Data BriefData BriefData in Brief2352-3409Elsevier269586354764771S2352-3409(16)30031-210.1016/j.dib.2016.02.009Data ArticleData on interaction between adeno-associated virus and U87 cell via cRGD chemical modificationZhangChuanlingYaoTianzhuoZhengYongxiangLiZhongjunZhangLiheZhouDemindeminzhou@bjmu.edu.cn⁎State Key Laboratory of Natural and Biomimetic Drugs, School of Pharmaceutical Sciences, Peking University, No. 38, Xueyuan Road, Beijing 100191, ChinaCorresponding author. Tel.: +86 10 8280 5857; fax: +86 10 8280 5519. deminzhou@bjmu.edu.cn10220166201610220167778081220151812016222016© 2016 Published by Elsevier Inc.2016This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).

RGD tripeptide is a specific, high-affinity ligand for integrin, which is highly expressed in cancer cells. We previously reported that cRGD chemically modified AAV2 (AAV2N587+1/azido+RGD) showed significantly enhanced infectivity compared to RGD genetically inserted AAV2 (AAV2N587+RGD) (10.1016/j.biomaterials.2015.11.066) [1]. Herein we provide the binding ability analysis of RGD modified AAV2 and U87 cell by flow cytometry and the theoretical working model of RGD–αvβ3 integrin interaction.

KeywordsAdeno-associated virusViral modificationTargeted gene delivery<bold>Specifications table</bold>

Table
Subject areaBiology, Chemistry
More specific subject areaGene therapy
Type of dataFigure
How data was acquiredFlow cytometry
Data formatAnalyzed
Experimental factorsSite-specific modification of AAV2 with cRGD
Experimental featuresBinding ability between AAV2 and U87 was analyzed by Flow Cytometry
Data source locationPeking University, Beijing, China
Data accessibilityData is within this article and at Protein data bank PDB: 1L5G, PDB: 1LP3

Value of the data

This data set will be of value to the scientific community wanting to analyze the binding ability of virus and host cell.

The data show new way to study the biological mechanisms of AAV2 entry.

The data may stimulate further research on viral targeted gene delivery.

<bold>Data</bold>

The data shared in this article is the experimental and theoretical analysis of interaction between cRGD modified AAV2 and host cell (U87).

Experimental design, materials and methodsCell lines

U87 cells were maintained in an atmosphere containing 5% CO2 in Dulbecco’s modified Eagle’s medium (Gibco, Carlsbad, CA, USA) supplemented with 10% fetal bovine serum (FBS; PAA, Austria) and 2 mM l-glutamine (Gibco).

Cell surface binding assays

Cells were resuspended at a density of 2×106 cells/mL in binding buffer containing 5% FBS. Equal amounts of viral vectors were incubated with cells at 4 °C for 2 h, and unbound vector particles were then removed by washing with PBS. Vector particles bound to HeLa or U87 cells were detected by staining with anti-AAV A20 monoclonal antibodies and subsequent FACS analysis. *P<0.05 versus the corresponding control (Fig. 1, Fig. 2).

ReferencesC. Zhang, T. Yao, Y. Zheng, Z. Li, L. Zhang and D. Zhou, Development of next generation of adeno-associated viral vectors via precision engineering for preferable selective tropism and efficient gene delivery, Biomaterials. 80 (2016) 134–145, 10.1016/j.biomaterials.2015.11.066.XiongJ.P.StehleT.ZhangR.JoachimiakA.FrechM.GoodmanS.L.Crystal structure of the extracellular segment of integrin alpha Vbeta3 in complex with an Arg–Gly–Asp ligandScience2965565200215115511884718GottschalkK.E.KesslerH.A computational model of transmembrane integrin clusteringStructure12620041109111615274930XieQ.BuW.BhatiaS.HareJ.SomasundaramT.AzziA.The atomic structure of adeno-associated virus (AAV-2), a vector for human gene therapyProc. Natl. Acad. Sci. USA99162002104051041012136130Supplementary material

Supplementary material

Acknowledgments

We thank Drs. Qihua He, Bo Xu (Peking University) and Meng Lai (PerkinElmer) for their assistance with the single virus tracking experiment and Dr. Jinmin Zhou for assistance with viral purification. This work was supported by the National Basic Research Program of China (973 Program; Grant no. 2010CB12300), the National Natural Science Foundation of China (Grant nos. 31200568, 81530090), the Research Fund for the Doctoral Program of Higher Education of China (RFDP, Grant no. 20110001120037), and the Beijing Natural Science Foundation (Grant no. 7153170).

Supplementary data associated with this article can be found in the online version at 10.1016/j.dib.2016.02.009.

Analysis of the binding ability of vector particles with HeLa and U87 cells.

Fig. 1

Theoretical analysis of the different effects of RGD tethering versus RGD fusion on improvement of tropism selectivity [2], [3], [4]. (A) The three-dimensional model of αvβ3 receptor clustering. The distance between clustering αvβ3 molecules for RGD binding was labeled accordingly. Black arrows indicate RGD binding sites. (B) Schematic representative of the structure of RGD tethering versus RGD fusion to the AAV capsid protein at site N587+1. The distance between the two adjacent sites of RGD fused on AAV2 was 37.52 Å. The length of DIBO-cRGD was 43.41 Å. Upon tethering of cRGD via a DIBO linker, the maximum distance between two cRGD on AAV2N587+1/NAEK+RGD increased to 124.34 Å (2×43.41 Å+37.52 Å=124.34 Å). (C) Schematic illustration of the interactions between the clustering αvβ3 receptor and adjacent RGD-tethered versus RGD-fused ligands within the AAV2 vector. The distance between two adjacent RGD fusion motifs (~37.52 Å) was much shorter than the distance between the clustering αvβ3 binding sites (either 65.78 or 41.92 Å), preventing simultaneous binding. In contrast, the distance between the two adjacent tethered RGD motifs on AAV2N587+1/NAEK+RGD was 124.34 Å, allowing simultaneous binding of multiple integrin αvβ3 receptors. Blue indicates the RGD motifs. (For interpretation of the references to color in this figure legend, the reader is referred to the web version of this article.)

Fig. 2