scholarly journals Enhancing Capsid Proteins Capacity in Plant Virus-Vector Interactions and Virus Transmission

Cells ◽  
2021 ◽  
Vol 10 (1) ◽  
pp. 90
Author(s):  
Alexey Agranovsky
Keyword(s):  
Capsid Protein ◽  
Virus Transmission ◽  
Minor Component ◽  
Aphid Transmission ◽  
Plant Viruses ◽  
Cauliflower Mosaic Virus ◽  
Capsid Proteins ◽  
Helper Component ◽  
Associated Proteins ◽  
A Minor

Vector transmission of plant viruses is basically of two types that depend on the virus helper component proteins or the capsid proteins. A number of plant viruses belonging to disparate groups have developed unusual capsid proteins providing for interactions with the vector. Thus, cauliflower mosaic virus, a plant pararetrovirus, employs a virion associated p3 protein, the major capsid protein, and a helper component for the semi-persistent transmission by aphids. Benyviruses encode a capsid protein readthrough domain (CP-RTD) located at one end of the rod-like helical particle, which serves for the virus transmission by soil fungal zoospores. Likewise, the CP-RTD, being a minor component of the luteovirus icosahedral virions, provides for persistent, circulative aphid transmission. Closteroviruses encode several CPs and virion-associated proteins that form the filamentous helical particles and mediate transmission by aphid, whitefly, or mealybug vectors. The variable strategies of transmission and evolutionary ‘inventions’ of the unusual capsid proteins of plant RNA viruses are discussed.

scholarly journals Engineering of Adenovirus Vectors Containing Heterologous Peptide Sequences in the C Terminus of Capsid Protein IX

2002 ◽  
Vol 76 (14) ◽  
pp. 6893-6899 ◽  
Author(s):  
Igor P. Dmitriev ◽  
Elena A. Kashentseva ◽  
David T. Curiel
Keyword(s):  
Heparan Sulfate ◽  
Capsid Protein ◽  
Minor Component ◽  
Cell Types ◽  
Binding Motif ◽  
Flag Epitope ◽  
C Terminus ◽  
Protein Ix ◽  
A Minor ◽  
Carboxy Terminal

ABSTRACT The utility of the present generation of adenovirus (Ad) vectors for gene therapy applications could be improved by restricting native viral tropism to selected cell types. In order to achieve modification of Ad tropism, we proposed to exploit a minor component of viral capsid, protein IX (pIX), for genetic incorporation of targeting ligands. Based on the proposed structure of pIX, we hypothesized that its C terminus could be used as a site for incorporation of heterologous peptide sequences. We engineered recombinant Ad vectors containing modified pIX carrying a carboxy-terminal Flag epitope along with a heparan sulfate binding motif consisting of either eight consecutive lysines or a polylysine sequence. Using an anti-Flag antibody, we have shown that modified pIXs are incorporated into virions and display Flag-containing C-terminal sequences on the capsid surface. In addition, both lysine octapeptide and polylysine ligands were accessible for binding to heparin-coated beads. In contrast to virus bearing lysine octapeptide, Ad vector displaying a polylysine was capable of recognizing cellular heparan sulfate receptors. We have demonstrated that incorporation of a polylysine motif into the pIX ectodomain results in a significant augmentation of Ad fiber knob-independent infection of CAR-deficient cell types. Our data suggest that the pIX ectodomain can serve as an alternative to the fiber knob, penton base, and hexon proteins for incorporation of targeting ligands for the purpose of Ad tropism modification.

scholarly journals Biochemical Characterization of the Helper Component of Cauliflower Mosaic Virus

2001 ◽  
Vol 75 (18) ◽  
pp. 8538-8546 ◽  
Author(s):  
Eugenie Hebrard ◽  
Martin Drucker ◽  
Denis Leclerc ◽  
Thomas Hohn ◽  
Marilyne Uzest ◽  
...  
Keyword(s):  
Mosaic Virus ◽  
Biochemical Characterization ◽  
Active Form ◽  
Recombinant Baculovirus ◽  
Aphid Transmission ◽  
Cauliflower Mosaic Virus ◽  
Biologically Active ◽  
Size Exclusion ◽  
Viral Gene ◽  
Helper Component

