Fungus Transmission

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D'ann Rochon - One of the best experts on this subject based on the ideXlab platform.

  • Current Protocols in Microbiology - Fungal Transmission of plant viruses.
    Current protocols in microbiology, 2020
    Co-Authors: D'ann Rochon
    Abstract:

    Fungal zoospores of Olpidium species transmit several viruses in the family Tombusviridae as well as in the Ophio- and Varicosavirus genera. This unit describes procedures for virus Transmission by Olpidium sp. The method is useful for assessing fungal transmissibility of a given virus as well as for further studies on molecular and biological aspects of virus/vector interaction. Curr. Protoc. Microbiol. 12:16B.4.1-16B.4.17. © 2009 by John Wiley & Sons, Inc. Keywords: Olpidium bornovanus; Olpidium brassicae; Fungus Transmission

  • evaluation of the roles of specific regions of the cucumber necrosis virus coat protein arm in particle accumulation and Fungus Transmission
    Journal of Virology, 2006
    Co-Authors: D'ann Rochon
    Abstract:

    The Cucumber necrosis virus (CNV) particle is a T3 icosahedron composed of 180 identical coat protein (CP) subunits. Each CP subunit includes a 34-amino-acid (aa) arm which connects the RNA binding and shell domains. The arm is comprised of an 18-aa “” region and a 16-aa “” region, with the former contributing to a -annular structure involved in particle stability and the latter contributing to quasiequivalence and virion RNA binding. Previous work has shown that specific regions of the CNV capsid play important roles in Transmission by zoospores of the fungal vector Olpidium bornovanus and that particle expansion is essential for this process. To assess the importance of the two arm regions in particle accumulation, stability, and virus Transmission, five CP arm deletion mutants were constructed. Our findings indicate that () mutants are capable of producing particles in plants; however, the arm() and () mutants are not. In addition, () particles bind zoospores less efficiently than wild-type CNV and are not fungally transmissible. () particles are also less thermally stable and disassemble under swelling conditions. Our finding that () mutants can accumulate in plants suggests that other features of the virion, such as RNA/CP interactions, may also be important for particle stability. The capsids of many plant and animal viruses are multifunctional (2), having roles in genome protection, cell-to-cell and long-distance movement within plants (4), vector Transmission (9, 16, 21, 25), replication (1), and suppression of gene silencing (22, 34). Structural studies of several plant viruses have revealed that the overall architecture of the T3 capsid can be highly conserved between otherwise divergent virus groups, including those of several animal viruses (14). The structures of many plant virus particles have been obtained, and several in vitro studies have been conducted to assess the roles of the different structural domains in particle integrity and assembly, but few in vivo studies have been conducted. Moreover, fewer studies that relate the various structural domains to other possible functions of viral capsids have been reported.

  • identification of specific cucumber necrosis virus coat protein amino acids affecting Fungus Transmission and zoospore attachment
    Journal of Virology, 2001
    Co-Authors: Kishore Kakani, Jeanyves Sgro, D'ann Rochon
    Abstract:

    Cucumber necrosis virus (CNV) is naturally transmitted in the soil by zoospores of the fungal vector Olpidium bornovanus. Successful Transmission requires that virus particles attach to the surface of zoospores prior to zoospore encystment on host roots. Mechanically passaged CNV was screened for mutants deficient in Fungus Transmission. We found six such mutants, exhibiting Transmission efficiencies ranging from approximately 14 to 76% of that of wild-type (WT) CNV. Results of in vitro virus-zoospore binding assays show that each mutant binds to zoospores less efficiently than WT CNV (21 to 68%), suggesting that defects in Transmission for these mutants are at least partially due to inefficient zoospore binding. Analysis of the structure of the CNV coat protein subunit and trimer indicates that affected amino acids in all of the mutants are located in the shell or protruding domain and that five of six of them are potentially exposed on the surface of the virus particle. In addition, several of the mutated sites, along with a previously identified site in a region of subunit-subunit interaction in the coat protein shell domain (M. A. Robbins, R. D. Reade, and D. M. Rochon, Virology 234:138–146, 1997), are located on the particle quasi-threefold axis, suggesting that this region of the capsid may be important in recognition of a putative zoospore receptor. The individual sites may directly affect attachment to a receptor or could indirectly affect attachment via changes in virion conformation.

