scholarly journals Expression of the Peanut stunt virus Coat Protein Gene Is Essential and Sufficient for Production of Host-Dependent Ribbon-Like Inclusions in Infected Plants

2004 ◽  
Vol 94 (7) ◽  
pp. 722-729 ◽  
Author(s):  
N. S. Bashir ◽  
M. Sanger ◽  
U. Järlfors ◽  
S. A. Ghabrial
Keyword(s):  
Coat Protein ◽  
Leaf Tissue ◽  
Potato Virus X ◽  
Open Reading Frames ◽  
Subgroup Ii ◽  
Enzymelinked Immunosorbent Assay ◽  
Polymerase Chain ◽  
Peanut Stunt Virus ◽  
Virus Coat ◽  
Reading Frames

We previously have reported that infection of tobacco protoplasts or leaf tissue with the cucumovirus Peanut stunt virus (PSV) induced the production of unusual cytoplasmic ribbon-like inclusions. The formation of these novel inclusions is strain-specific, because infection of tobacco with subgroup II PSV strains, but not subgroup I strains, induced the production of inclusions. Furthermore, we have demonstrated that induction of the ribbon-like inclusions maps to PSV subgroup II RNA3, which codes for the coat protein (CP) and movement protein (MP). We have now extended these studies using chimeric constructs containing CP and MP open reading frames (ORFs) from PSV strains ER and W that belong to subgroups I and II, respectively. Additionally, recombinant Potato virus X (PVX) vectors containing translatable and untranslatable PSV CP ORF were constructed. Plants inoculated with infectious chimeric PSV or recombinant PVX transcripts were analyzed for CP expression by enzymelinked immunosorbent assay and reverse transcription-polymerase chain reaction and for inclusion production by electron microscopy. The results of these experiments indicated that translation of the CP ORF alone is essential and sufficient for inclusion production. In immunogold labeling experiments using an antiserum to PSV virions, abundant gold labeling of the inclusions was observed, suggesting that PSV CP is probably a major component of the inclusions. Because inclusion production is host specific, a host factor is likely to be involved. In addition to their diagnostic importance, these novel inclusions may also prove valuable in identifying the host factors that interact with PSV CP.

RNA3 nucleotide sequence analyses ofpeanut stunt virusMi strain

2005 ◽  
Vol 2 (1) ◽  
pp. 33-38
Author(s):  
Xu Ze-Yong ◽  
Yan Li-Ying ◽  
Chen Kun-Rong ◽  
Marcel Prins
Keyword(s):  
Nucleotide Sequence ◽  
Movement Protein ◽  
Amino Acid Identity ◽  
Open Reading Frames ◽  
Sequence Analyses ◽  
Tomato Aspermy Virus ◽  
Subgroup Ii ◽  
Putative Movement Protein ◽  
Peanut Stunt Virus ◽  
Reading Frames

AbstractNucleotide sequence of full-length cDNA ofpeanut stunt virus(PSV) Mi strain RNA3 was determined and compared with those of PSV-ER and -J (subgroup I) and PSV-W (subgroup II), strains ofcucumber mosaic virus(CMV) andtomato aspermy virus(TAV). PSV-Mi RNA3 consists of 2170 nt and has two open reading frames, encoding a putative movement protein (3a protein) and a coat protein (CP). PSV-Mi RNA3 is 77.7% and 78.5% identical to those of PSV-ER and -J, whereas it shares 76.6% identity with PSV-W. Nucleotide identity of3aandcpgenes between PSV strains Mi and ER, J and W was 78.3–79.3% and 74.4–77.8%, respectively. Amino acid identity of 3a and CP between PSV-Mi and -ER, -J and -W was 73.9–77.4% and 64.8–77.5%, respectively. RNA3 of PSV-Mi (GenBank accession no. AY775057) had a varied intercistronic and 5′-untranslated region compared with those of PSV strains ER, J and W. Results indicate that PSV-Mi represents a new PSV subgroup from China, designated as subgroup III.

scholarly journals Nucleotide sequence of the open reading frames adjacent to the coat protein cistron in potato virus X genome

