scholarly journals Transmission by Olpidium brassicae of Mirafiori lettuce virus and Lettuce big-vein virus, and Their Roles in Lettuce Big-Vein Etiology

2002 ◽  
Vol 92 (3) ◽  
pp. 288-293 ◽  
Author(s):  
Hervé Lot ◽  
Robert N. Campbell ◽  
Sylvie Souche ◽  
Robert G. Milne ◽  
Piero Roggero

Big-vein disease occurs on lettuce worldwide in temperate conditions; the causal agent has been presumed to be Lettuce big-vein virus (LBVV), genus Varicosavirus, vectored by the soilborne fungus Olpidium brassicae. Recently, the role of LBVV in the etiology of big-vein disease has been questioned because a second soilborne virus, Mirafiori lettuce virus (MiLV), genus Ophiovirus, has been found frequently in big-vein-affected lettuce. LBVV and MiLV, detectable and distinguishable by enzyme-linked immunosorbent assay using specific antisera, were tested for their ability to be transmitted from lettuce to lettuce by mechanical inoculation of sap extracts, or by zoospores of O. brassicae, and to cause big-vein disease. Both viruses were mechanically transmissible from lettuce to herbaceous hosts and to lettuce, but very erratically. LBVV was transmitted by O. brassicae but lettuce infected with only this virus never showed symptoms. MiLV was transmitted in the same manner, and lettuce infected with this virus alone consistently developed big-vein symptoms regardless of the presence or absence of LBVV. With repeated mechanical transmission, isolates of both viruses appeared to lose the ability to be vectored, and MiLV appeared to lose the ability to cause big-vein symptoms. The recovery of MiLV (Mendocino isolate, from Cali-fornia) from stored O. brassicae resting spores puts the earliest directly demonstrable existence of MiLV at 1990.

Blood ◽  
1988 ◽  
Vol 71 (1) ◽  
pp. 220-225 ◽  
Author(s):  
PJ Declerck ◽  
MC Alessi ◽  
M Verstreken ◽  
EK Kruithof ◽  
I Juhan-Vague ◽  
...  

An enzyme-linked immunosorbent assay for plasminogen activator inhibitor-1 (PAI-1) in biologic fluids was developed on the basis of two murine monoclonal antibodies raised against PAI-1 purified from HT- 1080 fibrosarcoma cells. The lower limit of sensitivity of the assay in plasma is 2 ng/mL. The assay is 12 times less sensitive toward the PAI- 1/human tissue-type plasminogen activator (t-PA) complex as compared with free PAI-1. The intraassay, interassay, and interdilution coefficients of variation are 5.2%, 8.0%, and 7.1%, respectively. The level of PAI-1 in platelet-poor plasma of healthy subjects is 18 +/- 10 ng/mL (mean +/- SD, n = 45). In platelet-rich plasma after freezing and thawing, 92% of PAI-1 antigen is released from platelets, whereas only 8% is found in the corresponding platelet-poor plasma. In platelet-poor plasma from healthy subjects, a linear correlation (r = 0.80) was found between PAI activity and PAI-1 antigen. In plasma approximately two thirds of the PAI-1 antigen was functionally active, whereas only 5% of the PAI-1 antigen released from platelets was active. During pregnancy a progressive increase of PAI-1 antigen levels up to three- to sixfold the control value was observed. In plasma of patients with recurrent deep vein thrombosis, PAI-1 levels were 44 +/- 20 ng/mL (mean +/- SD, n = 7), during a clinically silent phase. Four of these patients had a level above 38 ng/mL (mean +/- 2 SD of normal). The present assay, based on stable and reproducible reagents, allows the specific determination of PAI-1 antigen in biologic fluids. It may facilitate interlaboratory comparisons and be useful for further investigations of the role of PAI-1 in clinical conditions associated with impaired fibrinolysis and/or a tendency to thrombosis and investigations of the role of PAI-1 in platelets.


Blood ◽  
1988 ◽  
Vol 71 (1) ◽  
pp. 220-225 ◽  
Author(s):  
PJ Declerck ◽  
MC Alessi ◽  
M Verstreken ◽  
EK Kruithof ◽  
I Juhan-Vague ◽  
...  

Abstract An enzyme-linked immunosorbent assay for plasminogen activator inhibitor-1 (PAI-1) in biologic fluids was developed on the basis of two murine monoclonal antibodies raised against PAI-1 purified from HT- 1080 fibrosarcoma cells. The lower limit of sensitivity of the assay in plasma is 2 ng/mL. The assay is 12 times less sensitive toward the PAI- 1/human tissue-type plasminogen activator (t-PA) complex as compared with free PAI-1. The intraassay, interassay, and interdilution coefficients of variation are 5.2%, 8.0%, and 7.1%, respectively. The level of PAI-1 in platelet-poor plasma of healthy subjects is 18 +/- 10 ng/mL (mean +/- SD, n = 45). In platelet-rich plasma after freezing and thawing, 92% of PAI-1 antigen is released from platelets, whereas only 8% is found in the corresponding platelet-poor plasma. In platelet-poor plasma from healthy subjects, a linear correlation (r = 0.80) was found between PAI activity and PAI-1 antigen. In plasma approximately two thirds of the PAI-1 antigen was functionally active, whereas only 5% of the PAI-1 antigen released from platelets was active. During pregnancy a progressive increase of PAI-1 antigen levels up to three- to sixfold the control value was observed. In plasma of patients with recurrent deep vein thrombosis, PAI-1 levels were 44 +/- 20 ng/mL (mean +/- SD, n = 7), during a clinically silent phase. Four of these patients had a level above 38 ng/mL (mean +/- 2 SD of normal). The present assay, based on stable and reproducible reagents, allows the specific determination of PAI-1 antigen in biologic fluids. It may facilitate interlaboratory comparisons and be useful for further investigations of the role of PAI-1 in clinical conditions associated with impaired fibrinolysis and/or a tendency to thrombosis and investigations of the role of PAI-1 in platelets.


