Involvement of cellular adhesion sequences in the attachment of adenovirus to the HeLa cell surface

Belin, Marie-Thérèse; Boulanger, Pierre

doi:10.1099/0022-1317-74-8-1485

Cited by 67 publications

(60 citation statements)

References 37 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…This would explain the complexity of the Ad2 receptor sites and of the Ad2 fiber cell membrane ligands previously observed (Lonberg-Holm et al, 1976;Hennache and Boulanger, 1977;Boulanger and Philipson, 1981;Defer et al, 1990;Belin and Boulanger, 1993). Thus it is conceivable that adenovirus, as suggested for other viruses (reviewed in Haywood, 1994), uses a variety of binding motifs present as constitutive units of several cell membrane proteins with receptor functions.…”

Section: Relative Affinities Between Phages and Ligandsmentioning

confidence: 89%

“…No significant difference was observed between the three different phages or a mixture of the three; the combined set of the three phages MTSDDL, LPRARA and GLSIWN did not result in any more pronounced effect. The observed inhibiting effect on Ad2 entry by phages was significant, considering that the maximum decrease in virus binding to HeLa cells obtained was 4-fold in homologous competition between radiolabeled Ad2 and a 100-fold excess of cold Ad2 competitor (Belin and Boulanger, 1993).…”

Section: Resultsmentioning

confidence: 99%

“…Thus in the currently accepted model of sequential interactions between Ad and its cell receptor(s), the primary event would consist of virus-cell recognition and attachment, involving the fiber knob and an as yet unidentified cell surface receptor. Subsequently the conserved RGD motifs in the penton base and host cell components (such as XV03 and av135 integrins) within the plasma membrane would interact and permit (or facilitate) endocytosis of the virion (Lonberg-Holm and Philipson, 1969;Hennache and Boulanger, 1977;Svensson et al, 1981;Neuman et al, 1988;Defer et al, 1990;Varga et al, 1991;Bai et al, 1993;Belin and Boulanger, 1993;White 1993; Wickham et al, 1993;Cuzange et al, 1994;Mathias et al, 1994;Nemerow et al, 1994;Sprengel et al, 1994). However, significant differences in RGD ligand usage have been observed between Ad2 and Adi2 (Bai et al, 1994) and additional capsid proteins, which remain to be identified, could also participate in Ad cell entry (Greber et al, 1993;Wickham et al, 1994).…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

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

Self Cite

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

Section: Relative Affinities Between Phages and Ligandsmentioning

confidence: 89%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

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

Self Cite

View full text Add to dashboard Cite

show abstract

“…Next, the adenovirus achieves internalization through interaction with integrins of the a V class. 29,30 Even if Adv -F/ RGD bypasses the initial step, binding CAR through fiber protein with high -affinity Ad and modified Ad uses the same pathway to enter the target cell. Therefore, Adv -F /RGD may not efficiently further enhance gene transduction through binding of the RGD peptide to integrins on target cells, which already express sufficient CAR, such as HeLa cells.…”

Section: Cancer Gene Therapymentioning

confidence: 99%

Enhanced antitumor effect of RGD fiber-modified adenovirus for gene therapy of oral cancer

et al. 2002

View full text Add to dashboard Cite

Current clinical success rates of adenoviral vector ( Adv ) -based gene therapy of squamous cell carcinoma ( SCC ) of the head and neck remain unsatisfactory. A major problem with this approach is thought to be related to low Adv transduction efficiency due to weak expression of the adenovirus receptor, coxsackie -adenovirus receptor ( CAR ), in SCC. To improve the limited infectivity of Adv in oral SCC, we constructed mutated Adv incorporating the integrin -binding motif, RGD, in the HI loop of the fiber knob. The mutated Adv infected target cells through integrins commonly expressed in oral SCC. LacZ marker gene expression after infection with this mutated Adv ( Adv -F / RGD ) in oral SCC cell lines that showed reduced expression of CAR was approximately 5 -10 times higher than that obtained with the parental Adv containing wild -type fiber knob ( Adv -F / wt ). In an in vitro study, transduction of oral cancer cell lines with Adv -F / RGD expressing human IL -2 ( AxCAhIL2 -F / RGD ) resulted in greater production of cytokine than AxCAhIL2 -F / wt infection. In an in vivo therapeutic xenograft model of oral SCC in nude mice, AxCAhIL2 -F / RGD demonstrated antitumor effects superior to those of AxCAhIL2 -F / wt. These data suggest that exploitation of genetically altered adenovirus vectors with integrin -binding motifs may offer significant improvements in oral SCC gene therapy.

show abstract

“…First, the virus attaches with high affinity to an as yet unidentified cell surface receptor via the globular head domains of the protruding viral fibers (Philipson et al, 1968;Louis et al, 1994;Xia et al, 1995). A secondary receptor, the fibronectin binding integrin, then associates with the penton base protein, and as a result the virus is endocytosed via coated pits and coated vesicles (Varga et al, 1991;Bai et al, 1993;Belin and Boulanger, 1993; Wickham et al, 1993). 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).…”

Section: Introductionmentioning

confidence: 99%

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

et al. 1996

View full text Add to dashboard Cite

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.

show abstract

Involvement of cellular adhesion sequences in the attachment of adenovirus to the HeLa cell surface

Cited by 67 publications

References 37 publications

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.

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.

Enhanced antitumor effect of RGD fiber-modified adenovirus for gene therapy of oral cancer

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

Contact Info

Product

Resources

About