scholarly journals Stable Display of Artificially Long Foreign Antigens on Chimeric Bamboo mosaic virus Particles

Viruses ◽  
2021 ◽  
Vol 13 (4) ◽  
pp. 572
Author(s):  
Tsung-Hsien Chen ◽  
Chung-Chi Hu ◽  
Chin-Wei Lee ◽  
Yu-Min Feng ◽  
Na-Sheng Lin ◽  
...  
Keyword(s):  
Amino Acids ◽  
Mosaic Virus ◽  
Foot And Mouth Disease ◽  
Plant Viruses ◽  
Foreign Protein ◽  
Virus Particles ◽  
Mouth Disease Virus ◽  
N Terminus ◽  
Linker Peptides ◽  
Different Strains

Plant viruses can be genetically modified to generate chimeric virus particles (CVPs) carrying heterologous peptides fused on the surface of coat protein (CP) subunits as vaccine candidates. However, some factors may be especially significant in determining the properties of chimeras. In this study, peptides from various sources and of various lengths were inserted into the Bamboo mosaic virus-based (BaMV) vector CP N-terminus to examine the chimeras infecting and accumulating in plants. Interestingly, it was found that the two different strains Foot-and-mouth disease virus (FMDV) VP1 antigens with flexible linker peptides (77 or 82 amino acids) were directly expressed on the BaMV CP, and the chimeric particles self-assembled and continued to express FMDV antigens. The chimeric CP, when directly fused with a large foreign protein (117 amino acids), can self-fold into incomplete virus particles or disks. The physicochemical properties of heterologus peptides N-terminus, complex strand structures of heterologus peptides C-terminus and different flexible linker peptides, can affect the chimera accumulation. Based on these findings, using plant virus-based chimeras to express foreign proteins can increase their length limitations, and engineered plant-made CVP-based vaccines have increasing potential for further development as novel vaccines.

scholarly journals Generation of Antibodies against Foot-and-Mouth-Disease Virus Capsid Protein VP4 Using Hepatitis B Core VLPs as a Scaffold

Life ◽  
2021 ◽  
Vol 11 (4) ◽  
pp. 338
Author(s):  
Jessica Swanson ◽  
Rennos Fragkoudis ◽  
Philippa C. Hawes ◽  
Joseph Newman ◽  
Alison Burman ◽  
...  
Keyword(s):  
Amino Acids ◽  
Hepatitis B ◽  
Capsid Protein ◽  
Disease Virus ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Specific Antibodies ◽  
Mouth Disease Virus ◽  
N Terminus ◽  
Foot And Mouth

The picornavirus foot-and-mouth disease virus (FMDV) is the causative agent of the economically important disease of livestock, foot-and-mouth disease (FMD). VP4 is a highly conserved capsid protein, which is important during virus entry. Previous published work has shown that antibodies targeting the N-terminus of VP4 of the picornavirus human rhinovirus are broadly neutralising. In addition, previous studies showed that immunisation with the N-terminal 20 amino acids of enterovirus A71 VP4 displayed on the hepatitis B core (HBc) virus-like particles (VLP) can induce cross-genotype neutralisation. To investigate if a similar neutralising response against FMDV VP4 could be generated, HBc VLPs displaying the N-terminus of FMDV VP4 were designed. The N-terminal 15 amino acids of FMDV VP4 was inserted into the major immunodominant region. HBc VLPs were also decorated with peptides of the N-terminus of FMDV VP4 attached using a HBc-spike binding tag. Both types of VLPs were used to immunise mice and the resulting serum was investigated for VP4-specific antibodies. The VLP with VP4 inserted into the spike, induced VP4-specific antibodies, however the VLPs with peptides attached to the spikes did not. The VP4-specific antibodies could recognise native FMDV, but virus neutralisation was not demonstrated. This work shows that the HBc VLP presents a useful tool for the presentation of FMDV capsid epitopes.

scholarly journals A Nonviral Peptide Can Replace the Entire N Terminus of Zucchini Yellow Mosaic Potyvirus Coat Protein and Permits Viral Systemic Infection

