scholarly journals Diversity of Plant Virus Movement Proteins: What Do They Have in Common?

Processes ◽  
2020 ◽  
Vol 8 (12) ◽  
pp. 1547
Author(s):  
Yuri L. Dorokhov ◽  
Ekaterina V. Sheshukova ◽  
Tatiana E. Byalik ◽  
Tatiana V. Komarova
Keyword(s):  
Movement Protein ◽  
Plant Viruses ◽  
Movement Proteins ◽  
Vitro Binding ◽  
Specific Manner ◽  
Intercellular Movement ◽  
Movement Function ◽  
In Trans ◽  
Viral Reproduction

The modern view of the mechanism of intercellular movement of viruses is based largely on data from the study of the tobacco mosaic virus (TMV) 30-kDa movement protein (MP). The discovered properties and abilities of TMV MP, namely, (a) in vitro binding of single-stranded RNA in a non-sequence-specific manner, (b) participation in the intracellular trafficking of genomic RNA to the plasmodesmata (Pd), and (c) localization in Pd and enhancement of Pd permeability, have been used as a reference in the search and analysis of candidate proteins from other plant viruses. Nevertheless, although almost four decades have passed since the introduction of the term “movement protein” into scientific circulation, the mechanism underlying its function remains unclear. It is unclear why, despite the absence of homology, different MPs are able to functionally replace each other in trans-complementation tests. Here, we consider the complexity and contradictions of the approaches for assessment of the ability of plant viral proteins to perform their movement function. We discuss different aspects of the participation of MP and MP/vRNA complexes in intra- and intercellular transport. In addition, we summarize the essential MP properties for their functioning as “conditioners”, creating a favorable environment for viral reproduction.

scholarly journals Stability in vitro of the 69K movement protein of Turnip yellow mosaic virus is regulated by the ubiquitin-mediated proteasome pathway

2002 ◽  
Vol 83 (12) ◽  
pp. 3187-3197 ◽  
Author(s):  
Gabrièle Drugeon ◽  
Isabelle Jupin
Keyword(s):  
Mosaic Virus ◽  
Movement Protein ◽  
Cell Movement ◽  
Plant Viruses ◽  
Yellow Mosaic Virus ◽  
Turnip Yellow Mosaic Virus ◽  
Movement Proteins ◽  
Transient Nature ◽  
Reticulocyte Lysate

Plant viruses move to adjacent cells with the use of virus-encoded cell-to-cell movement proteins. Using proteins produced by in vitro translation, we present evidence that the ‘69K’ movement protein of Turnip yellow mosaic virus (TYMV) is recognized as a substrate for the attachment of polyubiquitin chains and for subsequent rapid and selective proteolysis by the proteasome, the ATP-dependent proteolytic system present in reticulocyte lysate. Truncation of the 69K protein suggests the existence of two degradation signals within its sequence. We propose that selective degradation of virus movement proteins may contribute to the previously reported transient nature of their accumulation during infection.

scholarly journals The Potato Virus X TGBp2 Protein Plays Dual Functional Roles in Viral Replication and Movement

2018 ◽  
Vol 93 (5) ◽  
Author(s):  
Xiaoyun Wu ◽  
Jiahui Liu ◽  
Mengzhu Chai ◽  
Jinhui Wang ◽  
Dalong Li ◽  
...  
Keyword(s):  
Triple Gene Block ◽  
Potato Virus X ◽  
Plant Viruses ◽  
Open Reading Frames ◽  
Movement Proteins ◽  
Gene Block ◽  
Functional Roles ◽  
Viral Rdrp ◽  
Dual Functional ◽  
Intercellular Movement

ABSTRACTPlant viruses usually encode one or more movement proteins (MP) to accomplish their intercellular movement. A group of positive-strand RNA plant viruses requires three viral proteins (TGBp1, TGBp2, and TGBp3) that are encoded by an evolutionarily conserved genetic module of three partially overlapping open reading frames (ORFs), termed the triple gene block (TGB). However, how these three viral movement proteins function cooperatively in viral intercellular movement is still elusive. Using a novelin vivodouble-stranded RNA (dsRNA) labeling system, we showed that the dsRNAs generated by potato virus X (PVX) RNA-dependent RNA polymerase (RdRp) are colocalized with viral RdRp, which are further tightly covered by “chain mail”-like TGBp2 aggregates and localizes alongside TGBp3 aggregates. We also discovered that TGBp2 interacts with the C-terminal domain of PVX RdRp, and this interaction is required for the localization of TGBp3 and itself to the RdRp/dsRNA bodies. Moreover, we reveal that the central and C-terminal hydrophilic domains of TGBp2 are required to interact with viral RdRp. Finally, we demonstrate that knockout of the entire TGBp2 or the domain involved in interacting with viral RdRp attenuates both PVX replication and movement. Collectively, these findings suggest that TGBp2 plays dual functional roles in PVX replication and intercellular movement.IMPORTANCEMany plant viruses contain three partially overlapping open reading frames (ORFs), termed the triple gene block (TGB), for intercellular movement. However, how the corresponding three proteins coordinate their functions remains obscure. In the present study, we provided multiple lines of evidence supporting the notion that PVX TGBp2 functions as the molecular adaptor bridging the interaction between the RdRp/dsRNA body and TGBp3 by forming “chain mail”-like structures in the RdRp/dsRNA body, which can also enhance viral replication. Taken together, our results provide new insights into the replication and movement of PVX and possibly also other TGB-containing plant 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.

