scholarly journals Biological Behavior and Partial Molecular Characterization of Six Chilean Isolates of Plum pox virus

Plant Disease ◽  
2003 ◽  
Vol 87 (1) ◽  
pp. 15-20 ◽  
Author(s):  
F. Reyes ◽  
N. Fiore ◽  
M. A. Reyes ◽  
P. Sepúlveda ◽  
V. Paredes ◽  
...  
Keyword(s):  
Coat Protein ◽  
Central Zone ◽  
Fruit Production ◽  
Amino Acid Sequences ◽  
Biological Behavior ◽  
Plum Pox Virus ◽  
Replicase Gene ◽  
Protein Amino Acid ◽  
Nontranslated Region

Plum pox virus (PPV) strain D was first detected in Chile in 1992 infecting Prunus trees including peaches, nectarines, apricots, and plums. Since then, quarantine efforts have included periodic surveys in the central zone of the country, the main region for stone fruit production. This work describes the characterization of six PPV isolates from this area of Chile, using biological and molecular approaches. PPV isolates were introduced into Prunus tomentosa and Nicotiana benthamiana hosts by grafting and mechanical inoculation, respectively. Symptoms were evaluated by following the appearance of circular necrotic spots and mosaic in leaves of P. tomentosa and mosaic and some leaf deformation in N. benthamiana. Molecular analysis was carried out using reverse transcription-polymerase chain reaction, allowing the cloning and sequencing of 1.34-kb fragments corresponding to the 3' region of the replicase gene, the complete coat protein (CP) gene, and the 3' nontranslated region of the PPV genome. Evolutionary distance analysis of these nucleotide sequences and their deduced coat protein amino acid sequences grouped the six Chilean isolates among strain D isolates, with closest genetic distances to those of Central Germany and Poland. Representative sources of these isolates suggest that strain D could be the only type of PPV currently present in Chile.

Serological Characterization of Hungarian Plum Pox Virus Isolates

1997 ◽  
Vol 52 (5-6) ◽  
pp. 391-395
Author(s):  
Juan José López-Moya ◽  
Dionisio López-Abella ◽  
José-Ramón Díaz-Rúiz ◽  
Belén Martinez-Garcia ◽  
Richard Gáborjányi
Keyword(s):  
Monoclonal Antibodies ◽  
Coat Protein ◽  
Blot Analysis ◽  
Plum Pox Virus ◽  
Rt Pcr ◽  
Dot Blot ◽  
Serological Characterization ◽  
Spanish Isolate ◽  
Virus Isolates

Abstract Three Hungarian (No.2, 4 and 9), and a Moldavian (K) plum pox virus isolates were compared with a characterized Spanish isolate (5.15) by RT-PCR, ELISA, dot-blot and West­ern blot analysis. Monoclonal antibodies prepared against the external, intermediate and internal sequences of the coat protein of the Spanish isolate were able to differentiate the four isolates. Hungarian isolate No. 2 proved to be serologically identical to the Spanish isolate, while No. 4 showed appreciable differences and No. 9 could be recognized only by the monoclonal antibodies representing the intermedial and internal parts of the coat protein. K isolate showed a more distant relationship to other isolates. Our experiment provided the first demonstration of the presence of D type isolates in Hungary.

scholarly journals Detection and partial molecular characterization of Grapevine fleck virus, Grapevine virus D, Grapevine leafroll-associated virus -5 and -6 infecting grapevines in Brazil

2012 ◽  
Vol 42 (12) ◽  
pp. 2127-2130 ◽  
Author(s):  
Thor Vinícius Martins Fajardo ◽  
Marcelo Eiras ◽  
Osmar Nickel ◽  
Carla Rosa Dubiela ◽  
Eliezer Rodrigues de Souto
Keyword(s):  
Coat Protein ◽  
Molecular Characterization ◽  
Rna Binding ◽  
Rna Binding Protein ◽  
Amino Acid Sequences ◽  
Viral Diseases ◽  
Grapevine Virus ◽  
Available Information ◽  
First Time

Grapevine fleck, rugose wood and leafroll are three grapevine viral diseases whose causal agents (or associated viruses) respectively are Grapevine fleck virus (GFkV), Grapevine virus D (GVD) and Grapevine leafroll-associated virus 5 and 6 (GLRaV-5 and -6). The objective of this work was to perform a partial molecular characterization of local isolates of these four viral species that infect grapevines. The nucleotide and deduced amino acid sequences of complete genes of the coat protein (CP) (of GFkV), the CP and the RNA binding protein (of GVD), the CP and the partial hHSP70 gene (of GLRaV-5) and the partial hHSP70 gene (of GLRaV-6) were aligned and compared in silico with other isolates. These data extend the available information about Brazilian isolates of GFkV, GLRaV-5 and -6, and reports for the first time the GVD occurrence in Brazil.

scholarly journals Characterization of a New Potyvirus Naturally Infecting Chickpea