ABSTRACT The helper component of Cauliflower mosaic virus is encoded by viral gene II. This protein (P2) is dispensable for virus replication but required for aphid transmission. The purification of P2 has never been reported, and hence its biochemical properties are largely unknown. We produced the P2 protein via a recombinant baculovirus with a His tag fused at the N terminus. The fusion protein was purified by affinity chromatography in a soluble and biologically active form. Matrix-assisted laser desorption time-of-flight mass spectrometry demonstrated that P2 is not posttranslationally modified. UV circular dichroism revealed the secondary structure of P2 to be 23% α-helical. Most α-helices are suggested to be located in the C-terminal domain. Using size exclusion chromatography and aphid transmission testing, we established that the active form of P2 assembles as a huge soluble oligomer containing 200 to 300 subunits. We further showed that P2 can also polymerize as long paracrystalline filaments. We mapped P2 domains involved in P2 self-interaction, presumably through coiled-coil structures, one of which is proposed to form a parallel trimer. These regions have previously been reported to also interact with viral P3, another protein involved in aphid transmission. Possible interference between the two types of interaction is discussed with regard to the biological activity of P2.

scholarly journals A Single Amino Acid Position in the Helper Component of Cauliflower Mosaic Virus Can Change the Spectrum of Transmitting Vector Species

2005 ◽  
Vol 79 (21) ◽  
pp. 13587-13593 ◽  
Author(s):  
Aranzazu Moreno ◽  
Eugénie Hébrard ◽  
Marilyne Uzest ◽  
Stéphane Blanc ◽  
Alberto Fereres
Keyword(s):  
Amino Acid ◽  
Mosaic Virus ◽  
Amino Acid Position ◽  
Plant Viruses ◽  
Aphid Species ◽  
Virus Vector ◽  
Cauliflower Mosaic Virus ◽  
Vector Species ◽  
Helper Component ◽  
Mode Of Transmission

ABSTRACT Viruses frequently use insect vectors to effect rapid spread through host populations. In plant viruses, vector transmission is the major mode of transmission, used by nearly 80% of species described to date. Despite the importance of this phenomenon in epidemiology, the specificity of the virus-vector relationship is poorly understood at both the molecular and the evolutionary level, and very limited data are available on the precise viral protein motifs that control specificity. Here, using the aphid-transmitted Cauliflower mosaic virus (CaMV) as a biological model, we confirm that the “noncirculative” mode of transmission dominant in plant viruses (designated “mechanical vector transmission” in animal viruses) involves extremely specific virus-vector recognition, and we identify an amino acid position in the “helper component” (HC) protein of CaMV involved in such recognition. Site-directed mutagenesis revealed that changing the residue at this position can differentially affect transmission rates obtained with various aphid species, thus modifying the spectrum of vector species for CaMV. Most interestingly, in a virus line transmitted by a single vector species, we observed the rapid appearance of a spontaneous mutant specifically losing its transmissibility by another aphid species. Hence, in addition to the first identification of an HC motif directly involved in specific vector recognition, we demonstrate that change of a virus to a different vector species requires only a single mutation and can occur rapidly and spontaneously.

scholarly journals Tenuivirususes a molecular bridge strategy to overcome insect midgut barriers for virus persistent transmission

2018 ◽  
Author(s):  
Gang Lu ◽  
Shuo Li ◽  
Changwei Zhou ◽  
Xin Qian ◽  
Qing Xiang ◽  
...  
Keyword(s):  
Brown Planthopper ◽  
Specific Interaction ◽  
Virus Transmission ◽  
Plant Viruses ◽  
Insect Vector ◽  
Terminal Protein ◽  
Insect Midgut ◽  
Helper Component ◽  
Vector Interaction ◽  
Molecular Bridge

