scholarly journals Determination of the Disulfide Bonds within a B Domain Variant Surface Glycoprotein fromTrypanosoma congolense

1998 ◽  
Vol 273 (49) ◽  
pp. 32582-32586 ◽  
Author(s):  
Holm Bußler ◽  
Monica Linder ◽  
Dietmar Linder ◽  
Erwin Reinwald
1968 ◽  
Vol 33 (2) ◽  
pp. 441-461 ◽  
Author(s):  
V. Holeyšovský ◽  
B. Mesrob ◽  
V. Tomášek ◽  
O. Mikeš ◽  
F. Šorm
Keyword(s):  

2015 ◽  
Vol 200 (1-2) ◽  
pp. 1-4 ◽  
Author(s):  
Kiantra Ramey-Butler ◽  
Elisabetta Ullu ◽  
Nikolay G. Kolev ◽  
Christian Tschudi

2003 ◽  
Vol 2 (1) ◽  
pp. 84-94 ◽  
Author(s):  
Mihaela Lorger ◽  
Markus Engstler ◽  
Matthias Homann ◽  
H. Ulrich Göringer

ABSTRACT African trypanosomes cause sleeping sickness in humans and Nagana in cattle. The parasites multiply in the blood and escape the immune response of the infected host by antigenic variation. Antigenic variation is characterized by a periodic change of the parasite protein surface, which consists of a variant glycoprotein known as variant surface glycoprotein (VSG). Using a SELEX (systematic evolution of ligands by exponential enrichment) approach, we report the selection of small, serum-stable RNAs, so-called aptamers, that bind to VSGs with subnanomolar affinity. The RNAs are able to recognize different VSG variants and bind to the surface of live trypanosomes. Aptamers tethered to an antigenic side group are capable of directing antibodies to the surface of the parasite in vitro. In this manner, the RNAs might provide a new strategy for a therapeutic intervention to fight sleeping sickness.


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