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1.
Biochem Biophys Res Commun ; 508(3): 791-796, 2019 01 15.
Article in English | MEDLINE | ID: mdl-30528388

ABSTRACT

Recent developments in tumour treatment had focused on virotherapies that were currently revolutionising new innovated treatment pathways. This study focused on the fabrication of oncolytic adenoviral vector (Ad) nanosphere that self-targeted at lung tumour cells (A549), utilising the immune response for upper respiratory tract infection, caused by the Ad infection. This system was dependent upon T-cell immune response, surface charge and blood metabolism. Oncolytic Ad attacked lung A549 tumour cells by incorporated its own DNA to replace A549's, the triggered immune response generated T-cells also further attack A549. Direct Ad injection was demonstrated to be lethal and prohibited in vivo. In this research a multifunctional principal using polyprotein surface precipitation technique (PSP) whist maintaining biological controls for self-assembly polyprotein Ad nanosphere both biocompatible and reproducible, was demonstrated as a result of the enhanced transfection efficiency and a successful multifunctional drug delivery system for virotherapy.


Subject(s)
Adenoviridae/metabolism , Chemical Precipitation , Nanospheres/chemistry , Oncolytic Virotherapy , Oncolytic Viruses/metabolism , Polyproteins/metabolism , Transfection , A549 Cells , Adenoviridae/ultrastructure , Humans , Nanospheres/ultrastructure , Oncolytic Viruses/ultrastructure , Surface Properties , Ultrasonics
2.
Viruses ; 9(11)2017 10 30.
Article in English | MEDLINE | ID: mdl-29084163

ABSTRACT

LuIII, a protoparvovirus pathogenic to rodents, replicates in human mitotic cells, making it applicable for use to kill cancer cells. This virus group includes H-1 parvovirus (H-1PV) and minute virus of mice (MVM). However, LuIII displays enhanced oncolysis compared to H-1PV and MVM, a phenotype mapped to the major capsid viral protein 2 (VP2). This suggests that within LuIII VP2 are determinants for improved tumor lysis. To investigate this, the structure of the LuIII virus-like-particle was determined using single particle cryo-electron microscopy and image reconstruction to 3.17 Å resolution, and compared to the H-1PV and MVM structures. The LuIII VP2 structure, ordered from residue 37 to 587 (C-terminal), had the conserved VP topology and capsid morphology previously reported for other protoparvoviruses. This includes a core ß-barrel and α-helix A, a depression at the icosahedral 2-fold and surrounding the 5-fold axes, and a single protrusion at the 3-fold axes. Comparative analysis identified surface loop differences among LuIII, H-1PV, and MVM at or close to the capsid 2- and 5-fold symmetry axes, and the shoulder of the 3-fold protrusions. The 2-fold differences cluster near the previously identified MVM sialic acid receptor binding pocket, and revealed potential determinants of protoparvovirus tumor tropism.


Subject(s)
Oncolytic Viruses/chemistry , Oncolytic Viruses/ultrastructure , Parvovirus/chemistry , Parvovirus/ultrastructure , Animals , Capsid/chemistry , Capsid/ultrastructure , Capsid Proteins/chemistry , Cryoelectron Microscopy/methods , H-1 parvovirus/chemistry , H-1 parvovirus/ultrastructure , Humans , Image Processing, Computer-Assisted , Imaging, Three-Dimensional , Mice , Minute Virus of Mice/chemistry , Minute Virus of Mice/ultrastructure , Models, Molecular
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