FEBS Letters ◽  
1987 ◽  
Vol 213 (2) ◽  
pp. 438-442 ◽  
Author(s):  
S.Yu. Morozov ◽  
L.I. Lukasheva ◽  
B.K. Chernov ◽  
K.G. Skryabin ◽  
J.G. Atabekov
Keyword(s):  
Nucleotide Sequence ◽  
Coat Protein ◽  
Potato Virus ◽  
Potato Virus X ◽  
Open Reading Frames ◽  
Reading Frames

scholarly journals Pepper Mild Mottle Virus Coat Protein Alone Can Elicit the Capsicum spp. L3 Gene-Mediated Resistance

1998 ◽  
Vol 11 (12) ◽  
pp. 1253-1257 ◽  
Author(s):  
P. Gilardi ◽  
I. García-Luque ◽  
M. T. Serra
Keyword(s):  
Coat Protein ◽  
Resistance Gene ◽  
Protein Gene ◽  
Expression System ◽  
Potato Virus X ◽  
Mottle Virus ◽  
Capsicum Chinense ◽  
Pepper Mild Mottle Virus ◽  
Capsicum Spp ◽  
Virus Coat

The pepper mild mottle virus (PMMoV-S) (an L3 hypersensitive response [HR]-inducer strain) coat protein was expressed in Capsicum chinense (L3L3) plants with the heterologous potato virus X (PVX)-based expression system. The chimeric virus was localized in the inoculated leaves and induced the HR, thus indicating that the tobamoviral sequences that affect induction of the HR conferred by the L3 resistance gene reside in the coat protein gene. Furthermore, transient expression of the PMMoV-S coat protein in C. chinense leaves by biolistic co-bombardment with a plasmid expressing the β-glucuronidase (GUS) gene leads to the induction of cell death and expression of host defense genes. Thus, the coat protein of PMMoV-S is the elicitor of the Capsicum spp. L3 resistance gene-mediated HR.

Inactivation of the Streptococcus mutans fxpC Gene Confers Resistance to Xylitol, a Caries-preventive Natural Carbohydrate Sweetener

2002 ◽  
Vol 81 (6) ◽  
pp. 380-386 ◽  
Author(s):  
H. Benchabane ◽  
L.-A. Lortie ◽  
N.D. Buckley ◽  
L. Trahan ◽  
M. Frenette
Keyword(s):  
Streptococcus Mutans ◽  
Northern Blot Analysis ◽  
Regulatory Protein ◽  
Open Reading Frames ◽  
Phosphotransferase System ◽  
Chain Reactions ◽  
Polymerase Chain Reactions ◽  
Resistant Strains ◽  
Polymerase Chain ◽  
Reading Frames

Xylitol is transported by Streptococcus mutans via a constitutive phosphoenolpyruvate:fructose phosphotransferase system (PTS) composed of a IIABC protein. Spontaneous xylitol-resistant strains are depleted in constitutive fructose-PTS activity, exhibit additional phenotypes, and are associated with the caries-preventive properties of xylitol. Polymerase chain-reactions and chromosome walking were used to clone the fxp operon that codes for the constitutive fructose/xylitol-PTS. The operon contained three open reading frames: fxpA, which coded for a putative regulatory protein of the deoxyribose repressor (DeoR) family, fxpB, which coded for a 1-phosphofructokinase, and fxpC, which coded for a IIABC protein of the fructose-PTS family. Northern blot analysis revealed that these genes were co-transcribed into a 4.4-kb mRNA even in the absence of fructose. Inactivation of the fxpC gene conferred resistance to xylitol, confirming its function. The fxp operon is also present in the genomes of other xylitol-sensitive streptococci, which could explain their sensitivity to xylitol.

scholarly journals Cloning of two Bombyx homologues of the Drosophila rosy gene and their relationship to larval translucent skin colour mutants

1998 ◽  
Vol 71 (1) ◽  
pp. 11-19 ◽  
Author(s):  
YUJI YASUKOCHI ◽  
TOSHIO KANDA ◽  
TOSHIKI TAMURA
Keyword(s):  
Tissue Specificity ◽  
Amino Acid Sequences ◽  
Open Reading Frames ◽  
Striking Similarity ◽  
Wild Type ◽  
Rt Pcr ◽  
Significant Difference ◽  
Phage Dna ◽  
Polymerase Chain ◽  
Reading Frames