Plant Disease ◽  
1998 ◽  
Vol 82 (5) ◽  
pp. 569-572 ◽  
Author(s):  
E. L. Barnard ◽  
E. C. Ash ◽  
D. L. Hopkins ◽  
R. J. McGovern

A survey of more than 200 trees has documented the widespread occurrence of Xylella fastidiosa in Florida oak populations. The pathogen was detected readily via enzyme-linked immunosorbent assay in oaks exhibiting decline or leaf scorch symptoms and was infrequently detected in asymptomatic trees. It was also associated with reduced growth in Quercus laevis as measured by current-year shoot length. The occurrence of X. fastidiosa in Q. laevis and the evidence for its occurrence in Q. incana represent first reports for these oak hosts. The role of X. fastidiosa in oak decline scenarios deserves further attention.


2006 ◽  
Vol 17 (8) ◽  
pp. 621-624 ◽  
Author(s):  
Ariella Bar-Gil Shitrit ◽  
Dan Tzivony ◽  
Yuval Shilon ◽  
Bernard Rudensky ◽  
Jacklin Sulkes ◽  
...  

2008 ◽  
Vol 16 (1) ◽  
pp. 66-72 ◽  
Author(s):  
C. E. Lange ◽  
K. Tobler ◽  
C. Favrot ◽  
M. Müller ◽  
J. O. Nöthling ◽  
...  

ABSTRACT The role of papillomaviruses (PVs) in the development of canine cancers is controversial. However, recently a novel canine PV (CPV3) was detected in a dog affected with a condition reminiscent of epidermodysplasia verruciformis (EV). The aim of the present study was to investigate the seroprevalence of CPV3 by using generic enzyme-linked immunosorbent assays (ELISAs) for the detection of antibodies against either canine oral PV (COPV) or CPV3. Therefore, the capsid proteins of both PV types were expressed as glutathione S-transferase fusion protein antigens and adsorbed to glutathione-casein-coated ELISA plates. After showing that PV type-specific antibodies could be detected in the sera from dogs with confirmed COPV or CPV3 infection, CPV3- and COPV-seropositive samples were detected in two sets of canine sera collected in Switzerland and South Africa, respectively. We found specific antibodies against COPV and CPV3 among the tested sera and also a large number that were positive for both antigens. The seroprevalences of PV antibodies of 21.9% (COPV) and 26.9% (CPV3) among the tested dogs from South Africa were higher than those among the dogs from Switzerland at 10.5% (COPV) and 1.3% (CPV3). Our data suggest a need for further CPV-related seroepidemiological surveys in different countries, especially in the context of clinical manifestations and possible breed predispositions. For this purpose, the newly developed ELISAs can be a useful tool.


Blood ◽  
1983 ◽  
Vol 61 (1) ◽  
pp. 119-124 ◽  
Author(s):  
JD Nel ◽  
K Stevens ◽  
A Mouton ◽  
FJ Pretorius

Abstract Elevated levels of platelet-bound IgG (PA-IgG) are a feature of autoimmune thrombocytopenia (ATP), but it is well documented that this does not occur in all cases. This has led us to investigate the role of platelet-bound IgM (PA-IgM) in these patients using a quantitative enzyme-linked immunosorbent assay (ELISA). Forty-five determinations of PA-IgM and PA-IgG were done on 24 patients with ATP. Elevated levels of PA-IgM were found in 93.3% of the determinations, while PA-IgG was elevated in only 71.7%. In 64.4% of determinations, both were elevated. Elevated PA-IgM or PA-IgG alone occurred in 28.9% and 6.7% of determinations, respectively. These results show the hitherto unrecognized frequent involvement of PA-IgM in ATP and suggests that a complex interrelationship exists between the two immunoglobulin classes in ATP. Some of the possibilities that might explain this interrelationship are discussed.


1991 ◽  
Vol 37 (9) ◽  
pp. 1645-1648 ◽  
Author(s):  
M Tozuka ◽  
Y Yoshida ◽  
J Tanigami ◽  
M Miyachi ◽  
T Katsuyama ◽  
...  

Abstract Measurement of apolipoprotein (apo) E-AII complex in human plasma is important in determining the role of apoE in lipoprotein metabolism. In this paper, we demonstrate a new and simple method to determine apoE-All complex by using an enzyme-linked immunosorbent assay. Anti-apoE IgG (goat) was used as a capture antibody, and captured apoE-All complexes were detected by an anti-apoAll (rabbit) horseradish peroxidase-conjugated anti-rabbit IgG (goat) system. With this method, apoE-All complex was specifically determined without the interference of apoAll and was not affected by apoE monomer less than 250 mg/L. The content of the complex in reference serum, a normolipidemic serum pooled from five subjects with phenotype E3/E3, was arbitrarily defined as 100%. The coefficients of variation were 3.5%-6.3% within assay and 8.8%-11.6% between assays.


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