2001 ◽  
Vol 75 (14) ◽  
pp. 6329-6336 ◽  
Author(s):  
T. Arazi ◽  
Y. M. Shiboleth ◽  
A. Gal-On
Keyword(s):  
Amino Acids ◽  
Coat Protein ◽  
Foot And Mouth Disease ◽  
Systemic Infection ◽  
Deletion Mutants ◽  
Amino Acid Residues ◽  
Amino Terminal ◽  
Immunogenic Epitope ◽  
Mouth Disease Virus ◽  
N Terminus

ABSTRACT Systematic deletion and peptide tagging of the amino-terminal domain (NT, ∼43 amino acids) of an attenuated zucchini yellow mosaic potyvirus (ZYMV-AGII) coat protein (CP) were used to elucidate its role in viral systemic infection. Deletion mutants truncated by 8, 13, and 33 amino acid residues from the CP-NT 5′ end were systemically infectious and produced symptoms similar to those of the AGII virus. Tagging these deletion mutants with either human c-Myc (Myc) or hexahistidine peptides maintained viral infectivity. Similarly, addition of these peptides to the intact AGII CP-NT did not affect viral life cycle. To determine which parts, if any, of the CP-NT are essential for viral systemic infection, a series of Myc-tagged mutants with 8 to 43 amino acids removed from the CP-NT were constructed. All Myc-tagged CP-NT deletion mutants, including those from which virtually all the viral CP-NT had been eliminated, were able to encapsidate and cause systemic infection. Furthermore, chimeric viruses with deletions of up to 33 amino acids from CP-NT produced symptoms indistinguishable from those caused by the parental AGII virus. In contrast to CP-NT Myc fusion, addition of the foot-and-mouth disease virus (FMDV) immunogenic epitope to AGII CP-NT did not permit systemic infection. However, fusion of the Myc peptide to the N terminus of the FMDV peptide restored the capability of the virus to spread systemically. We have demonstrated that all CP-NT fused peptides were exposed on the virion surface, masking natural CP immunogenic determinants. Our findings demonstrate that CP-NT is not essential for ZYMV spread and that it can be replaced by an appropriate foreign peptide while maintaining systemic infectivity.

Foot-and-mouth disease virus particles inactivated with binary ethylenimine are efficiently internalized into cultured cells

Vaccine ◽  
2011 ◽  
Vol 29 (52) ◽  
pp. 9655-9662 ◽  
Author(s):  
Miguel A. Martín-Acebes ◽  
Ángela Vázquez-Calvo ◽  
Mónica González-Magaldi ◽  
Francisco Sobrino
Keyword(s):  
Disease Virus ◽  
Cultured Cells ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Virus Particles ◽  
Mouth Disease Virus ◽  
Foot And Mouth

scholarly journals Actin Cytoskeleton Is Involved in Targeting of a Viral Hsp70 Homolog to the Cell Periphery

2005 ◽  
Vol 79 (22) ◽  
pp. 14421-14428 ◽  
Author(s):  
Alexey I. Prokhnevsky ◽  
Valera V. Peremyslov ◽  
Valerian V. Dolja
Keyword(s):  
Actin Cytoskeleton ◽  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Movement Protein ◽  
Fluorescent Proteins ◽  
Cell Movement ◽  
Plant Viruses ◽  
Cell Periphery ◽  
Virus Particles ◽  
Shock Proteins

ABSTRACT The cell-to-cell movement of plant viruses involves translocation of virus particles or nucleoproteins to and through the plasmodesmata (PDs). As we have shown previously, the movement of the Beet yellows virus requires the concerted action of five viral proteins including a homolog of cellular ∼70-kDa heat shock proteins (Hsp70h). Hsp70h is an integral component of the virus particles and is also found in PDs of the infected cells. Here we investigate subcellular distribution of Hsp70h using transient expression of Hsp70h fused to three spectrally distinct fluorescent proteins. We found that fluorophore-tagged Hsp70h forms motile granules that are associated with actin microfilaments, but not with microtubules. In addition, immobile granules were observed at the cell periphery. A pairwise appearance of these granules at the opposite sides of cell walls and their colocalization with the movement protein of Tobacco mosaic virus indicated an association of Hsp70h with PDs. Treatment with various cytoskeleton-specific drugs revealed that the intact actomyosin motility system is required for trafficking of Hsp70h in cytosol and its targeting to PDs. In contrast, none of the drugs interfered with the PD localization of Tobacco mosaic virus movement protein. Collectively, these findings suggest that Hsp70h is translocated and anchored to PDs in association with the actin cytoskeleton.