Plant Disease ◽  
2003 ◽  
Vol 87 (11) ◽  
pp. 1366-1371 ◽  
Author(s):  
Richard C. Larsen ◽  
Walter J. Kaiser ◽  
Stephen D. Wyatt ◽  
Keri L. Buxton-Druffel ◽  
Phillip H. Berger
Keyword(s):  
Coat Protein ◽  
Mosaic Virus ◽  
Yellow Mosaic Virus ◽  
Plum Pox Virus ◽  
Cdna Clones ◽  
Coat Proteins ◽  
Serological Reaction ◽  
Protein Amino Acid ◽  
Western Blots ◽  
Putative Coat Protein

During the 1999 to 2001 growing seasons, symptoms consisting of mosaic, stunting, yellowing, wilting, shortening of internodes, and phloem discoloration were observed in chickpea (Cicer arietinum) grown in the Department of Chuquisaca in southern Bolivia. In some fields, approximately 10% of the plants exhibited viruslike symptoms and suffered greatly reduced seed yields. Lentil (Lens culinaris) was also observed to be infected but not pea (Pisum sativum) or faba bean (Vicia faba) growing in nearby fields. Infected chickpea tissue reacted positively to the potyvirus group-specific monoclonal antibody (MAb), but there was no serological reaction with antisera to the potyviruses Bean yellow mosaic virus, Clover yellow vein virus, Cowpea aphid-borne mosaic virus, Pea seedborne mosaic virus, Bean common mosaic virus, or Bean common mosaic necrosis virus. Western blots of total protein extracts probed with the potyvirus MAb revealed a single band ca. 32 kDa. Comparative sequence analysis of cDNA clones generated from the putative coat protein gene consisted of 282 amino acids (31.9 kDa) and showed moderate identities of 67, 66, 63, 63, and 61% with the coat proteins of potyviruses Pepper severe mosaic virus, Pepper yellow mosaic virus, Potato virus Y, Plum pox virus, and Pepper mottle virus, respectively. Phylogenetic analysis of the coat protein amino acid sequence revealed that this virus is a unique member of the family Potyviridae and is phylogenetically most closely related to a group of Solanaceae-infecting potyviruses rather than to other legumeinfecting potyviruses. The proposed name for the new causal agent is Chickpea yellow mosaic virus.

CHARACTERIZATION OF PLUM POX VIRUS COAT PROTEIN EPITOPES USING FUSION PROTEINS EXPRESSED IN E. COLI

1998 ◽  
pp. 461-468 ◽  
Author(s):  
T. Candresse ◽  
F. Rafia ◽  
J. Dunez ◽  
M. Navratil ◽  
D. Boscia ◽  
...  
Keyword(s):  
Coat Protein ◽  
Fusion Proteins ◽  
Plum Pox Virus ◽  
E Coli ◽  
Virus Coat Protein ◽  
Virus Coat

scholarly journals Identification and Genetic Characterization of a Novel Respirovirus in Alpine Chamois (Rupicapra rupicapra rupicapra)

Animals ◽  
2020 ◽  
Vol 10 (4) ◽  
pp. 704
Author(s):  
Camilla Luzzago ◽  
Erika Ebranati ◽  
Antonio Lavazza ◽  
Martina Besozzi ◽  
Gianguglielmo Zehender ◽  
...  
Keyword(s):  
Genetic Characterization ◽  
Phylogenetic Analyses ◽  
Amino Acid Sequences ◽  
Species Demarcation Criterion ◽  
Demarcation Criterion ◽  
Protein Amino Acid ◽  
Rupicapra Rupicapra ◽  
Separate Branch ◽  
Alpine Chamois

The Respirovirus genus, family Paramamixoviridae, includes respiratory viral pathogens. Here we report the identification and genetic characterization of a respirovirus in an Alpine chamois showing interstitial pneumonia associated with catarrhal bronchopneumonia. The full-genome characterization of this respirovirus, named ChamoisRV/IT2014, revealed low similarities to caprine respirovirus (77.1%), bovine respirovirus (74.5%) and human respirovirus (72.0%). The phylogenetic analyses based on the full-length genome sequence of the novel isolate and reference respirovirus strains showed that ChamoisRV/IT2014 clustered with caprine respirovirus but formed a separate branch. The phylogenetic tree topology of complete large protein amino acid sequences, representing the current species demarcation criterion for Respirovirus genus, showed a 0.05 branch length of ChamoisRV/IT2014 sequence between the nearest node and the tip of the branch, suggesting that this virus belongs to a novel species. This new isolate in a new host species raises several questions to be addressed on the epidemiological role of chamois and the risks of cross-transmission between wild ruminants and livestock.

scholarly journals Identification of Variants of the High Plains virus Infecting Wheat in Kansas