scholarly journals Identification of a Movement Protein of Rice Yellow Stunt Rhabdovirus

2005 ◽  
Vol 79 (4) ◽  
pp. 2108-2114 ◽  
Author(s):  
Yan-Wei Huang ◽  
Yun-Feng Geng ◽  
Xiao-Bao Ying ◽  
Xiao-Ying Chen ◽  
Rong-Xiang Fang
Keyword(s):  
Movement Protein ◽  
Specific Interaction ◽  
Protein Structures ◽  
Cell Movement ◽  
Protein Product ◽  
N Protein ◽  
Intercellular Movement ◽  
Main Component ◽  
Plant Rhabdovirus

ABSTRACT Rice yellow stunt rhabdovirus (RYSV) encodes seven genes in its negative-sense RNA genome in the order 3′-N-P-3-M-G-6-L-5′. The existence of gene 3 in the RYSV genome and an analogous gene(s) of other plant rhabdoviruses positioned between the P and M genes constitutes a unique feature for plant rhabdoviruses that is distinct from animal-infecting rhabdoviruses in which the P and M genes are directly linked. However, little is known about the function of these extra plant rhabdovirus genes. Here we provide evidence showing that the protein product encoded by gene 3 of RYSV, P3, possesses several properties related to a viral cell-to-cell movement protein (MP). Analyses of the primary and secondary protein structures suggested that RYSV P3 is a member of the “30K” superfamily of viral MPs. Biolistic bombardment transcomplementation experiments demonstrated that RYSV P3 can support the intercellular movement of a movement-deficient potexvirus mutant in Nicotiana benthamiana leaves. In addition, Northwestern blot analysis indicated that the RYSV P3 protein can bind single-stranded RNA in vitro, a common feature of viral MPs. Finally, glutathione S- transferase pull-down assays revealed a specific interaction between the RYSV P3 protein and the N protein which is a main component of the ribonucleocapsid, a subviral structure believed to be involved in the intercellular movement of plant rhabdoviruses. Together, these data suggest that RYSV P3 is likely a MP of RYSV, thus representing the first example of characterized MPs for plant rhabdoviruses.

scholarly journals Evidence that Binding of Cucumber Necrosis Virus to Vector Zoospores Involves Recognition of Oligosaccharides

2003 ◽  
Vol 77 (7) ◽  
pp. 3922-3928 ◽  
Author(s):  
Kishore Kakani ◽  
Marjorie Robbins ◽  
D'Ann Rochon
Keyword(s):  
Plant Viruses ◽  
Necrosis Virus ◽  
Molecular Features ◽  
Olpidium Bornovanus ◽  
Low Concentrations ◽  
Vitro Binding ◽  
Cucumber Necrosis Virus ◽  
Specific Receptors ◽  
Mannose Derivatives

ABSTRACT Despite the importance of vectors in natural dissemination of plant viruses, relatively little is known about the molecular features of viruses and vectors that permit their interaction in nature. Cucumber necrosis virus (CNV) is a small spherical virus whose transmission in nature is facilitated by zoospores of the fungus Olpidium bornovanus. Previous studies have shown that specific regions of the CNV capsid are involved in transmission and that transmission defects in several CNV transmission mutants are due to inefficient attachment of virions to the zoospore surface. In this study, we have undertaken to determine if zoospores contain specific receptors for CNV. We show that in vitro binding of CNV to zoospores is saturable and that vector zoospores bind CNV more efficiently than nonvector zoospores. Further studies show that treatment of zoospores with periodate and trypsin reduces CNV binding, suggesting the involvement of glycoproteins in zoospore attachment. In virus overlay assays, CNV binds to several proteins, whereas CNV transmission mutants either fail to bind or bind at significantly reduced levels. The possible involvement of specific sugars in attachment was investigated by incubating CNV with zoospores in the presence of various sugars. Two mannose derivatives (methyl α-d-mannopyranoside and d-mannosamine), as well as three mannose-containing oligosaccharides (mannotriose, α3,α6-mannopentaose, and yeast mannan) and l-(−)-fucose, all inhibited CNV binding at relatively low concentrations. Taken together, our studies suggest that binding of CNV to zoospores is mediated by specific mannose and/or fucose-containing oligosaccharides. This is the first time sugars have been implicated in transmission of a plant virus.