scholarly journals Adaptation of Soybean mosaic virus Avirulent Chimeras Containing P3 Sequences from Virulent Strains to Rsv1-Genotype Soybeans Is Mediated by Mutations in HC-Pro

2008 ◽  
Vol 21 (7) ◽  
pp. 937-946 ◽  
Author(s):  
M. R. Hajimorad ◽  
A. L. Eggenberger ◽  
J. H. Hill
Keyword(s):  
Amino Acids ◽  
Mosaic Virus ◽  
Hypersensitive Response ◽  
Soybean Mosaic Virus ◽  
Extreme Resistance ◽  
Sequence Analyses ◽  
Virulent Strains ◽  
N Terminus ◽  
Helper Component Proteinase ◽  
Avirulent Isolate

In Rsv1-genotype soybean, Soybean mosaic virus (SMV)-N (an avirulent isolate of strain G2) elicits extreme resistance (ER) whereas strain SMV-G7 provokes a lethal systemic hypersensitive response (LSHR). SMV-G7d, an experimentally evolved variant of SMV-G7, induces systemic mosaic. Thus, for Rsv1-genotype soybean, SMV-N is avirulent whereas SMV-G7 and SMV-G7d are both virulent. Exploiting these differential interactions, we recently mapped the elicitor functions of SMV provoking Rsv1-mediated ER and LSHR to the N-terminal 271 amino acids of P3 from SMV-N and SMV-G7, respectively. The phenotype of both SMV-G7 and SMV-G7d were rendered avirulent on Rsv1-genotype soybean when the part of the genome encoding the N-terminus or the entire P3 cistron was replaced with that from SMV-N; however, reciprocal exchanges did not confer virulence to SMV-N-derived P3 chimeras. Here, we describe virulent SMV-N-derived P3 chimeras containing the full-length or the N-terminal P3 from SMV-G7 or SMV-G7d, with or without additional mutations in P3, that were selected on Rsv1-genotype soybean by sequential transfers on rsv1 and Rsv1-genotype soybean. Sequence analyses of the P3 and helper-component proteinase (HC-Pro) cistrons of progeny recovered from Rsv1-genotype soybean consistently revealed the presence of mutations in HC-Pro. Interestingly, the precise mutations in HC-Pro required for the adaptation varied among the chimeras. No mutation was detected in the HC-Pro of progeny passaged continuously in rsv1-genotype soybean, suggesting that selection is a consequence of pressure imposed by Rsv1. Mutations in HC-Pro alone failed to confer virulence to SMV-N; however, reconstruction of mutations in HC-Pro of the SMV-N-derived P3 chimeras resulted in virulence. Taken together, the data suggest that HC-Pro complementation of P3 is essential for SMV virulence on Rsv1-genotype soybean.

ELECTRON MICROSCOPY OF TWO SMALL SPHERICAL PLANT VIRUSES IN THIN SECTIONS

1966 ◽  
Vol 44 (6) ◽  
pp. 821-826 ◽  
Author(s):  
J. R. Edwardson ◽  
D. E. Purcifull ◽  
R. G. Christie
Keyword(s):  
Electron Microscopy ◽  
Mosaic Virus ◽  
Leaf Tissue ◽  
Plant Viruses ◽  
Tobacco Necrosis Virus ◽  
Necrosis Virus ◽  
Thin Sections ◽  
Virus Particles ◽  
Southern Bean Mosaic Virus

Particles within lesions of leaf tissue infected with either tobacco necrosis virus (TNV) or southern bean mosaic virus (SBMV) were compared with particles in embedded pellets of purified preparations of these viruses by an examination of thin sections. The mode of the diameters of particles in tissues and pellets was 20.5 mµ.It is assumed that the particles in infected tissues are virus particles on the basis of their similarities in size, shape, and arrangement with the particles in purified preparations.