Plant Disease ◽  
2009 ◽  
Vol 93 (12) ◽  
pp. 1265-1274 ◽  
Author(s):  
Dallas L. Seifers ◽  
T. J. Martin ◽  
Tom L. Harvey ◽  
S. Haber ◽  
O. Krokhin ◽  
...  
Keyword(s):  
Amino Acid ◽  
Coat Protein ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Amino Acid Sequences ◽  
Enzyme Linked Immunosorbent Assay ◽  
High Plains ◽  
Protein Amino Acid ◽  
Sds Page ◽  
Virus Isolates

The properties of two virus isolates (U04-82 and U04-83) obtained from two wheat (Triticum aestivum) plants expressing mosaic symptoms were investigated using enzyme-linked immunosorbent assay (ELISA), sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), time-of-flight mass spectrometry (TOFMS), and infection of wheat with resistance to Wheat streak mosaic virus (WSMV). The coat protein mass was estimated by SDS-PAGE as approximately 32 kDa for U04-82 and 30 kDa for U04-83. The amino acid sequence of the coat protein of U04-82 was 99.6 and 85.5% identical to two isolates, ABC58222 and TX96, respectively, of High Plains virus (HPV) described from Texas. U04-82 was transmitted by wheat curl mites and caused significant yield reductions in wheat resistant to WSMV. U04-83 was actually two distinct virus isolates whose capsid protein amino acid sequences were only 57 and 50% similar to that of TX96. Antiserum prepared to a synthetic peptide from the sequence of the U04-83 isolate recognized the two U04-83 isolates, but not the U04-82 isolate.

Characterization of a natural Plum pox virus isolate bearing a truncated coat protein

2008 ◽  
Vol 154 (1) ◽  
pp. 141-145 ◽  
Author(s):  
Erzsébet Szathmáry ◽  
Júlia Novák Nádudvari ◽  
László Szabó ◽  
István Tóbiás ◽  
Ervin Balázs ◽  
...  
Keyword(s):  
Coat Protein ◽  
Virus Isolate ◽  
Plum Pox Virus

Characterization of a cDNA for Rhesus Monkey Protein C Inhibitor – Evidence for N-Terminal Involvement in Heparin Stimulation

1995 ◽  
Vol 74 (04) ◽  
pp. 1079-1087 ◽  
Author(s):  
Klaus-P Radtke ◽  
José A Fernández ◽  
Bruno O Villoutreix ◽  
Judith S Greengard ◽  
John H Griffin
Keyword(s):  
Rhesus Monkey ◽  
Protein C ◽  
Activated Protein C ◽  
Pcr Amplification ◽  
Amino Acid Sequences ◽  
Heparin Binding ◽  
Reactive Center ◽  
Protein C Inhibitor ◽  
Polymerase Chain

SummarycDNAs for protein C inhibitor (PCI) were cloned from human and rhesus monkey 1 liver RNAs by reverse transcription and polymerase chain reaction (PCR) amplification. Sequencing showed that rhesus monkey and human PCI cDNAs were 93% identical. Predicted amino acid sequences differed at 26 of 387 residues. Pour of these differences (T352M, N359S, R362K, L3631) were in the reactive center loop that is important for inhibitory specificity, and two were in the N-terminal helix (M8T, E13K) that is implicated in glycosaminoglycan binding. PCI in human or rhesus monkey plasma showed comparable inhibitory activity towards human activated protein C in the presence of 10 U/ml heparin. However, maximal acceleration of the inhibition of activated protein C required 5-fold lower heparin concentration for rhesus monkey than for human plasma, consistent with the interpretation that the additional positive charge (E13K) in a putative-heparin binding region increased the affinity for heparin.

Characterization of Glycoprotein Fraction from Carp Pituitaries Isolated Using Concanavalin A as the Affinity Ligand

1998 ◽  
Vol 63 (3) ◽  
pp. 434-440 ◽  
Author(s):  
Irena Hulová ◽  
Jana Barthová ◽  
Helena Ryšlavá ◽  
Václav Kašička
Keyword(s):  
Concanavalin A ◽  
Reversed Phase ◽  
Amino Acid Sequences ◽  
Gel Chromatography ◽  
Affinity Ligand ◽  
Sds Page ◽  
Terminal Amino ◽  
Α And Β Subunits

Glycoproteins that have affinity to Concanavalin A were isolated from the acetone-dried pituitaries of common carp (Cyprinus carpio L.). Two fractions of glycoproteins were separated using gel chromatography on Superdex 75HR. The fraction with lower molecular weight (30 000) corresponding to the carp gonadotropin cGtH II was composed of two subunits as determined using SDS-PAGE. This protein fraction was further divided into four components using reversed-phase HPLC. Two fractions were pure α and β subunits of cGtH II as follows from immunodetection and from determination of N-terminal amino acid sequences. The other two were a mixture of α and β subunits as was also revealed by N-terminal analysis. Capillary electrophoresis was also used for characterization of isolated glycoproteins.

Sign in / Sign up

Export Citation Format

Share Document