To clone the Bombyx xanthine dehydrogenase (XDH) gene as a dominant marker for silkworm transgenesis, we performed nested reverse transcriptase–polymerase chain reaction (RT-PCR) using embryonic mRNA and primers designed from the conserved region of Drosophila and rat XDH genes. Sequencing of amplified 180 bp fragments showed that two different sequences were present in the fragments. Since both possessed striking similarity to XDH genes of other organisms, we considered these to be portions of silkworm XDH genes and designated them BmXDH1 and BmXDH2. Subsequently we cloned separately the entire region of the two cDNAs by PCR using phage DNA of an embryonic cDNA library and sequenced them. The two cDNAs were around 4 kb in size and possessed complete open reading frames. The deduced amino acid sequences of the two BmXDHs were very similar to each other and to those of other organisms. The expression pattern of wild-type larvae basically followed the tissue specificity of the enzyme and no significant difference was observed between the two XDH genes. The expression of both genes was detected in the XDH-deficient mutants, oq and og, but non-synonymous substitutions were specifically detected in the BmXDH1 of the oq mutant. In addition, a length polymorphism of the second intron of the BmXDH1 co-segregated with the oq translucent phenotype, suggesting that deficiency in BmXDH1 is the cause of the oq translucent phenotype.

scholarly journals Complete Genome Sequence of a Novel Satellite Virus Associated with Cassava Plants

2017 ◽  
Vol 5 (16) ◽  
Author(s):  
Adriana N. Souza ◽  
Fábio N. Silva ◽  
Claudine M. Carvalho
Keyword(s):  
Amino Acids ◽  
Coat Protein ◽  
Genome Sequence ◽  
Complete Genome Sequence ◽  
Complete Genome ◽  
Open Reading Frames ◽  
Putative Protein ◽  
Satellite Virus ◽  
Cassava Plant ◽  
Reading Frames

ABSTRACT A novel satellite virus of 1,228 bp in length was found in a single cassava plant. Bioinformatic analyses show that it has two open reading frames (ORFs) in its genome, probably encoding a coat protein of 156 and a putative protein of 90 amino acids.

scholarly journals The Previously Unidentified, Divergent Badnavirus Species Cacao red vein-banding virus is Associated with Cacao Swollen Shoot Disease in Nigeria

Plant Disease ◽  
2019 ◽  
Vol 103 (6) ◽  
pp. 1302-1308 ◽  
Author(s):  
Nomatter Chingandu ◽  
Lelia Dongo ◽  
Osman A. Gutierrez ◽  
Judith K. Brown
Keyword(s):  
Phylogenetic Analyses ◽  
Pcr Amplification ◽  
West African ◽  
Open Reading Frames ◽  
Nucleotide Identity ◽  
Genome Sequences ◽  
Foliar Symptoms ◽  
Field Samples ◽  
Polymerase Chain ◽  
Reading Frames

Cacao swollen shoot disease (CSSD) of Theobroma cacao was reported in Nigeria in 1944; however, no badnaviral genome sequences have been found associated with the symptomatic trees. In 2017, leaf samples (n = 18) were collected from cacao trees from Osun and Oyo, Nigeria showing foliar symptoms that included red vein-banding and shoot swelling, and variable secondary mosaic, mottling, and fern-like pattern symptoms. Abutting primers designed around previously determined 500-bp intergenic region sequences were used for polymerase chain reaction (PCR) amplification. Of the 18 samples, 9 yielded an approximately 7,000-bp, apparently genome-size product. The nine genomes were sequenced and found to encode four open reading frames, and to share 86 to 99% nucleotide identity. Pairwise analysis of the Nigerian genomes with 21 previously reported CSSD badnaviruses, at the complete genome and reverse-transcription ribonuclease H (1,230 bp) sequence levels, indicated 71 to 75 and 72 to 76% nucleotide identity, respectively. Phylogenetic analysis of the nine complete genomes indicated that the closest relatives of the divergent Nigerian isolates were previously described West African CSSD badnaviruses. Based on pairwise comparisons and phylogenetic analyses, the Nigerian CSSD isolates constitute a previously unrecognized Badnavirus sp., herein named Cacao red vein-banding virus (CRVBV). Primers designed based on the CRVBV genome sequences amplified a 1,068-bp fragment from 16 of 18 field samples tested by PCR, suggesting the possible existence of additional CRVBV variants.

