MICROARRAY CHARACTERIZATION OF THE HRPL REGULON OF THE FIRE BLIGHT PATHOGEN ERWINIA AMYLOVORA

2011 ◽  
pp. 263-270
Author(s):  
R.R. McNally ◽  
G.W. Sundin ◽  
Y.F. Zhao ◽  
I.K. Toth ◽  
P.J.A. Cock ◽  
...  

2015 ◽  
Vol 14 (3) ◽  
pp. 142-147 ◽  
Author(s):  
Nader A. Ashmawy ◽  
Taha I. Zaghlou ◽  
Moustafa A. El-Saba


Author(s):  
Stefano Benini

Abstract Together with genome analysis and knock-out mutants, structural and functional characterization of proteins provide valuable hints on the biology of the organism under investigation. Structural characterization can be achieved by techniques such as X-ray crystallography, NMR, Cryo-EM. The information derived from the structure are a good starting point to comprehend the details of the proteins molecular function for a better understanding of their biological role. This review aims at describing the progress in the structural and functional characterization of proteins from the plant pathogen Erwinia amylovora obtained by structural biology and currently deposited in the Protein Data Bank.



2002 ◽  
Vol 68 (11) ◽  
pp. 5704-5710 ◽  
Author(s):  
Abdelhamid Jabrane ◽  
Ahmed Sabri ◽  
Philippe Compère ◽  
Philippe Jacques ◽  
Isabel Vandenberghe ◽  
...  

ABSTRACT Serratia plymithicum J7 culture supernatant displayed activity against many pathogenic strains of Erwinia amylovora, the causal agent of the most serious bacterial disease of apple and pear trees, fire blight, and against Klebsiella pneumoniae, Serratia liquefaciens, Serratia marcescens, and Pseudomonas fluorescens. This activity increased significantly upon induction with mitomycin C. A phage-tail-like bacteriocin, named serracin P, was purified from an induced culture supernatant of S. plymithicum J7. It was found to be the only compound involved in the antibacterial activity against sensitive strains. The N-terminal amino acid sequence analysis of the two major subunits (23 and 43 kDa) of serracin P revealed high homology with the Fels-2 prophage of Salmonella enterica, the coliphages P2 and 168, the φCTX prophage of Pseudomonas aeruginosa, and a prophage of Yersinia pestis. This strongly suggests a common ancestry for serracin P and these bacteriophages.



2017 ◽  
Vol 149 (3) ◽  
pp. 639-652 ◽  
Author(s):  
I. Schwarczinger ◽  
J. Kolozsváriné Nagy ◽  
A. Künstler ◽  
L. Szabó ◽  
K. Geider ◽  
...  


Author(s):  
M. Hevesi ◽  
J. Papp ◽  
E. Jámbor-Benczúr ◽  
K. Kaszáné Csizmár ◽  
I. Pozsgai ◽  
...  

A useful method was improved to test and to evaluate the susceptibility of plants to fire blight and the virulence of E. amylovora strains. Six Hungarian strains from different host plants were tested on in vitro cultured apple rootstocks. Disease rating was used for the characterization of the process of disease development. The different strains had different capacity to cause disease, mainly in the first period of incubation. There were significant differences between the virulence of the strains.



2018 ◽  
Vol 202 (3) ◽  
pp. 236-249 ◽  
Author(s):  
Marco Salomone-Stagni ◽  
Joseph D. Bartho ◽  
Ivan Polsinelli ◽  
Dom Bellini ◽  
Martin A. Walsh ◽  
...  


2020 ◽  
Vol 367 (20) ◽  
Author(s):  
Candace R Alexander ◽  
Regan B Huntley ◽  
Neil P Schultes ◽  
George S Mourad

ABSTRACT Erwinia amylovora is the causal agent of fire blight, an economically important disease of apples and pears. As part of the infection process, Er. amylovora propagates on different plant tissues each with distinct nutrient environments. Here, the biochemical properties of the Er. amylovora adenine permease (EaAdeP) are investigated. Heterologous expression of EaAdeP in nucleobase transporter-deficient Escherichia coli strains, coupled with radiolabel uptake studies, revealed that EaAdeP is a high affinity adenine transporter with a Km of 0.43 ± 0.09 μM. Both Es. coli and Er. amylovora carrying extra copies of EaAdeP are sensitive to growth on the toxic analog 8-azaadenine. EaAdeP is expressed during immature pear fruit infection. Immature pear and apple fruit virulence assays reveal that an E. amylovora ΔadeP::Camr mutant is still able to cause disease symptoms, however, with growth at a lower level, indicating that external adenine is utilized in disease establishment.



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