The Oligomeric Structure of Vaccinia Viral Envelope Protein A27L is Essential for Binding to Heparin and Heparan Sulfates on Cell Surfaces: A Structural and Functional Approach Using Site-specific Mutagenesis

Ho, Yu; Yang, Min Hsiang; Chung, Che Sheng; Peng, Yi; Lin, Ta Hsien; Chang, Wen; Tzou, Der‐Lii M.

doi:10.1016/j.jmb.2005.04.024

Cited by 31 publications

(51 citation statements)

References 36 publications

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“…2A) shows only the signals originating from the flexible random coil (21-42 residues), whereas any remaining signals arising from the structured domains, such as CCD, DLD, and LZD (i.e. the A17 binding domain), were absent, consistent with the truncated A27 crystal structure (27) and previous reports (24,26,44). In contrast, as shown in Fig.…”

Section: A27 Binds To the N Terminus Of A17 As Revealed By Hsqc-supporting

confidence: 87%

“…SPR-Real time SPR experiments were performed on a BIAcore Biosensor 3000 system (BIAcore, Uppsala, Sweden) as described previously (24). CM5 sensor chips were purchased from BIAcore.…”

Section: Purification Of Recombinant Proteins-mentioning

confidence: 99%

“…In the infected cells, A17 is synthesized as a 23-kDa precursor of 203 amino acids and is subsequently cleaved at both the N and C termini during maturation (30), as indicated by arrows. The three A17 fragments used in this study are shown below: A17-N, A17-C, and A17-S, in which the A17-N sequence 24 LFTEEQQQSFM 34 was scrambled to 24 QLESQFQTMEF 34 . These A17 fragments tagged with thioredoxin were expressed in E. coli, and the tag was removed by factor Xa cleavage (for details, see "Experimental Procedures").…”

Section: N Terminus Of A17 Has a Higher A27 Binding Affinity Than Thementioning

confidence: 99%

“…1B). In the A17-S construct, the A27-binding sequence 24 LFTE-EQQQSFM 34 was scrambled to 24 QLESQFQTMEF 34 . When A17-S was titrated with A27, the A17-S cross-peak pattern detected by HSQC remained intact, indicating that A17-S loses its binding specificity to A27 (Fig.…”

Section: A27 Binding To the N Terminus Of A17 Ismentioning

confidence: 99%

“…1A), including an N-terminal heparin-binding sequence (HBS, 21-32 residues) essential for heparin binding to the cell surface (6), a flexible spacer (33-42 residues), an ␣-helical coiled-coil domain (CCD, 43-65 residues) critical for A27 oligomerization, a disulfide-linked domain (DLD, 66 -84 residues) (24), and a C-terminal leucine zipper domain (LZD, 85-110 residues) responsible for anchoring to the viral membrane via interaction with A17 (23,25). Previous studies have suggested that the N-and C-terminal domains are structurally distinct.…”

mentioning

confidence: 99%

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Vaccinia Viral Protein A27 Is Anchored to the Viral Membrane via a Cooperative Interaction with Viral Membrane Protein A17

Wang

Hsiao

Wong

et al. 2014

Journal of Biological Chemistry

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Background: Vaccinia viral protein A27 associates with viral membrane protein A17 for anchoring to the viral membrane. Results: A27 specifically interacts with two binding regions within the N-terminal domain of A17. Conclusion: The A27-A17 interaction is mediated through a specific and cooperative binding mechanism. Significance: As demonstrated, the F1 and F2 bindings are critical for A27 anchoring to the viral membrane and virion assembly.

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Section: A27 Binds To the N Terminus Of A17 As Revealed By Hsqc-supporting

confidence: 87%

“…SPR-Real time SPR experiments were performed on a BIAcore Biosensor 3000 system (BIAcore, Uppsala, Sweden) as described previously (24). CM5 sensor chips were purchased from BIAcore.…”

Section: Purification Of Recombinant Proteins-mentioning

confidence: 99%

Section: N Terminus Of A17 Has a Higher A27 Binding Affinity Than Thementioning

confidence: 99%

Section: A27 Binding To the N Terminus Of A17 Ismentioning

confidence: 99%

mentioning

confidence: 99%

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Vaccinia Viral Protein A27 Is Anchored to the Viral Membrane via a Cooperative Interaction with Viral Membrane Protein A17

Wang

Hsiao

Wong

et al. 2014

Journal of Biological Chemistry

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Highly Efficient Multivalent 2D Nanosystems for Inhibition of Orthopoxvirus Particles

