scholarly journals EXPRESSION AND PURIFICATION CAPSID PROTEINS VP0, VP1 AND VP3 OF FOOT AND MOUTH DISEASE VIRUS TYPE O IN ESCHERICHIA COLI

2016 ◽  
Vol 54 (5) ◽  
pp. 597
Author(s):  
Nguyen Hoang Duong ◽  
Chi-Ning Chuang ◽  
Nguyen Phuong Hoa ◽  
Tran Thi Kim Dung ◽  
Le Hong Minh ◽  
...  
Keyword(s):  
Disease Virus ◽  
Expression System ◽  
Foot And Mouth Disease ◽  
Initial Step ◽  
Mouth Disease ◽  
Capsid Proteins ◽  
Virus Like Particles ◽  
Safety Issues ◽  
Mouth Disease Virus ◽  
Foot And Mouth

Foot and mouth disease virus (FMDV) causing infectious disease affects broadly cloven-hoofed animals. It has 7 different serotypes. However O is the most prevalent type in 3 founded types (O, A, Asia1) recurrence in Vietnam fields. The current vaccine for FMDV is inactivated or attenuated forms. Vaccines were able to raise strong immune responses but still caused the safety concerns. Virus-like particles could be a new vaccine generation that fulfills the present questions. On the one hand, it can tackle the safety issues, on the other hand, it can reserve FMDV intrinsic form which will provoke high immunogenicity. The important initial step to make virus-like particles is expression the capsid proteins of FMDV in appropriate system. So this study we describe how to design, express and purify of all capsid proteins: VP0, VP1 and VP3 of O type FMDV isolated in Vietnam field using SUMO fusion expression system.

scholarly journals Assembly and characterization of foot-and-mouth disease virus empty capsid particles expressed within mammalian cells

2013 ◽  
Vol 94 (8) ◽  
pp. 1769-1779 ◽  
Author(s):  
Maria Gullberg ◽  
Bartosz Muszynski ◽  
Lindsey J. Organtini ◽  
Robert E. Ashley ◽  
Susan L. Hafenstein ◽  
...  
Keyword(s):  
Disease Virus ◽  
Mammalian Cells ◽  
Expression System ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Capsid Proteins ◽  
Dependent Manner ◽  
Empty Capsid ◽  
Mouth Disease Virus ◽  
Foot And Mouth

The foot-and-mouth disease virus (FMDV) structural protein precursor, P1-2A, is cleaved by the virus-encoded 3C protease (3Cpro) into the capsid proteins VP0, VP1 and VP3 (and 2A). In some systems, it is difficult to produce large amounts of these processed capsid proteins since 3Cpro can be toxic for cells. The expression level of 3Cpro activity has now been reduced relative to the P1-2A, and the effect on the yield of processed capsid proteins and their assembly into empty capsid particles within mammalian cells has been determined. Using a vaccinia-virus-based transient expression system, P1-2A (from serotypes O and A) and 3Cpro were expressed from monocistronic cDNA cassettes as P1-2A-3C, or from dicistronic cassettes with the 3Cpro expression dependent on a mutant FMDV internal ribosome entry site (IRES) (designated P1-2A-mIRES-3C). The effects of using a mutant 3Cpro with reduced catalytic activity or using two different mutant IRES elements (the wt GNRA tetraloop sequence GCGA converted, in the cDNA, to GAGA or GTTA) were analysed. For both serotypes, the P1-2A-mIRES-3C construct containing the inefficient GTTA mutant IRES produced the highest amount of processed capsid proteins. These products self-assembled to form FMDV empty capsid particles, which have a related, but distinct, morphology (as determined by electron microscopy and reconstruction) from that determined previously by X-ray crystallography. The assembled empty capsids bind, in a divalent cation-dependent manner, to the RGD-dependent integrin αvβ6, a cellular receptor for FMDV, and are recognized appropriately in serotype-specific antigen ELISAs.

scholarly journals Immunoreactivity and trypsin sensitivity of recombinant virus-like particles of foot-and-mouth disease virus

2015 ◽  
Vol 59 (01) ◽  
pp. 84-91 ◽  
Author(s):  
S. H. BASAGOUDANAVAR ◽  
M. HOSAMANI ◽  
R. P. TAMIL ◽  
B. P. SREENIVASA ◽  
B. K. CHANDRASEKHAR ◽  
...  
Keyword(s):  
Disease Virus ◽  
Recombinant Virus ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Virus Like Particles ◽  
Mouth Disease Virus ◽  
Foot And Mouth

scholarly journals Evidence for the role of His-142 of protein 1C in the acid-induced disassembly of foot-and-mouth disease virus capsids

1999 ◽  
Vol 80 (8) ◽  
pp. 1911-1918 ◽  
Author(s):  
Fiona M. Ellard ◽  
Jeff Drew ◽  
Wendy E. Blakemore ◽  
David I. Stuart ◽  
Andrew M. Q. King
Keyword(s):  
Disease Virus ◽  
Expression System ◽  
Foot And Mouth Disease ◽  
Dipole Interaction ◽  
Virus Genome ◽  
Mouth Disease ◽  
Mouth Disease Virus ◽  
Foot And Mouth ◽  
Acidic Conditions ◽  
Α Helix

Foot-and-mouth disease virus (FMDV) capsids are inherently labile under mildly acidic conditions, dissociating to pentamers at pH values in the region of 6·5, with the release of protein 1A and the viral RNA. This acid-induced disassembly is thought to be required for the entry of the virus genome into the host cell. Previous work has highlighted a histidine–α-helix charge-dipole interaction at the twofold axes of symmetry between pentamers and has suggested that this interaction plays a role in acid-induced disassembly. The validity of this theory has now been tested by converting the implicated residue, His-142 of protein 1C, to Arg, Phe and Asp. The effects of such changes were studied by using a previously described vaccinia virus expression system, in which synthesis and processing of FMDV capsid proteins results in the self-assembly of capsids. In agreement with the histidine–α-helix charge-dipole theory, assembly in the arginine mutant was found to be greatly reduced, while capsids of the aspartic acid mutant were considerably more stable under acidic conditions than the wild-type. Aberrant but acid-stable complexes were obtained in the phenylalanine mutant.

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