scholarly journals Plant Virus Cell-to-Cell Movement Is Not Dependent on the Transmembrane Disposition of Its Movement Protein

2009 ◽  
Vol 83 (11) ◽  
pp. 5535-5543 ◽  
Author(s):  
Luis Martínez-Gil ◽  
Jesús A. Sánchez-Navarro ◽  
Antonio Cruz ◽  
Vicente Pallás ◽  
Jesús Pérez-Gil ◽  
...  
Keyword(s):  
Movement Protein ◽  
Transmembrane Protein ◽  
Cell Movement ◽  
Plant Viruses ◽  
Integral Membrane Proteins ◽  
Membrane Interface ◽  
Hydrophobic Region ◽  
Movement Proteins ◽  
Structural Conformation ◽  
Prunus Necrotic Ringspot Virus

ABSTRACT The cell-to-cell transport of plant viruses depends on one or more virus-encoded movement proteins (MPs). Some MPs are integral membrane proteins that interact with the membrane of the endoplasmic reticulum, but a detailed understanding of the interaction between MPs and biological membranes has been lacking. The cell-to-cell movement of the Prunus necrotic ringspot virus (PNRSV) is facilitated by a single MP of the 30K superfamily. Here, using a myriad of biochemical and biophysical approaches, we show that the PNRSV MP contains only one hydrophobic region (HR) that interacts with the membrane interface, as opposed to being a transmembrane protein. We also show that a proline residue located in the middle of the HR constrains the structural conformation of this region at the membrane interface, and its replacement precludes virus movement.

scholarly journals P3N-PIPO Interacts with P3 via the Shared N-Terminal Domain To Recruit Viral Replication Vesicles for Cell-to-Cell Movement

2020 ◽  
Vol 94 (8) ◽  
Author(s):  
Mengzhu Chai ◽  
Xiaoyun Wu ◽  
Jiahui Liu ◽  
Yue Fang ◽  
Yameng Luan ◽  
...  
Keyword(s):  
Viral Replication ◽  
Mosaic Virus ◽  
Essential Role ◽  
Movement Protein ◽  
Cell Movement ◽  
Plant Viruses ◽  
Turnip Mosaic Virus ◽  
Limited Information ◽  
Intercellular Movement ◽  
Model Virus

ABSTRACT P3N-PIPO, the only dedicated movement protein (MP) of potyviruses, directs cylindrical inclusion (CI) protein from the cytoplasm to the plasmodesma (PD), where CI forms conical structures for intercellular movement. To better understand potyviral cell-to-cell movement, we further characterized P3N-PIPO using Turnip mosaic virus (TuMV) as a model virus. We found that P3N-PIPO interacts with P3 via the shared P3N domain and that TuMV mutants lacking the P3N domain of either P3N-PIPO or P3 are defective in cell-to-cell movement. Moreover, we found that the PIPO domain of P3N-PIPO is sufficient to direct CI to the PD, whereas the P3N domain is necessary for localization of P3N-PIPO to 6K2-labeled vesicles or aggregates. Finally, we discovered that the interaction between P3 and P3N-PIPO is essential for the recruitment of CI to cytoplasmic 6K2-containing structures and the association of 6K2-containing structures with PD-located CI inclusions. These data suggest that both P3N and PIPO domains are indispensable for potyviral cell-to-cell movement and that the 6K2 vesicles in proximity to PDs resulting from multipartite interactions among 6K2, P3, P3N-PIPO, and CI may also play an essential role in this process. IMPORTANCE Potyviruses include numerous economically important viruses that represent approximately 30% of known plant viruses. However, there is still limited information about the mechanism of potyviral cell-to-cell movement. Here, we show that P3N-PIPO interacts with and recruits CI to the PD via the PIPO domain and interacts with P3 via the shared P3N domain. We further report that the interaction of P3N-PIPO and P3 is associated with 6K2 vesicles and brings the 6K2 vesicles into proximity with PD-located CI structures. These results support the notion that the replication and cell-to-cell movement of potyviruses are processes coupled by anchoring viral replication complexes at the entrance of PDs, which greatly increase our knowledge of the intercellular movement of potyviruses.

scholarly journals The Movement Protein of Cowpea Mosaic Virus Binds GTP and Single-Stranded Nucleic Acid In Vitro

2004 ◽  
Vol 78 (3) ◽  
pp. 1591-1594 ◽  
Author(s):  
C. M. Carvalho ◽  
J. Pouwels ◽  
J. W. M. van Lent ◽  
T. Bisseling ◽  
R. W. Goldbach ◽  
...  
Keyword(s):  
Mosaic Virus ◽  
Binding Sites ◽  
Rna Binding ◽  
Mutational Analysis ◽  
Movement Protein ◽  
Cowpea Mosaic Virus ◽  
Gtp Binding ◽  
Targeted Transport ◽  
Specific Manner