AbstractMany persistent transmitted plant viruses, includingRice stripe tenuivirus(RSV), cause serious damages to crop productions in China and worldwide. Although many reports have indicated that successful insect-mediated virus transmission depends on proper virus–insect vector interactions, the mechanism(s) controlling interactions between viruses and insect vectors for virus persistent transmission remained poorly understood. In this study, we used RSV and its small brown planthopper (SBPH) vector as a working model to elucidate the molecular mechanism controlling RSV virion entrance into SBPH midgut for persistent transmission. We have now demonstrated that this non-envelopedTenuivirususes its non-structural glycoprotein NSvc2 as a helper component to bridge the specific interaction between virion and SBPH midgut cells, leading to overcome SBPH midgut barriers for virus persistent transmission. In the absence of this glycoprotein, purified RSV virion is not capable of entering SBPH midgut cells. In RSV-infected cells, glycoprotein NSvc2 is processed into two mature proteins: an amino-terminal protein NSvc2-N and a carboxyl-terminal protein NSvc2-C. We determined that NSvc2-N interacted with RSV virion and bound directly to midgut lumen surface via its N-glycosylation sites. Upon recognition by midgut cells, the midgut cells underwent endocytosis followed by compartmentalizing RSV virion and NSvc2 into early and then late endosomes. The acidic condition inside the late endosome triggered conformation change of NSvc2-C and caused cell membrane fusion via its highly conserved fusion loop motifs, leading to the release of RSV virion from endosome into cytosol. In summary, our results showed for the first time that a riceTenuivirususes a molecular bridge strategy to ensure proper interactions between virus and insect midgut for successful persistent transmission.Author summaryOver 75% of the known plant viruses are insect transmitted. Understanding how plant viruses interacted with their insect vectors during virus transmission is one of the key steps to manage virus diseases worldwide. Both the direct and indirect virus–insect vector interaction models have been proposed for virus non-persistent and semi-persistent transmission. However, the indirect virus–vector interaction mechanism during virus persistent transmission has not been reported previously. In this study, we developed a new reverse genetics technology and demonstrated that the circulative and propagative transmittedRice stripe tenuivirusutilizes a glycoprotein NSvc2 as a helper component to ensure a specific interaction betweenTenuivirusvirion and midgut cells of small brown planthopper (SBPH), leading to conquering the midgut barrier of SBPH. This is the first report of a helper component mediated-molecular bridge mechanism for virus persistent transmission. These new findings and our new model on persistent transmission expand our understanding of molecular mechanism(s) controlling virus–insect vector interactions during virus transmission in nature.

scholarly journals MAP 1C is a microtubule-activated ATPase which translocates microtubules in vitro and has dynein-like properties.

1987 ◽  
Vol 105 (3) ◽  
pp. 1273-1282 ◽  
Author(s):  
B M Paschal ◽  
H S Shpetner ◽  
R B Vallee
Keyword(s):  
Atpase Activity ◽  
Heavy Chain ◽  
Sedimentation Coefficient ◽  
Minor Component ◽  
High Molecular Mass ◽  
Microtubule Associated Proteins ◽  
Associated Proteins ◽  
Axonemal Dynein ◽  
A Minor

We observe that one of the high molecular mass microtubule-associated proteins (MAPs) from brain exhibits nucleotide-dependent binding to microtubules. We identify the protein as MAP IC, which was previously described in this laboratory as a minor component of standard microtubule preparations (Bloom, G.S., T. Schoenfeld, and R.B. Vallee, 1984, J. Cell Biol., 98:320-330). We find that MAP 1C is enriched in microtubules prepared in the absence of nucleotide. Kinesin is also found in these preparations, but can be specifically extracted with GTP. A fraction highly enriched in MAP 1C can be prepared by subsequent extraction of the microtubules with ATP. Two activities cofractionate with MAP 1C upon further purification, a microtubule-activated ATPase activity and a microtubule-translocating activity. These activities indicate a role for the protein in cytoplasmic motility. MAP 1C coelectrophoreses with the beta heavy chain of Chlamydomonas flagellar dynein, and has a sedimentation coefficient of 20S. Exposure to ultraviolet light in the presence of vanadate and ATP results in the production of two large fragments of MAP 1C. These characteristics suggest that MAP 1C may be a cytoplasmic analogue of axonemal dynein.

