Core-Shell Imprinted Particles for Adenovirus Binding

Virus-imprinted polymers were synthesized via surface imprinting strategies to produce core-shell imprinted particles selective for human adenovirus type 5. High binding affinity of the target virus towards the resulting imprinted layer was confirmed and unspecific binding was reduced in presence of blocking agents, i.e., via bovine serum albumin and skim milk in combination with Tween 20. In addition, the imprinted materials were applied for adenovirus extraction from cell culture supernatants. High levels of virus binding with negligible binding of matrix proteins confirmed the suitability of these materials for binding and extraction of the target virus from complex matrices.

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In Vitro and In Vivo Evaluation of Human Adenovirus Type 49 as a Vector for Therapeutic Applications

Viruses ◽

10.3390/v13081483 ◽

2021 ◽

Vol 13 (8) ◽

pp. 1483

Author(s):

Emily A. Bates ◽

John R. Counsell ◽

Sophie Alizert ◽

Alexander T. Baker ◽

Natalie Suff ◽

...

Keyword(s):

Viral Vector ◽

Ex Vivo ◽

Human Adenovirus ◽

Adenovirus Type ◽

Cell Types ◽

In Vivo Evaluation ◽

In Vivo Biodistribution ◽

Adenovirus Type 5

The human adenovirus phylogenetic tree is split across seven species (A–G). Species D adenoviruses offer potential advantages for gene therapy applications, with low rates of pre-existing immunity detected across screened populations. However, many aspects of the basic virology of species D—such as their cellular tropism, receptor usage, and in vivo biodistribution profile—remain unknown. Here, we have characterized human adenovirus type 49 (HAdV-D49)—a relatively understudied species D member. We report that HAdV-D49 does not appear to use a single pathway to gain cell entry, but appears able to interact with various surface molecules for entry. As such, HAdV-D49 can transduce a broad range of cell types in vitro, with variable engagement of blood coagulation FX. Interestingly, when comparing in vivo biodistribution to adenovirus type 5, HAdV-D49 vectors show reduced liver targeting, whilst maintaining transduction of lung and spleen. Overall, this presents HAdV-D49 as a robust viral vector platform for ex vivo manipulation of human cells, and for in vivo applications where the therapeutic goal is to target the lung or gain access to immune cells in the spleen, whilst avoiding liver interactions, such as intravascular vaccine applications.

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The endosomal epsilon-coatomer protein is involved in human adenovirus type 5 internalisation

Acta Veterinaria Hungarica ◽

10.1556/avet.50.2002.4.10 ◽

2002 ◽

Vol 50 (4) ◽

pp. 481-489 ◽

Cited By ~ 1

Author(s):

Cs. Jeney ◽

Boglárka Banizs ◽

Orsolya Dobay ◽

Keyword(s):

Chinese Hamster ◽

Human Adenovirus ◽

Adenovirus Type ◽

Inhibitory Effect ◽

Bafilomycin A1 ◽

Cho Cell ◽

Coxsackie Adenovirus Receptor ◽

Downstream Effector ◽

Adenovirus Receptor ◽

Adenovirus Type 5

The effects of bafilomycin A1 and of the reduced level of endosomal epsilon-COP (coatomer protein) on the infectivity of human adenovirus type 5 were investigated in Coxsackie adenovirus receptor- (CAR-) transfected Chinese hamster ovary (CHO) cells. The endosomal proton pump inhibitor bafilomycin A1 was able to cause only partial inhibition. Using ldlF cells (an epsilon-COP thermosensitive mutant CHO cell line) the reduction of epsilon-COP level also had partial inhibitory effect. Based on these results and comparing them to existing models of the adenovirus entry, we propose a refined model in which there are two pathways of adenoviral entry: the first one involves the epsilon-COP as the downstream effector of the acidification and can be blocked by bafilomycin A1 and the second one is a pH-independent pathway.

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Chimpanzee adenovirus CV-68 adapted as a gene delivery vector interacts with the coxsackievirus and adenovirus receptor

Journal of General Virology ◽

10.1099/0022-1317-83-1-151 ◽

2002 ◽

Vol 83 (1) ◽

pp. 151-155 ◽

Cited By ~ 43

Author(s):

Christopher J. Cohen ◽

Zhi Quan Xiang ◽

Guang-Ping Gao ◽

Hildegund C. J. Ertl ◽

James M. Wilson ◽

...

