Multiple Amino Acid Sequence Alignment of the Major Outer Surface Proteins OspA and OspB of Various Borrelia Burgdorferi Strains

1994 ◽  
pp. 181-186
Author(s):  
Waltraud Fellinger ◽  
Markus Reindl ◽  
Georg Stöffler ◽  
Bernhard Redl
PLoS ONE ◽  
2013 ◽  
Vol 8 (9) ◽  
pp. e72751 ◽  
Author(s):  
James B. Howard ◽  
Katerina J. Kechris ◽  
Douglas C. Rees ◽  
Alexander N. Glazer

2012 ◽  
Vol 66 (1) ◽  
pp. 1-19 ◽  
Author(s):  
Melisha R. Kenedy ◽  
Tiffany R. Lenhart ◽  
Darrin R. Akins

1995 ◽  
Vol 33 (7) ◽  
pp. 1867-1869 ◽  
Author(s):  
V Fingerle ◽  
U Hauser ◽  
G Liegl ◽  
B Petko ◽  
V Preac-Mursic ◽  
...  

1994 ◽  
Vol 112 (3) ◽  
pp. 533-542 ◽  
Author(s):  
C. M. Hu ◽  
S. Leuba-Garcia ◽  
M. D. Kramer ◽  
A. Aeschlimann ◽  
L. Gern

SUMMARYBorrelia burgdorferiisolates were obtained fromIxodes ricinusfrom three sites in Switzerland. They were examined by SDS-PAGE and immunoblotting. The phenotypes, in respect of three outer surface proteins (Osp), differed between the sites of collection. In site 1, most isolates had an OspA of 31 kDa and an OspB of 34 kDa: in site 2, isolates presenting an OspA of 33 kDa dominated and in site 3, the isolates with an OspA of 32 kDa and an OspB of 35 kDa were most frequent. This distribution differed significantly. About half of the isolates from sites 1 and 3 reacted with anti-OspA monoclonal antibody H5332 compared to 29% from site 2. Site 1 isolates reacted significantly more frequently (81 %) with another anti-OspA monoclonal antibody LA-31 than isolates from site 3 (P< 0·0001). These findings have implications for the epidemiology of Lyme borreliosis, for the further development of serodiagnostic reagents and for the development of a vaccine.


2005 ◽  
Vol 73 (9) ◽  
pp. 6138-6142 ◽  
Author(s):  
Rodolfo C. Garcia ◽  
Rossella Murgia ◽  
Marina Cinco

ABSTRACT Persistence of borreliae within the vertebrate host depends on the fate of interactions between the spirochetes and target cells. The present work demonstrates the direct binding of the Borrelia burgdorferi outer surface proteins OspA and OspB to CR3 and that this binding is independent of iC3b.


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