Literature DB >> 22490664

Chimeric hexon HVRs protein reflects partial function of adenovirus.

Bin Yu1, Chu Wang, Jianing Dong, Min Zhang, Haihong Zhang, Jiaxin Wu, Yuqing Wu, Wei Kong, Xianghui Yu.   

Abstract

Adenovirus is widely used in gene therapy and vaccination as a viral vector, and its hypervariable regions (HVRs) on hexon are the main antigen recognition sites of adenovirus. The modification of this area by genetic engineering will change the antigenic specificity of the virus. In addition, recent studies have demonstrated the importance of coagulation factor X (FX) in adenovirus serotype 5-mediated liver transduction in vivo. The binding site of adenovirus to FX is the HVRs on hexon. By constructing five proteins containing chimeric HVRs from different adenovirus serotypes, we focused on the antigenic specificity and the affinity for FX of these proteins compared with the corresponding viruses. Our data showed that HVR5 and HVR7 had only a part of hexon activity to neutralizing antibodies (NAbs) compared with the complete activity of HVR1-7. Results also demonstrated a differential high-affinity interaction of the HVRs proteins with FX and indicated that HVRs protein had a similar binding ability with corresponding adenovirus serotype. These results highlighted some properties of chimeric HVRs proteins and revealed the influence on the structure and function of hexon proteins and adenovirus resulting from the HVRs.
Copyright © 2012 Elsevier Inc. All rights reserved.

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Year:  2012        PMID: 22490664     DOI: 10.1016/j.bbrc.2012.03.125

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  7 in total

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Journal:  Cell Death Dis       Date:  2016-06-23       Impact factor: 8.469

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  7 in total

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