  • involvement of the cucumber necrosis virus coat protein in the specificity of Fungus Transmission by olpidium bornovanus
    Virology, 1994
    Co-Authors: Morven A Mclean, R N Campbell, Richard I Hamilton, D'ann Rochon
    Abstract:

    Abstract Cucumber necrosis (CNV) and the cherry strain of tomato bushy stunt (TBSV-Ch) are tombusviruses which differ in transmissibility by the Fungus Olpidium bornovanus (Sahtiyanci) Karling (= O. radicale Schwartz and Cook). Zoospores acquire and transmit CNV, but not TBSV-Ch, in the in vitro manner. To assess the robe of the coat protein in the specificity of Fungus Transmission, reciprocal exchanges were made between the coat protein genes of these two viruses in full-length infectious cDNA crones. Virions containing a modified TBSV-Ch genome with the CNV coat protein gene were efficiently transmitted, but those containing a modified CNV genome with the TBSV-Ch coat protein gene were not. This is the first direct demonstration for the role of a viral coat protein in the specificity of Transmission by a Fungus.

M J Adams - One of the best experts on this subject based on the ideXlab platform.

  • the complete nucleotide sequence of rna 2 of a fungally transmitted uk isolate of barley mild mosaic bymovirus and identification of amino acid combinations possibly involved in Fungus Transmission
    Virus Research, 1996
    Co-Authors: Ellen Peerenboom, Volker Jacobi, J F Antoniw, Ursula Schlichter, Ewen J Cartwright, Hanshenning Steinbiss, M J Adams
    Abstract:

    Abstract The complete nucleotide sequence of RNA-2 of a fungally-transmitted UK isolate of barley mild mosaic bymovirus (BaMMV isolate UK-F) was determined and compared with other published sequences, particularly UK-M, an isolate derived from the same source but which has been mechanically passaged for several years, has a deletion of about 1 kb and cannot be fungally transmitted. From an alignment of the BaMMV RNA-2 encoded protein with that for barley yellow mosaic bymovirus (BaYMV), several regions of consistent homology were identified and extensive searches made for similarities with the proteins of other fungally-transmitted viruses, especially amongst the furovirus capsid readthrough proteins which seem especially prone to deletion and which have already been implicated in Fungus Transmission. The amino acid combinations ER (glutamic acid-arginine) or QR (glutamine-arginine) were found consistently in all of the viruses. They occurred in positions predicted to be on the outside of the protein, and therefore available for interaction with the Fungus vector, and were also within the regions prone to spontaneous deletion. In view of the lack of other structural or sequence homologies, it is suggested that these motifs are strong candidates for involvement in Fungus Transmission.

  • cloning and sequence analysis of rna 2 of a mechanically transmitted uk isolate of barley mild mosaic bymovirus bammv
    Virus Research, 1995
    Co-Authors: Volker Jacobi, Ellen Peerenboom, J F Antoniw, Hanshenning Steinbiss, Peer M Schenk, M J Adams
    Abstract:

    A mutant of the 'Streatley' isolate of barley mild mosaic bymovirus was selected from the original field isolate by repeated mechanical incoulation. Unlike the wild-type barley mild mosaic virus, which is transmitted by the soilborne Fungus Polymyxa graminis, the mutant could not be transmitted by this vector. RNA-2 of the mutant virus was shorter than that of the wild-type virus suggesting that a deletion of part of the genome segment had occurred. The nucleotide sequence of the mutant RNA-2 was determined and revealed a high degree of homology with the RNA-2 of a German BaMMV field isolate. The deletion comprises 1092 nucleotides and is located in the 3′-terminal part of the coding region. The 34-kDa truncated form of the C-terminal protein is less than half the size of the corresponding protein of full-length BaMMV RNA-2. Taken together, the sequence data and results of biological experiments suggest an essential role of the C-terminal protein for Fungus Transmission of BaMMV.

Ellen Peerenboom - One of the best experts on this subject based on the ideXlab platform.

  • Complete RNA1 sequences of two UK isolates of barley mild mosaic virus: a wild-type Fungus-transmissible isolate and a non-Fungus-transmissible derivative
    Virus Research, 1997
    Co-Authors: Ellen Peerenboom, Ewen J Cartwright, Hanshenning Steinbiss, Ian J. Foulds, Michael J. Adams, Rebecca Stratford, Arie Rosner, John F. Antoniw
    Abstract:

    Abstract The complete RNA1 sequences of two isolates (Fungus transmissible and non-Fungus transmissible) of barley mild mosaic virus (BaMMV) were obtained. The two isolates' RNA1 sequences had very high sequence identity (99.3%), and of the 15 amino acid differences (out of 2258) between the putative polyproteins, 11 were conservative and unlikely to affect the structure or function of the protein. The remaining amino acid differences were thought unlikely to affect Fungus Transmission because they occur in the CI- and NIb-coding regions. This strongly suggests that the P73 protein of RNA2 (which has a 364-aa deletion in the non-Fungus-transmissible isolate) is involved in Fungus Transmission of BaMMV.

