Characterization of bacteriophage pAh-1 and its protective effects on experimental infection of Aeromonas hydrophila in Zebrafish (Danio rerio )

2016 ◽  
Vol 40 (6) ◽  
pp. 841-846 ◽  
Author(s):  
M Easwaran ◽  
S H S Dananjaya ◽  
S C Park ◽  
J Lee ◽  
H-J Shin ◽  
...  
PLoS ONE ◽  
2015 ◽  
Vol 10 (4) ◽  
pp. e0122365 ◽  
Author(s):  
Pellegrino Mazzone ◽  
Ivan Scudiero ◽  
Angela Ferravante ◽  
Marina Paolucci ◽  
Luca E. D’Andrea ◽  
...  

2013 ◽  
Vol 142-143 ◽  
pp. 447-457 ◽  
Author(s):  
Afonso C.D. Bainy ◽  
Akira Kubota ◽  
Jared V. Goldstone ◽  
Roger Lille-Langøy ◽  
Sibel I. Karchner ◽  
...  

2018 ◽  
Vol 9 (11) ◽  
pp. 5791-5804 ◽  
Author(s):  
Yi Zhang ◽  
Yuhang Zhou ◽  
Qingyang Tang ◽  
Feng Hu ◽  
Lixue Feng ◽  
...  

Beta-cypermethrin (beta-CYP), which is widely used for the control of indoor and field pests, is a highly lipophilic insecticide with environmental estrogenic effects.


2006 ◽  
Vol 74 (7) ◽  
pp. 3742-3755 ◽  
Author(s):  
Lakshmi Pillai ◽  
Jian Sha ◽  
Tatiana E. Erova ◽  
Amin A. Fadl ◽  
Bijay K. Khajanchi ◽  
...  

ABSTRACT Human diseases caused by species of Aeromonas have been classified into two major groups: septicemia and gastroenteritis. In this study, we reported the molecular and functional characterization of a new virulence factor, ToxR-regulated lipoprotein, or TagA, from a diarrheal isolate, SSU, of Aeromonas hydrophila. The tagA gene of A. hydrophila exhibited 60% identity with that of a recently identified stcE gene from Escherichia coli O157:H7, which encoded a protein (StcE) that provided serum resistance to the bacterium and prevented erythrocyte lysis by controlling classical pathway of complement activation by cleaving the complement C1-esterase inhibitor (C1-INH). We purified A. hydrophila TagA as a histidine-tagged fusion protein (rTagA) from E. coli DE3 strain using a T7 promoter-based pET30 expression vector and nickel affinity column chromatography. rTagA cleaved C1-INH in a time-dependent manner. The tagA isogenic mutant of A. hydrophila, unlike its corresponding wild-type (WT) or the complemented strain, was unable to cleave C1-INH, which is required to potentiate the C1-INH-mediated lysis of host and bacterial cells. We indeed demonstrated colocalization of C1-INH and TagA on the bacterial surface by confocal fluorescence microscopy, which ultimately resulted in increased serum resistance of the WT bacterium. Likewise, we delineated the role of TagA in contributing to the enhanced ability of C1-INH to inhibit the classical complement-mediated lysis of erythrocytes. Importantly, we provided evidence that the tagA mutant was significantly less virulent in a mouse model of infection (60%) than the WT bacterium at two 50% lethal doses, which resulted in 100% mortality within 48 h. Taken together, our data provided new information on the role of TagA as a virulence factor in bacterial pathogenesis. This is the first report of TagA characterization from any species of Aeromonas.


2007 ◽  
Vol 408 (3) ◽  
pp. 395-406 ◽  
Author(s):  
Marta Manzoni ◽  
Paolo Colombi ◽  
Nadia Papini ◽  
Luana Rubaga ◽  
Natascia Tiso ◽  
...  

Sialidases remove sialic acid residues from various sialo-derivatives. To gain further insights into the biological roles of sialidases in vertebrates, we exploited zebrafish (Danio rerio) as an animal model. A zebrafish transcriptome- and genome-wide search using the sequences of the human NEU polypeptides as templates revealed the presence of seven different genes related to human sialidases. neu1 and neu4 are the putative orthologues of the mammalian sialidases NEU1 and NEU4 respectively. Interestingly, the remaining genes are organized in clusters located on chromosome 21 and are all more closely related to mammalian sialidase NEU3. They were thus named neu3.1, neu3.2, neu3.3, neu3.4 and neu3.5. Using RT–PCR (reverse transcription–PCR) we detected transcripts for all genes, apart from neu3.4, and whole-mount in situ hybridization experiments show a localized expression pattern in gut and lens for neu3.1 and neu4 respectively. Transfection experiments in COS7 (monkey kidney) cells demonstrate that Neu3.1, Neu3.2, Neu3.3 and Neu4 zebrafish proteins are sialidase enzymes. Neu3.1, Neu3.3 and Neu4 are membrane-associated and show a very acidic pH optimum below 3.0, whereas Neu3.2 is a soluble sialidase with a pH optimum of 5.6. These results were further confirmed by subcellular localization studies carried out using immunofluorescence. Moreover, expression in COS7 cells of these novel zebrafish sialidases (with the exception of Neu3.2) induces a significant modification of the ganglioside pattern, consistent with the results obtained with membrane-associated mammalian sialidases. Overall, the redundancy of sialidases together with their expression profile and their activity exerted on gangliosides of living cells indicate the biological relevance of this class of enzymes in zebrafish.


FEBS Letters ◽  
2000 ◽  
Vol 467 (2-3) ◽  
pp. 221-225 ◽  
Author(s):  
Maria Hernandez Valladares ◽  
Martin Kiefer ◽  
Uwe Heinz ◽  
Raquel Paul Soto ◽  
Wolfram Meyer-Klaucke ◽  
...  

Sign in / Sign up

Export Citation Format

Share Document