RHD gene deletion occurred in the Rhesus box

Blood ◽  
2000 ◽  
Vol 95 (12) ◽  
pp. 3662-3668 ◽  
Author(s):  
Franz F. Wagner ◽  
Willy A. Flegel
Keyword(s):  
Open Reading Frames ◽  
Chromosome 1 ◽  
Nucleotide Sequencing ◽  
Blood Group Antigens ◽  
Specific Detection ◽  
Pcr Rflp ◽  
Polymerase Chain ◽  
Specific Priming ◽  
Rh Blood Group ◽  
Reading Frames

Abstract The Rh blood group antigens derive from 2 genes,RHD and RHCE, that are located at chromosomal position 1p34.1-1p36 (chromosome 1, short arm, region 3, band 4, subband 1, through band 6). In whites, a cde haplotype with a deletion of the whole RHD gene occurs with a frequency of approximately 40%. The relative position of the 2 RH genes and the location of the RHD deletion was previously unknown. A model has been developed for the RH locus using RHD- and RHCE-related nucleotide sequences deposited in nucleotide sequence databases along with polymerase chain reaction (PCR) and nucleotide sequencing. The open reading frames of bothRH genes had opposite orientations. The 3′ ends of the genes faced each other and were separated by about 30 000 base pair (bp) that contained the SMP1 gene. The RHD gene was flanked by 2 DNA segments, dubbed Rhesus boxes, with a length of approximately 9000 bp, 98.6% homology, and identical orientation. The Rhesus box contained the RHD deletion occurring within a stretch of 1463 bp of identity. PCR with sequence-specific priming (PCR-SSP) and PCR with restriction fragment length polymorphism (PCR-RFLP) were used for specific detection of the RHDdeletion. The molecular structure of the RH gene locus explains the mechanisms for generating RHD/RHCE hybrid alleles and the RHD deletion. Specific detection of theRHD− genotype is now possible.

Detection of potential suberinase-encoding genes in Streptomyces scabiei strains and other actinobacteria

2013 ◽  
Vol 59 (5) ◽  
pp. 294-303 ◽  
Author(s):  
Doaa Komeil ◽  
Anne-Marie Simao-Beaunoir ◽  
Carole Beaulieu
Keyword(s):  
Esterase Activity ◽  
Common Scab ◽  
Blot Hybridization ◽  
Southern Blot Hybridization ◽  
Open Reading Frames ◽  
Streptomyces Scabiei ◽  
Polymerase Chain ◽  
Encoding Genes ◽  
Reading Frames ◽  
Important Disease

Streptomyces scabiei causes common scab, an economically important disease of potato tubers. Some authors have previously suggested that S. scabiei penetration into host plant tissue is facilitated by secretion of esterase enzymes degrading suberin, a lipidic biopolymer of the potato periderm. In the present study, S. scabiei EF-35 showed high esterase activity in suberin-containing media. This strain also exhibited esterase activity in the presence of other biopolymers, such as lignin, cutin, or xylan, but at a much lower level. In an attempt to identify the esterases involved in suberin degradation, translated open reading frames of S. scabiei 87-22 were examined for the presence of protein sequences corresponding to extracellular esterases of S. scabiei FL1 and of the fungus Coprinopsis cinerea VTT D-041011, which have previously been shown to be produced in the presence of suberin. Two putative extracellular suberinase genes, estA and sub1, were identified. The presence of these genes in several actinobacteria was investigated by Southern blot hybridization, and both genes were found in most common-scab-inducing strains. Moreover, reverse transcription – polymerase chain reaction performed with S. scabiei EF-35 showed that estA was expressed in the presence of various biopolymers, including suberin, whereas the sub1 gene appeared to be specifically expressed in the presence of suberin and cutin.

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