  • the complete nucleotide sequence of rna 2 of a fungally transmitted uk isolate of barley mild mosaic bymovirus and identification of amino acid combinations possibly involved in Fungus Transmission
    Virus Research, 1996
    Co-Authors: Ellen Peerenboom, Volker Jacobi, J F Antoniw, Ursula Schlichter, Ewen J Cartwright, Hanshenning Steinbiss, M J Adams
    Abstract:

    Abstract The complete nucleotide sequence of RNA-2 of a fungally-transmitted UK isolate of barley mild mosaic bymovirus (BaMMV isolate UK-F) was determined and compared with other published sequences, particularly UK-M, an isolate derived from the same source but which has been mechanically passaged for several years, has a deletion of about 1 kb and cannot be fungally transmitted. From an alignment of the BaMMV RNA-2 encoded protein with that for barley yellow mosaic bymovirus (BaYMV), several regions of consistent homology were identified and extensive searches made for similarities with the proteins of other fungally-transmitted viruses, especially amongst the furovirus capsid readthrough proteins which seem especially prone to deletion and which have already been implicated in Fungus Transmission. The amino acid combinations ER (glutamic acid-arginine) or QR (glutamine-arginine) were found consistently in all of the viruses. They occurred in positions predicted to be on the outside of the protein, and therefore available for interaction with the Fungus vector, and were also within the regions prone to spontaneous deletion. In view of the lack of other structural or sequence homologies, it is suggested that these motifs are strong candidates for involvement in Fungus Transmission.

  • cloning and sequence analysis of rna 2 of a mechanically transmitted uk isolate of barley mild mosaic bymovirus bammv
    Virus Research, 1995
    Co-Authors: Volker Jacobi, Ellen Peerenboom, J F Antoniw, Hanshenning Steinbiss, Peer M Schenk, M J Adams
    Abstract:

    A mutant of the 'Streatley' isolate of barley mild mosaic bymovirus was selected from the original field isolate by repeated mechanical incoulation. Unlike the wild-type barley mild mosaic virus, which is transmitted by the soilborne Fungus Polymyxa graminis, the mutant could not be transmitted by this vector. RNA-2 of the mutant virus was shorter than that of the wild-type virus suggesting that a deletion of part of the genome segment had occurred. The nucleotide sequence of the mutant RNA-2 was determined and revealed a high degree of homology with the RNA-2 of a German BaMMV field isolate. The deletion comprises 1092 nucleotides and is located in the 3′-terminal part of the coding region. The 34-kDa truncated form of the C-terminal protein is less than half the size of the corresponding protein of full-length BaMMV RNA-2. Taken together, the sequence data and results of biological experiments suggest an essential role of the C-terminal protein for Fungus Transmission of BaMMV.

Volker Jacobi - One of the best experts on this subject based on the ideXlab platform.

  • the complete nucleotide sequence of rna 2 of a fungally transmitted uk isolate of barley mild mosaic bymovirus and identification of amino acid combinations possibly involved in Fungus Transmission
    Virus Research, 1996
    Co-Authors: Ellen Peerenboom, Volker Jacobi, J F Antoniw, Ursula Schlichter, Ewen J Cartwright, Hanshenning Steinbiss, M J Adams
    Abstract:

    Abstract The complete nucleotide sequence of RNA-2 of a fungally-transmitted UK isolate of barley mild mosaic bymovirus (BaMMV isolate UK-F) was determined and compared with other published sequences, particularly UK-M, an isolate derived from the same source but which has been mechanically passaged for several years, has a deletion of about 1 kb and cannot be fungally transmitted. From an alignment of the BaMMV RNA-2 encoded protein with that for barley yellow mosaic bymovirus (BaYMV), several regions of consistent homology were identified and extensive searches made for similarities with the proteins of other fungally-transmitted viruses, especially amongst the furovirus capsid readthrough proteins which seem especially prone to deletion and which have already been implicated in Fungus Transmission. The amino acid combinations ER (glutamic acid-arginine) or QR (glutamine-arginine) were found consistently in all of the viruses. They occurred in positions predicted to be on the outside of the protein, and therefore available for interaction with the Fungus vector, and were also within the regions prone to spontaneous deletion. In view of the lack of other structural or sequence homologies, it is suggested that these motifs are strong candidates for involvement in Fungus Transmission.

