Characterization of the Babesia gibsoni 12-kDa protein as a potential antigen for the serodiagnosis

2009 ◽  
Vol 58 (1) ◽  
pp. 55-60 ◽  
Author(s):  
Youn-Kyoung Goo ◽  
Honglin Jia ◽  
G. Oluga Aboge ◽  
M. Alaa Terkawi ◽  
Eung-goo Lee ◽  
...  
Keyword(s):  
2009 ◽  
Vol 165 (3-4) ◽  
pp. 318-322 ◽  
Author(s):  
M. Trotta ◽  
E. Carli ◽  
G. Novari ◽  
T. Furlanello ◽  
L. Solano-Gallego

2006 ◽  
Vol 148 (2) ◽  
pp. 190-198 ◽  
Author(s):  
Jinlin Zhou ◽  
Shinya Fukumoto ◽  
Honglin Jia ◽  
Naoaki Yokoyama ◽  
Guohong Zhang ◽  
...  

2014 ◽  
Vol 76 (1) ◽  
pp. 139-143 ◽  
Author(s):  
Tatsunori MASATANI ◽  
Masahito ASADA ◽  
Madoka ICHIKAWA-SEKI ◽  
Miho USUI ◽  
Mohamad A. TERKAWI ◽  
...  
Keyword(s):  

2003 ◽  
Vol 131 (2) ◽  
pp. 129-136 ◽  
Author(s):  
Shinya Fukumoto ◽  
Xuenan Xuan ◽  
Noboru Inoue ◽  
Ikuo Igarashi ◽  
Chihiro Sugimoto ◽  
...  

2009 ◽  
Vol 123 (3) ◽  
pp. 273-276 ◽  
Author(s):  
Youn-Kyoung Goo ◽  
Honglin Jia ◽  
Mohamad Alaa Terkawi ◽  
Gabriel Oluga Aboge ◽  
Junya Yamagishi ◽  
...  

Parasitology ◽  
2007 ◽  
Vol 134 (9) ◽  
pp. 1185-1194 ◽  
Author(s):  
G. O. ABOGE ◽  
H. JIA ◽  
K. KURIKI ◽  
J. ZHOU ◽  
Y. NISHIKAWA ◽  
...  

SUMMARYWe cloned and expressed a novel gene encoding a 32-kDa merozoite protein ofBabesia gibsoni(BgP32). The length of nucleotide sequence of the cDNA was 1464 bp with an open reading frame of 969 bp. The truncated recombinant BgP32 (rBgP32) without a signal peptide and C-terminal hydrophobic sequence was expressed inEscherichia colias a soluble glutathione-S-transferase (GST) fusion protein. Western blotting demonstrated that the native protein was 32-kDa, consistent with molecular weight of the predicted mature polypeptide. Enzyme-linked immunosorbent assay (ELISA) using rBgP32 detected specific antibodies from 8 days to 541 days post-infection in the sequential sera from a dog experimentally infected withB. gibsoni. Moreover, the antigen did not cross-react withB. canissubspecies and closely related protozoan parasites, indicating that rBgP32 is a specific diagnostic antigen. Analysis of 47 sera taken from dogs with anaemic signs revealed that rBgP32 detected a higher proportion ofB. gibsoniseropositive samples (77%) than its previously identified rBgP50 (68%) homologue. These results indicate that the BgP32 is a novel immunodominant antigen ofB. gibsoni, and rBgP32 might be useful for diagnosis ofB. gibsoniinfection.


Parasitology ◽  
2009 ◽  
Vol 136 (9) ◽  
pp. 945-952 ◽  
Author(s):  
H. JIA ◽  
M. A. TERKAWI ◽  
G. O. ABOGE ◽  
Y.-K. GOO ◽  
Y. LUO ◽  
...  

SUMMARYPeptidases of parasitic protozoa are currently under intense investigation in order to identify novel virulence factors, drug targets, and vaccine candidates, except in Babesia. Leucine aminopeptidases in protozoa, such as Plasmodium and Leishmania, have been identified to be involved in free amino acid regulation. We report here the molecular and enzymatic characterization, as well as the localization of a leucine aminopeptidase, a member of the M17 cytosolic aminopeptidase family, from B. gibsoni (BgLAP). A functional recombinant BgLAP (rBgLAP) expressed in Escherichia coli efficiently hydrolysed synthetic substrates for aminopeptidase, a leucine substrate. Enzyme activity of the rBgLAP was found to be optimum at pH 8·0 and at 37°C. The substrate profile was slightly different from its homologue in P. falciprum. The activity was also strongly dependent on metal divalent cations, and was inhibited by bestatin, which is a specific inhibitor for metalloprotease. These results indicated that BgLAP played an important role in free amino acid regulation.


1997 ◽  
Vol 83 (4) ◽  
pp. 692 ◽  
Author(s):  
Edward J. Wozniak ◽  
Bradd C. Barr ◽  
John W. Thomford ◽  
Itsuro Yamane ◽  
Sean P. McDonough ◽  
...  

2020 ◽  
Vol 13 (1) ◽  
Author(s):  
Qin Liu ◽  
Long Yu ◽  
Fan Jiang ◽  
Muxiao Li ◽  
Xueyan Zhan ◽  
...  

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