ABSTRACT The movement protein (MP) of Cowpea mosaic virus forms tubules in plasmodesmata to enable the transport of mature virions. Here it is shown that the MP is capable of specifically binding riboguanosine triphosphate and that mutational analysis suggests that GTP binding plays a role in the targeted transport of the MP. Furthermore, the MP is capable of binding both single-stranded RNA and single-stranded DNA in a non-sequence-specific manner, and the GTP- and RNA-binding sites do not overlap.

scholarly journals Caulimoviridae Tubule-Guided Transport Is Dictated by Movement Protein Properties

2010 ◽  
Vol 84 (8) ◽  
pp. 4109-4112 ◽  
Author(s):  
Jesús Sánchez-Navarro ◽  
Thor Fajardo ◽  
Stefania Zicca ◽  
Vicente Pallás ◽  
Livia Stavolone
Keyword(s):  
Movement Protein ◽  
Rna Virus ◽  
Alfalfa Mosaic Virus ◽  
Plant Viruses ◽  
Dna Virus ◽  
Movement Proteins ◽  
Dna And Rna ◽  
Protein Properties ◽  
Nucleoprotein Complexes ◽  
Virus Genomes

ABSTRACT Plant viruses move through plasmodesmata (PD) either as nucleoprotein complexes (NPCs) or as tubule-guided encapsidated particles with the help of movement proteins (MPs). To explore how and why MPs specialize in one mechanism or the other, we tested the exchangeability of MPs encoded by DNA and RNA virus genomes by means of an engineered alfalfa mosaic virus (AMV) system. We show that Caulimoviridae (DNA genome virus) MPs are competent for RNA virus particle transport but are unable to mediate NPC movement, and we discuss this restriction in terms of the evolution of DNA virus MPs as a means of mediating DNA viral genome entry into the RNA-trafficking PD pathway.

In Vitro and in Vivo Comparison of Binding of 99m-Tc-Iabeled Anti-CEA MAb F33-104 with 99m-Tc-labeled Anti-CEA MAb BW431/26

1999 ◽  
Vol 38 (04) ◽  
pp. 115-119
Author(s):  
N. Oriuchi ◽  
S. Sugiyama ◽  
M. Kuroki ◽  
Y. Matsuoka ◽  
S. Tanada ◽  
...  
Keyword(s):  
Nude Mice ◽  
Binding Capacity ◽  
Colon Adenocarcinoma ◽  
Human Colon ◽  
Cell Binding ◽  
Vitro Binding ◽  
Labeling Method ◽  
Human Colon Adenocarcinoma

Summary Aim: The purpose of this study was to assess the potential for radioimmunodetection (RAID) of murine anti-carcinoembryonic antigen (CEA) monoclonal antibody (MAb) F33-104 labeled with technetium-99m (99m-Tc) by a reduction-mediated labeling method. Methods: The binding capacity of 99m-Tc-labeled anti-CEA MAb F33-104 with CEA by means of in vitro procedures such as immunoradiometric assay and cell binding assay and the biodistribution of 99m-Tc-labeled anti-CEA MAb F33-104 in normal nude mice and nude mice bearing human colon adenocarcinoma LS180 tumor were investigated and compared with 99m-Tc-labeled anti-CEA MAb BW431/26. Results: The in vitro binding rate of 99m-Tc-labeled anti-CEA MAb F33-104 with CEA in solution and attached to the cell membrane was significantly higher than 99m-Tclabeled anti-CEA MAb BW431/261 (31.4 ± 0.95% vs. 11.9 ± 0.55% at 100 ng/mL of soluble CEA, 83.5 ± 2.84% vs. 54.0 ± 2.54% at 107 of LS 180 cells). In vivo, accumulation of 99m-Tc-labeled anti-CEA MAb F33-104 was higher at 18 h postinjection than 99m-Tc-labeled anti-CEA MAb BW431/26 (20.1 ± 3.50% ID/g vs. 14.4 ± 3.30% ID/g). 99m-Tcactivity in the kidneys of nude mice bearing tumor was higher at 18 h postinjection than at 3 h (12.8 ± 2.10% ID/g vs. 8.01 ± 2.40% ID/g of 99m-Tc-labeled anti-CEA MAb F33-104, 10.7 ± 1.70% ID/g vs. 8.10 ± 1.75% ID/g of 99m-Tc-labeled anti-CEA MAb BW431/26). Conclusion: 99m-Tc-labeled anti-CEA MAb F33-104 is a potential novel agent for RAID of recurrent colorectal cancer.

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