Helper component for aphid transmission encoded by region II of cauliflower mosaic virus DNA

Virology ◽  
1983 ◽  
Vol 129 (1) ◽  
pp. 25-30 ◽  
Author(s):  
Susan L. Armour ◽  
Ulrich Melcher ◽  
Thomas P. Pirone ◽  
D.J. Lyttle ◽  
R.C. Essenberg
Keyword(s):  
Mosaic Virus ◽  
Aphid Transmission ◽  
Cauliflower Mosaic Virus ◽  
Helper Component ◽  
Region Ii

Age- and ploidy-related changes in rat liver nuclear proteins as assessed by one- and two-dimensional gel electrophoresis

1982 ◽  
Vol 60 (3) ◽  
pp. 204-214 ◽  
Author(s):  
Klaus Brasch
Keyword(s):  
Gel Electrophoresis ◽  
Minor Component ◽  
Subsequent Stage ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis ◽  
Nonhistone Proteins ◽  
Stage Of Development ◽  
Age Related ◽  
Associated Proteins ◽  
A Minor

Hepatocyte nuclei from young (3–5 week), mature (8–12 week), and aged (over 32 weeks) rats were isolated and characterized by flow cytometry. Nuclei were bulk separated into diploid (2C), tetraploid (4C), and octoploid (8C) enriched fractions on sucrose gradients. Total, 0.35 M NaCl soluble, and residual proteins were prepared from all nuclear stages and examined by one- and two-dimensional gel electrophoresis. Within limits of sensitivity of these techniques, the following general features emerged. (a) A majority of proteins visualized were common to and present in similar relative quantities in nuclei from all age and ploidy groups. (b) A relatively higher proportion of nonhistone proteins (NHP) were saline-soluble in 2C nuclei from young rats than at any subsequent stage of development. (c) Several age-related and to a lesser extent ploidy-related fluctuations in pattern among the NHP were evident. These reflected primarily differences in solubility rather than major quantitative changes among individual proteins. (d) Exceptions to the foregoing included a group of high molecular weight components (> 100 000), a major and a minor component between 45 000 and 50 000, and a heterogeneous group of proteins in 2C nuclei from very young animals. There were no obvious differences among the histones, although these proteins were not examined in detail. The complex pattern of changes observed are discussed in terms of known aspects of hepatocyte differentiation and are related to possible changes in nucleoplasmic, nuclear matrix and Hn-RNP associated proteins.

scholarly journals Aphid transmission of a Potexvirus, Foxtail mosaic virus, in the presence of the Potyvirus helper component proteinase

2021 ◽  
Author(s):  
Jun Jiang ◽  
Eric Yu ◽  
Clare L L Casteel
Keyword(s):  
Host Plant ◽  
Mosaic Virus ◽  
Physiological State ◽  
Potato Virus X ◽  
Aphid Transmission ◽  
Plant Viruses ◽  
Transmission Efficiency ◽  
Helper Component ◽  
Successful Infection ◽  
Helper Component Proteinase

To establish successful infections, plant viruses compete with the host plants for limited resources and thus alter the physiological state of the plants. After successful infection, insect vectors are required for the transmission of some plant viruses to the next host plant. One of the largest groups of plant viruses, the potyvirus, can be transmitted by aphids. During transmission, the potyvirus protein helper component proteinase (HC-Pro) binds to the yet-to-be-defined aphid receptor on the stylet, as well as to the virus particles through the Asp-Ala-Gly (DAG) motif of the viral coat protein. Previously it was determined that a naturally occurring DAG motif in the non-aphid transmissible potexvirus, Potato aucuba mosaic potexvirus (PAMV), is functional when the HC-Pro is provided through co-infection with a potyvirus. Further, the DAG motif of PAMV can be successfully transferred to another non-aphid transmissible potexvirus, Potato virus X (PVX), to convey aphid transmission capabilities. We expand on this previous work by demonstrating, the DAG motif from two different potyviruses, Sugarcane mosaic virus and Turnip mosaic virus, as well as the DAG motif from the previous potexvirus PAMV, can be added to another non-aphid transmissible potexvirus, Foxtail mosaic virus (FoMV), to make it aphid transmissible. Transmission efficiency varied from less than 10% to over 80% depending on the DAG motif and host plant used in transmission, suggesting not all DAG motifs are equal for engineering aphid transmission. The underlying mechanisms mediating this variation still need to be explored.

scholarly journals Mammalian alpha 1- and beta 1-syntrophin bind to the alternative splice-prone region of the dystrophin COOH terminus.