Keyword(s):

Gene Delivery ◽

Cho Cells ◽

Human Adenovirus ◽

Adenovirus Type ◽

Soluble Form ◽

Delivery Vector ◽

Coxsackievirus And Adenovirus Receptor ◽

Adenovirus Receptor ◽

Adenovirus Type 5 ◽

Dependent Mechanism

A replication-defective form of chimpanzee adenovirus type 68 (C68) has been developed to circumvent problems posed by widespread preexisting immunity to common human adenovirus vectors. To investigate the determinants of C68 tropism, its interaction with the coxsackievirus and adenovirus receptor (CAR) was studied. Although CHO cells were resistant to transduction by C68 as well as by adenovirus type 5 (Ad5), CHO cells expressing either human or murine CAR were transduced readily. C68 transduction, like Ad5 transduction, was blocked when cells were exposed to anti-CAR antibody or when virus was exposed to a soluble form of the CAR extracellular domain. These results indicate that gene delivery by C68 occurs by a CAR-dependent mechanism.

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Bovine herpesvirus 1 glycoprotein D expression in bovine upper respiratory tract mediated by a human adenovirus type 5

Veterinary Research ◽

10.1051/vetres:2004045 ◽

2004 ◽

Vol 35 (6) ◽

pp. 715-721 ◽

Cited By ~ 6

Author(s):

Sacha Gogev ◽

Jean-Pierre Georgin ◽

Fr�d�ric Schynts ◽

Alain Vanderplasschen ◽

Etienne Thiry

Keyword(s):

Respiratory Tract ◽

Bovine Herpesvirus ◽

Human Adenovirus ◽

Adenovirus Type ◽

Upper Respiratory Tract ◽

Glycoprotein D ◽

Bovine Herpesvirus 1 ◽

Upper Respiratory ◽

Herpesvirus 1 ◽

Adenovirus Type 5

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Comparative Sequence Analysis of the Largest E1A Proteins of Human and Simian Adenoviruses

Journal of Virology ◽

10.1128/jvi.76.16.7968-7975.2002 ◽

2002 ◽

Vol 76 (16) ◽

pp. 7968-7975 ◽

Cited By ~ 48

Author(s):

Nikita Avvakumov ◽

Russ Wheeler ◽

Jean Claude D'Halluin ◽

Joe S. Mymryk

Keyword(s):

Gene Expression ◽

Human Adenovirus ◽

Detailed Comparison ◽

Adenovirus Type ◽

Comparative Sequence Analysis ◽

Regulatory Proteins ◽

Carboxyl Terminus ◽

Adenovirus E1a ◽

Simian Adenovirus ◽

Adenovirus Type 5

ABSTRACT The early region 1A (E1A) gene is the first gene expressed after infection with adenovirus and has been most extensively characterized in human adenovirus type 5 (hAd5). The E1A proteins interact with numerous cellular regulatory proteins, influencing a variety of transcriptional and cell cycle events. For this reason, these multifunctional proteins have been useful as tools for dissecting pathways regulating cell growth and gene expression. Despite the large number of studies using hAd5 E1A, relatively little is known about the function of the E1A proteins of other adenoviruses. In 1985, a comparison of E1A sequences from three human and one simian adenovirus identified three regions with higher overall levels of sequence conservation designated conserved regions (CR) 1, 2, and 3. As expected, these regions are critical for a variety of E1A functions. Since that time, the sequences of several other human and simian adenovirus E1A proteins have been determined. Using these, and two additional sequences that we determined, we report here a detailed comparison of the sequences of 15 E1A proteins representing each of the six hAd subgroups and several simian adenoviruses. These analyses refine the positioning of CR1, 2, and 3; define a fourth CR located near the carboxyl terminus of E1A; and suggest several new functions for E1A.

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Mapping of cellular protein-binding sites on the products of early-region 1A of human adenovirus type 5

Molecular and Cellular Biology ◽

10.1128/mcb.8.9.3955-3959.1988 ◽

1988 ◽

Vol 8 (9) ◽

pp. 3955-3959 ◽

Cited By ~ 2

Author(s):

C Egan ◽

T N Jelsma ◽

J A Howe ◽

S T Bayley ◽

B Ferguson ◽

...

Keyword(s):

Biological Activity ◽

Binding Sites ◽

Human Adenovirus ◽

Adenovirus Type ◽

Cellular Protein ◽

Cellular Proteins ◽

Deletion Mutants ◽

Protein Binding Sites ◽

Amino Terminal ◽

Adenovirus Type 5

The binding sites for the 300-, 107-, and 105-kilodalton cellular proteins which associate with human adenovirus type 5 E1A products were studied with E1A deletion mutants. All appeared to bind to the amino-terminal half of E1A products in regions necessary for oncogenic transformation. These results suggest that these cellular species may be important for the biological activity of E1A products.

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