  • cloning and sequence analysis of rna 2 of a mechanically transmitted uk isolate of barley mild mosaic bymovirus bammv
    Virus Research, 1995
    Co-Authors: Volker Jacobi, Ellen Peerenboom, J F Antoniw, Hanshenning Steinbiss, Peer M Schenk, M J Adams
    Abstract:

    A mutant of the 'Streatley' isolate of barley mild mosaic bymovirus was selected from the original field isolate by repeated mechanical incoulation. Unlike the wild-type barley mild mosaic virus, which is transmitted by the soilborne Fungus Polymyxa graminis, the mutant could not be transmitted by this vector. RNA-2 of the mutant virus was shorter than that of the wild-type virus suggesting that a deletion of part of the genome segment had occurred. The nucleotide sequence of the mutant RNA-2 was determined and revealed a high degree of homology with the RNA-2 of a German BaMMV field isolate. The deletion comprises 1092 nucleotides and is located in the 3′-terminal part of the coding region. The 34-kDa truncated form of the C-terminal protein is less than half the size of the corresponding protein of full-length BaMMV RNA-2. Taken together, the sequence data and results of biological experiments suggest an essential role of the C-terminal protein for Fungus Transmission of BaMMV.

Hanshenning Steinbiss - One of the best experts on this subject based on the ideXlab platform.

  • Complete RNA1 sequences of two UK isolates of barley mild mosaic virus: a wild-type Fungus-transmissible isolate and a non-Fungus-transmissible derivative
    Virus Research, 1997
    Co-Authors: Ellen Peerenboom, Ewen J Cartwright, Hanshenning Steinbiss, Ian J. Foulds, Michael J. Adams, Rebecca Stratford, Arie Rosner, John F. Antoniw
    Abstract:

    Abstract The complete RNA1 sequences of two isolates (Fungus transmissible and non-Fungus transmissible) of barley mild mosaic virus (BaMMV) were obtained. The two isolates' RNA1 sequences had very high sequence identity (99.3%), and of the 15 amino acid differences (out of 2258) between the putative polyproteins, 11 were conservative and unlikely to affect the structure or function of the protein. The remaining amino acid differences were thought unlikely to affect Fungus Transmission because they occur in the CI- and NIb-coding regions. This strongly suggests that the P73 protein of RNA2 (which has a 364-aa deletion in the non-Fungus-transmissible isolate) is involved in Fungus Transmission of BaMMV.

  • the complete nucleotide sequence of rna 2 of a fungally transmitted uk isolate of barley mild mosaic bymovirus and identification of amino acid combinations possibly involved in Fungus Transmission
    Virus Research, 1996
    Co-Authors: Ellen Peerenboom, Volker Jacobi, J F Antoniw, Ursula Schlichter, Ewen J Cartwright, Hanshenning Steinbiss, M J Adams
    Abstract:

    Abstract The complete nucleotide sequence of RNA-2 of a fungally-transmitted UK isolate of barley mild mosaic bymovirus (BaMMV isolate UK-F) was determined and compared with other published sequences, particularly UK-M, an isolate derived from the same source but which has been mechanically passaged for several years, has a deletion of about 1 kb and cannot be fungally transmitted. From an alignment of the BaMMV RNA-2 encoded protein with that for barley yellow mosaic bymovirus (BaYMV), several regions of consistent homology were identified and extensive searches made for similarities with the proteins of other fungally-transmitted viruses, especially amongst the furovirus capsid readthrough proteins which seem especially prone to deletion and which have already been implicated in Fungus Transmission. The amino acid combinations ER (glutamic acid-arginine) or QR (glutamine-arginine) were found consistently in all of the viruses. They occurred in positions predicted to be on the outside of the protein, and therefore available for interaction with the Fungus vector, and were also within the regions prone to spontaneous deletion. In view of the lack of other structural or sequence homologies, it is suggested that these motifs are strong candidates for involvement in Fungus Transmission.

  • cloning and sequence analysis of rna 2 of a mechanically transmitted uk isolate of barley mild mosaic bymovirus bammv
    Virus Research, 1995
    Co-Authors: Volker Jacobi, Ellen Peerenboom, J F Antoniw, Hanshenning Steinbiss, Peer M Schenk, M J Adams
    Abstract:

    A mutant of the 'Streatley' isolate of barley mild mosaic bymovirus was selected from the original field isolate by repeated mechanical incoulation. Unlike the wild-type barley mild mosaic virus, which is transmitted by the soilborne Fungus Polymyxa graminis, the mutant could not be transmitted by this vector. RNA-2 of the mutant virus was shorter than that of the wild-type virus suggesting that a deletion of part of the genome segment had occurred. The nucleotide sequence of the mutant RNA-2 was determined and revealed a high degree of homology with the RNA-2 of a German BaMMV field isolate. The deletion comprises 1092 nucleotides and is located in the 3′-terminal part of the coding region. The 34-kDa truncated form of the C-terminal protein is less than half the size of the corresponding protein of full-length BaMMV RNA-2. Taken together, the sequence data and results of biological experiments suggest an essential role of the C-terminal protein for Fungus Transmission of BaMMV.