Ziem

Thien

Achazi

et al. 2016

Adv Healthcare Materials

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Efficient inhibition of cell-pathogen interaction to prevent subsequent infection is an urgent but yet unsolved problem. In this study, the synthesis and functionalization of novel multivalent 2D carbon nanosystems as well as their antiviral efficacy in vitro are shown. For this reason, a new multivalent 2D flexible carbon architecture is developed in this study, functionalized with sulfated dendritic polyglycerol, to enable virus interaction. A simple "graft from" approach enhances the solubility of thermally reduced graphene oxide and provides a suitable 2D surface for multivalent ligand presentation. Polysulfation is used to mimic the heparan sulfate-containing surface of cells and to compete with this natural binding site of viruses. In correlation with the degree of sulfation and the grafted polymer density, the interaction efficiency of these systems can be varied. In here, orthopoxvirus strains are used as model viruses as they use heparan sulfate for cell entry as other viruses, e.g., herpes simplex virus, dengue virus, or cytomegalovirus. The characterization results of the newly designed graphene derivatives demonstrate excellent binding as well as efficient inhibition of orthopoxvirus infection. Overall, these new multivalent 2D polymer nanosystems are promising candidates to develop potent inhibitors for viruses, which possess a heparan sulfate-dependent cell entry mechanism.

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Capturing of cell culture‐derived modified Vaccinia Ankara virus by ion exchange and pseudo‐affinity membrane adsorbers

Wolff

Siewert

Lehmann

et al. 2009

Biotech & Bioengineering

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Smallpox is an acute, highly infectious viral disease unique to humans, and responsible for an estimated 300-500 million deaths in the 20th century. Following successful vaccination campaigns through the 19th and 20th centuries, smallpox was declared eradicated by the World Health Organization in 1980. However, the threat of using smallpox as a biological weapon prompted efforts of some governments to produce smallpox vaccines for emergency preparedness. An additional aspect for the interest in smallpox virus is its potential use as a platform technology for vector vaccines. In particular, the latter requires a high safety level for routine applications. IMVAMUNE, a third generation smallpox vaccine based on the attenuated Modified Vaccinia Ankara (MVA) virus, demonstrates superior safety compared to earlier generations and represents therefore an interesting choice as viral vector. Current downstream production processes of Vaccinia virus and MVA are mainly based on labor-intensive centrifugation and filtration methods, requiring expensive nuclease treatment in order to achieve sufficient low host-cell DNA levels for human vaccines. This study compares different ion exchange and pseudo-affinity membrane adsorbers (MA) to capture chicken embryo fibroblast cell-derived MVA-BN after cell homogenization and clarification. In parallel, the overall performance of classical bead-based resin chromatography (Cellufine sulfate and Toyopearl AF-Heparin) was investigated. The two tested pseudo-affinity MA (i.e., sulfated cellulose and heparin) were superior over the applied ion exchange MA in terms of virus yield and contaminant depletion. Furthermore, studies confirmed an expected increase in productivity resulting from the increased volume throughput of MA compared to classical bead-based column chromatography methods. Overall virus recovery was approximately 60% for both pseudo-affinity MA and the Cellufine sulfate resin. Depletion of total protein ranged between 86% and 102% for all tested matrices. Remaining dsDNA in the product fraction varied between 24% and 7% for the pseudo-affinity chromatography materials. Cellufine sulfate and the reinforced sulfated cellulose MA achieved the lowest dsDNA product contamination. Finally, by a combination of pseudo-affinity with anion exchange MA a further reduction of host-cell DNA was achieved.

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The Oligomeric Structure of Vaccinia Viral Envelope Protein A27L is Essential for Binding to Heparin and Heparan Sulfates on Cell Surfaces: A Structural and Functional Approach Using Site-specific Mutagenesis

Cited by 31 publications

References 36 publications

Vaccinia Viral Protein A27 Is Anchored to the Viral Membrane via a Cooperative Interaction with Viral Membrane Protein A17

Vaccinia Viral Protein A27 Is Anchored to the Viral Membrane via a Cooperative Interaction with Viral Membrane Protein A17

Highly Efficient Multivalent 2D Nanosystems for Inhibition of Orthopoxvirus Particles

Capturing of cell culture‐derived modified Vaccinia Ankara virus by ion exchange and pseudo‐affinity membrane adsorbers

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