1995 ◽  
Vol 128 (3) ◽  
pp. 373-381 ◽  
Author(s):  
A Suzuki ◽  
M Yoshida ◽  
E Ozawa
Keyword(s):  
Binding Site ◽  
Protein Interactions ◽  
Minor Component ◽  
Amino Acid Residues ◽  
Protein Protein Interactions ◽  
Glycoprotein Complex ◽  
Associated Proteins ◽  
Alternatively Spliced ◽  
A Minor ◽  
Carboxy Terminal

The carboxy-terminal region of dystrophin has been suggested to be crucially important for its function to prevent muscle degeneration. We have previously shown that this region is the locus that interacts with the sarcolemmal glycoprotein complex, which mediates membrane anchoring of dystrophin, as well as with the cytoplasmic peripheral membrane protein, A0 and beta 1-syntrophin (Suzuki, A., M. Yoshida, K. Hayashi, Y. Mizuno, Y. Hagiwara, and E. Ozawa. 1994. Eur. J. Biochem. 220:283-292). In this work, by using the overlay assay technique developed previously, we further analyzed the dystrophin-syntrophin/A0 interaction. Two forms of mammalian syntrophin, alpha 1- and beta 1-syntrophin, were found to bind to very close but discrete regions on the dystrophin molecule. Their binding sites are located at the vicinity of the glycoprotein-binding site, and correspond to the amino acid residues encoded by exons 73-74 which are alternatively spliced out in some isoforms. This suggests that the function of syntrophin is tightly linked to the functional diversity among dystrophin isoforms. Pathologically, it is important that the binding site for alpha 1-syntrophin, which is predominantly expressed in skeletal muscle, coincides with the region whose deletion was suggested to result in a severe phenotype. In addition, A0, a minor component of dystrophin-associated proteins with a molecular mass of 94 kD which is immunochemically related to syntrophin, binds to the same site as beta 1-syntrophin. Finally, based on our accumulated evidence, we propose a revised model of the domain organization of dystrophin from the view point of protein-protein interactions.

Protonation effects on dynamic flux properties of aqueous metal complexes

2009 ◽  
Vol 74 (10) ◽  
pp. 1543-1557 ◽  
Author(s):  
Herman P. Van Leeuwen ◽  
Raewyn M. Town
Keyword(s):  
Complex Formation ◽  
Metal Ion ◽  
Good Description ◽  
Minor Component ◽  
Outer Sphere ◽  
Metal Species ◽  
Central Metal ◽  
Inner Sphere ◽  
A Minor ◽  
Protonated Ligand

The degree of (de)protonation of aqueous metal species has significant consequences for the kinetics of complex formation/dissociation. All protonated forms of both the ligand and the hydrated central metal ion contribute to the rate of complex formation to an extent weighted by the pertaining outer-sphere stabilities. Likewise, the lifetime of the uncomplexed metal is determined by all the various protonated ligand species. Therefore, the interfacial reaction layer thickness, μ, and the ensuing kinetic flux, Jkin, are more involved than in the conventional case. All inner-sphere complexes contribute to the overall rate of dissociation, as weighted by their respective rate constants for dissociation, kd. The presence of inner-sphere deprotonated H2O, or of outer-sphere protonated ligand, generally has a great impact on kd of the inner-sphere complex. Consequently, the overall flux can be dominated by a species that is a minor component of the bulk speciation. The concepts are shown to provide a good description of experimental stripping chronopotentiometric data for several protonated metal–ligand systems.

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