Research on Measures of Reducing Environmental Pollutions by Empty Capsid Virus Particles with Vaccine of Foot and Mouth Disease Virus to Control FMD

2014 ◽  
Vol 1023 ◽  
pp. 257-261
Author(s):  
Qi Hong ◽  
Zi Hong Liu ◽  
Duan Dan Han
Keyword(s):  
Virus Particle ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Promising Candidate ◽  
Effective Measure ◽  
Virus Particles ◽  
Empty Capsid ◽  
Mouth Disease Virus ◽  
Foot And Mouth ◽  
Potential Benefits

Foot-and-mouth disease (FMD) is a highly contagious disease in cloven-hoofed animals, and had been broken out worldwide several times in recent years. In order to extinct outbreak of FMD, a large number of infected animals are slaughtered in some countries, and the slaughterings had been caused a series of environmental pollutions seriously. To reduce this kind of pollution, vaccination is an effective measure to protect animals against FMD, however, FMD virus (FMDV) escaping from manufacturing plant and inactivated incompletely during vaccine production could cause an outbreak of FMD. Therefore, inactivated FMDV vaccines are not safe to animals and environment. FMDV empty capsid (lacking nucleic acid) can elicit the same antibody response as infectious FMDV, thus, empty capsid virus particle vaccine of FMDV would be the most promising candidate vaccine for its safety and protection against FMDV. In this report, we studied the empty capsid virus particle vaccine of FMDV to control FMD and its potential benefits to the environment.

scholarly journals Structural Fingerprinting: Subgrouping of Comoviruses by Structural Studies of Red Clover Mottle Virus to 2.4-Å Resolution and Comparisons with Other Comoviruses

2000 ◽  
Vol 74 (1) ◽  
pp. 493-504 ◽  
Author(s):  
Tianwei Lin ◽  
Anthony J. Clark ◽  
Zhongguo Chen ◽  
Michael Shanks ◽  
Jin-Bi Dai ◽  
...  
Keyword(s):  
Mosaic Virus ◽  
Red Clover ◽  
Plant Viruses ◽  
Small Subunit ◽  
Mottle Virus ◽  
Coat Proteins ◽  
Structural Studies ◽  
Bean Pod Mottle Virus ◽  
X Ray ◽  
N Terminus

ABSTRACT Red clover mottle virus (RCMV) is a member of the comoviruses, a group of picornavirus-like plant viruses. The X-ray structure of RCMV strain S has been determined and refined to 2.4 Å. The overall structure of RCMV is similar to that of two other comoviruses, Cowpea mosaic virus (CPMV) and Bean pod mottle virus (BPMV). The sequence of the coat proteins of RCMV strain O were modeled into the capsid structure of strain S without causing any distortion, confirming the close resemblance between the two strains. By comparing the RCMV structure with that of other comoviruses, a structural fingerprint at the N terminus of the small subunit was identified which allowed subgrouping of comoviruses into CPMV-like and BPMV-like viruses.

scholarly journals Conversion in the Requirement of Coat Protein in Cell-to-Cell Movement Mediated by the Cucumber Mosaic Virus Movement Protein

2001 ◽  
Vol 75 (17) ◽  
pp. 8045-8053 ◽  
Author(s):  
Hideaki Nagano ◽  
Kazuyuki Mise ◽  
Iwao Furusawa ◽  
Tetsuro Okuno
Keyword(s):  
Amino Acids ◽  
Coat Protein ◽  
Cucumber Mosaic Virus ◽  
Mosaic Virus ◽  
Movement Protein ◽  
Cell Movement ◽  
Plant Viruses ◽  
Brome Mosaic Virus ◽  
Viral Movement ◽  
Intercellular Movement

ABSTRACT Plant viruses have movement protein (MP) gene(s) essential for cell-to-cell movement in hosts. Cucumber mosaic virus (CMV) requires its own coat protein (CP) in addition to the MP for intercellular movement. Our present results using variants of both CMV and a chimeric Brome mosaic virus with the CMV MP gene revealed that CMV MP truncated in its C-terminal 33 amino acids has the ability to mediate viral movement independently of CP. Coexpression of the intact and truncated CMV MPs extremely reduced movement of the chimeric viruses, suggesting that these heterogeneous CMV MPs function antagonistically. Sequential deletion analyses of the CMV MP revealed that the dispensability of CP occurred when the C-terminal deletion ranged between 31 and 36 amino acids and that shorter deletion impaired the ability of the MP to promote viral movement. This is the first report that a region of MP determines the requirement of CP in cell-to-cell movement of a plant virus.

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