scholarly journals P103 Binding specificity and epitope analysis of monoclonal antibodies against trypanosome alternative oxidase (TAO)

2001 ◽  
Vol 52 (Supplement) ◽  
pp. 103
Author(s):  
Ayako YOSHIDA ◽  
Yoshisada YABU ◽  
Takashi SUZUKI ◽  
Kiyoshi KITA ◽  
Nobuko MINAGAWA ◽  
...  
Author(s):  
Sotaro Yamasaki ◽  
Mitsuo Shoji ◽  
Megumi Kayanuma ◽  
Vladimir Sladek ◽  
Daniel Ken Inaoka ◽  
...  

2003 ◽  
Vol 51 (2) ◽  
pp. 237-244 ◽  
Author(s):  
K. Yeşilbağ ◽  
I. Burgu

In this study, 15 bovine viral diarrhoea viruses (BVDV) isolated from the field in Turkey were characterised for their biotype, cloned and eventually analysed for their epitopic composition in terms of glycoprotein E2. Immunoplaque assay, plaque assay, limiting dilution and streptavidin-biotin-peroxidase techniques were used for biotype characterisation, cloning of cytopathic (cp) and noncytopathic (ncp) biotypes and epitope analysis, respectively. While 14 out of 15 BVDV isolates were distinguished as ncp biotype, 1 isolate was found to be containing both biotypes (cp + ncp). According to the reactivity patterns of isolates with 15 monoclonal antibodies, 4 different antigenic groups could be formed. There were no antigenic differences between the isolates derived from the same animal with various time intervals. On the other hand, biotype clones isolated from the same animal exhibited difference in one epitope. This is the first study describing antigenic characterisation of BVDV field isolates in Turkey.


2008 ◽  
Vol 64 (a1) ◽  
pp. C275-C275
Author(s):  
Y. Kido ◽  
K. Sakamoto ◽  
D.K. Inaoka ◽  
S. Fujioka ◽  
T. Suzuki ◽  
...  

1992 ◽  
Vol 29 (10) ◽  
pp. 1191-1201 ◽  
Author(s):  
H. Kahlert ◽  
A. Petersen ◽  
W.-M. Becker ◽  
M. Schlaak

Author(s):  
Pam Fredman ◽  
Thomas Brezicka ◽  
Jan Holmgren ◽  
Leif Lindholm ◽  
Olle Nilsson ◽  
...  

1993 ◽  
Vol 30 (1) ◽  
pp. 1-16 ◽  
Author(s):  
Natalia A. Tsekhanovskaya ◽  
Leonid E. Matveev ◽  
Semen G. Rubin ◽  
Andrey S. Karavanov ◽  
Evgeniy K. Pressman

2020 ◽  
Vol 492 (1) ◽  
pp. 135-138
Author(s):  
V. A. Misyurin ◽  
Yu. P. Finashutina ◽  
A. A. Turba ◽  
M. V. Larina ◽  
O. N. Solopova ◽  
...  

2014 ◽  
Vol 13 (4) ◽  
pp. 539-547 ◽  
Author(s):  
VaNae Hamilton ◽  
Ujjal K. Singha ◽  
Joseph T. Smith ◽  
Ebony Weems ◽  
Minu Chaudhuri

ABSTRACTRecognition of mitochondrial targeting signals (MTS) by receptor translocases of outer and inner membranes of mitochondria is one of the prerequisites for import of nucleus-encoded proteins into this organelle. The MTS for a majority of trypanosomatid mitochondrial proteins have not been well defined. Here we analyzed the targeting signal for trypanosome alternative oxidase (TAO), which functions as the sole terminal oxidase in the infective form ofTrypanosoma brucei. Deleting the first 10 of 24 amino acids predicted to be the classical N-terminal MTS of TAO did not affect its import into mitochondriain vitro. Furthermore, ectopically expressed TAO was targeted to mitochondria in both forms of the parasite even after deletion of first 40 amino acid residues. However, deletion of more than 20 amino acid residues from the N terminus reduced the efficiency of import. These data suggest that besides an N-terminal MTS, TAO possesses an internal mitochondrial targeting signal. In addition, both the N-terminal MTS and the mature TAO protein were able to target a cytosolic protein, dihydrofolate reductase (DHFR), to aT. bruceimitochondrion. Further analysis identified a cryptic internal MTS of TAO, located within amino acid residues 115 to 146, which was fully capable of targeting DHFR to mitochondria. The internal signal was more efficient than the N-terminal MTS for import of this heterologous protein. Together, these results show that TAO possesses a cleavable N-terminal MTS as well as an internal MTS and that these signals act together for efficient import of TAO into mitochondria.


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