virions the viral DNA is packed with histonelike proteins to form the inner core of the particle (3,35).…”

Section: Discussionmentioning

confidence: 99%

“…Proliferation was evaluated at day 3 by tory activity. However, capsomers released by DOC-treatment of Ad particles have been shown to retain full immunogenicity, as well as morphological integrity, as observed under the electron microscope (2,3,35).…”

Section: Discussionmentioning

confidence: 99%

“…The virus concentration was 5 ϫ 10 8 particles/l of saline buffer containing 0.005% Tween 80. For capsid disruption, AdE1°samples (10 9 particles) in 50 mM Tris-HCl were treated with sodium deoxycholate (DOC; final concentration, 0.5%) and heated at 56°C for 90 s. Treatment with such a mild detergent has been shown to disrupt the viral capsid and to release the nucleoprotein core, groups of nine hexon capsomers, free peripentonal hexons, penton base, and fiber capsomers (2,3,35).…”

Section: Methodsmentioning

confidence: 99%

“…DOC treatment of Ad has been shown to disrupt the viral particle and release the subcapsid elements, i.e., (i) the inner core containing the viral genome associated with core protein V and histone-like protein VII, (ii) the apex and facet proteins penton base (Pb), fiber (Fi), and IIIa, and (iii) groups of nine hexons (Hx) comprised of Hx capsomers connected to Hxassociated proteins VI, VIII, and IX (3,8,35). BALB/c mice were immunized with LP6 and 10 9 particles of DOC-disrupted AdE1°.…”

Section: Induction Of T-helper Type 1 and Humoral Responses By Coinjementioning

confidence: 99%

See 3 more Smart Citations

Adenovirus Hexon Protein Is a Potent Adjuvant for Activation of a Cellular Immune Response

Molinier‐Frenkel

Lengagne

Gaden

et al. 2002

J Virol

156

106

View full text Add to dashboard Cite

The capacity of recombinant adenoviruses (rAd) to induce immunization against their transgene products has been well documented. In the present study, we evaluated the vaccinal adjuvant role of rAd independently of its vector function. BALB/c mice received one subcutaneous injection of a mixture of six lipopeptides (LP6) used as a model immunogen, along with AdE1°(10 9 particles), a first-generation rAd empty vector. Although coinjected with a suboptimal dose of lipopeptides, AdE1°significantly improved the effectiveness of the vaccination, even in the absence of booster immunization. In contrast to mice that received LP6 alone or LP6 plus a mock adjuvant, mice injected with AdE1°plus LP6 developed both a polyspecific T-helper type 1 response and an effector CD8 T-cell response specific to at least two class I-restricted epitopes. The helper response was still observed when immunization was performed using LP6 plus a mixture of soluble capsid components released from detergent-disrupted virions. When mice were immunized with LP6 and each individual capsid component, i.e., hexon, penton base, or fiber, the results obtained suggested that hexon protein was responsible for the adjuvant effect exerted by disrupted Ad particles on the helper response to the immunogen. Our results thus have some important implications not only in vaccinology but also for gene therapy using rAd vectors.

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Induction Of T-helper Type 1 and Humoral Responses By Coinjementioning

confidence: 99%

See 2 more Smart Citations

Adenovirus Hexon Protein Is a Potent Adjuvant for Activation of a Cellular Immune Response

Molinier‐Frenkel

Lengagne

Gaden

et al. 2002

J Virol

156

106

View full text Add to dashboard Cite

show abstract

“…The vertex capsomer of the adenovirus (Ad) icosahedral capsid, the penton, is a heteromeric protein composed of two different late gene products, the penton base subunit, anchored in the capsid, and a fibrous projection, the fiber (Wilcox and Ginsberg, 1963;Valentine and Pereira, 1965;Nermut, 1984;Pettersson, 1984). The Ad penton is composed of four major domains with different structural and functional roles, namely (i) penton base, (ii) fiber tail, (iii) fiber shaft and (iv) fiber knob.…”

Section: Introductionmentioning

confidence: 99%

Protein ligands of the human adenovirus type 2 outer capsid identified by biopanning of a phage-displayed peptide library on separate domains of wild-type and mutant penton capsomers.

Hong

Boulanger

1995

The EMBO Journal

View full text Add to dashboard Cite

A filamentous phage-displayed random hexapeptide library was screened on the adenovirus type 2 (Ad2) penton capsomer and its separate domains, penton base, full-length fiber, fiber shaft and fiber knob. Affinity supports were designed to immobilize the penton ligate with a preferred orientation, via immunoadsorption to pre-coated antibody. Three classes of phagotopes were distinguished in the eluates from the penton and fiber domains. (i) The first class represented peptide sequences identified in certain Ad2 capsid proteins, protein Illa, protein pVllI, penton base and penton fiber. Data from specific ligand elution of phages bound to fiber and penton base wild-types and mutants suggested that the region overlapping the RLSNLLG motif at residues 254-260 in the penton base and the FNPVYP motif at residues 11-16 in the fiber tail formed mutual interacting sites in the penton capsomer.(ii) The second class consisted of phagotopes homologous to peptide sequences found in host cell membrane proteins involved in receptor or adhesion functions. One of the most abundant species corresponded to a conserved motif present in the 1-strand B of type III modules of human fibronectin. In addition, phages which were screened for their failure to bind to penton base RGD mutants were found to carry consensus motifs to peptide sequences present in the RGD recognition site of human integrin P subunits.(iii) The third class comprised peptide motifs common to both viral and cellular proteins, suggesting that a mechanism of ligand exchange could occur during virus entry and uncoating, and virus assembly and release.

show abstract

Adenoviral-mediated gene transfer to enhance neuronal survival, growth, and regeneration

Smith¹,

Romero²

1999

J. Neurosci. Res.

View full text Add to dashboard Cite

The Architecture of Adenoviruses

Cited by 22 publications

References 62 publications

Adenovirus Hexon Protein Is a Potent Adjuvant for Activation of a Cellular Immune Response

Adenovirus Hexon Protein Is a Potent Adjuvant for Activation of a Cellular Immune Response

Protein ligands of the human adenovirus type 2 outer capsid identified by biopanning of a phage-displayed peptide library on separate domains of wild-type and mutant penton capsomers.

Adenoviral-mediated gene transfer to enhance neuronal survival, growth, and regeneration

Contact Info

Product

Resources

About