scholarly journals Flagellin and Outer Surface Proteins from Borrelia burgdorferi Are Not Glycosylated

2008 ◽  
Vol 190 (7) ◽  
pp. 2619-2623 ◽  
Author(s):  
Ján Štěrba ◽  
Marie Vancová ◽  
Nataliia Rudenko ◽  
Maryna Golovchenko ◽  
Tammy-Lynn Tremblay ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Borrelia Burgdorferi ◽  
Outer Membrane ◽  
Outer Surface ◽  
Culture Medium ◽  
Outer Membrane Proteins ◽  
Surface Proteins ◽  
Outer Surface Proteins ◽  
Flagellar Proteins

ABSTRACT We investigated the presence of glycoproteins in Borrelia burgdorferi. We did not find any evidence for glycosylation of the major outer membrane proteins OspA and OspB or the structural flagellar proteins FlaB and FlaA. We suggest that glycoproteins present on the surface of B. burgdorferi may be tightly bound culture medium glycoproteins.

scholarly journals Differential Expression and Sequence Conservation of the Anaplasma marginale msp2 Gene Superfamily Outer Membrane Proteins

2006 ◽  
Vol 74 (6) ◽  
pp. 3471-3479 ◽  
Author(s):  
Susan M. Noh ◽  
Kelly A. Brayton ◽  
Donald P. Knowles ◽  
Joseph T. Agnes ◽  
Michael J. Dark ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Outer Membrane ◽  
Differential Expression ◽  
Outer Membrane Proteins ◽  
Anaplasma Marginale ◽  
Surface Proteins ◽  
Transcriptional Analysis ◽  
Mammalian Host ◽  
Anaplasma Ovis ◽  
Sequence Comparisons

ABSTRACT Bacterial pathogens in the genera Anaplasma and Ehrlichia encode a protein superfamily, pfam01617, which includes the predominant outer membrane proteins (OMPs) of each species, major surface protein 2 (MSP2) and MSP3 of Anaplasma marginale and Anaplasma ovis, Anaplasma phagocytophilum MSP2 (p44), Ehrlichia chaffeensis p28-OMP, Ehrlichia canis p30, and Ehrlichia ruminantium MAP1, and has been shown to be involved in both antigenic variation within the mammalian host and differential expression between the mammalian and arthropod hosts. Recently, complete sequencing of the A. marginale genome has identified an expanded set of genes, designated omp1-14, encoding new members of this superfamily. Transcriptional analysis indicated that, with the exception of the three smallest open reading frames, omp2, omp3, and omp6, these superfamily genes are transcribed in A. marginale-infected erythrocytes, tick midgut and salivary glands, and the IDE8 tick cell line. OMPs 1, 4, 7 to 9, and 11 were confirmed to be expressed as proteins by A. marginale within infected erythrocytes, with expression being either markedly lower (OMPs 1, 4, and 7 to 9) or absent (OMP11) in infected tick cells, which reflected regulation at the transcript level. Although the pfam01617 superfamily includes the antigenically variable MSP2 and MSP3 surface proteins, analysis of the omp1-14 sequences throughout a cycle of acute and persistent infection in the mammalian host and tick transmission reveals a high degree of conservation, an observation supported by sequence comparisons between the St. Maries strain and Florida strain genomes.

scholarly journals The role of Borrelia burgdorferi outer surface proteins

2012 ◽  
Vol 66 (1) ◽  
pp. 1-19 ◽  
Author(s):  
Melisha R. Kenedy ◽  
Tiffany R. Lenhart ◽  
Darrin R. Akins
Keyword(s):  
Borrelia Burgdorferi ◽  
Outer Surface ◽  
Surface Proteins ◽  
Outer Surface Proteins

scholarly journals Expression of outer surface proteins A and C of Borrelia burgdorferi in Ixodes ricinus.

1995 ◽  
Vol 33 (7) ◽  
pp. 1867-1869 ◽  
Author(s):  
V Fingerle ◽  
U Hauser ◽  
G Liegl ◽  
B Petko ◽  
V Preac-Mursic ◽  
...  
Keyword(s):  
Borrelia Burgdorferi ◽  
Ixodes Ricinus ◽  
Outer Surface ◽  
Surface Proteins ◽  
Outer Surface Proteins

The search forBrachyspiraouter membrane proteins that interact with the host

2001 ◽  
Vol 2 (1) ◽  
pp. 19-30 ◽  
Author(s):  
Darren J. Trott ◽  
David P. Alt ◽  
Richard L. Zuerner ◽  
Michael J. Wannemuehler ◽  
Thaddeus B. Stanton
Keyword(s):  
Membrane Proteins ◽  
Outer Membrane ◽  
Membrane Vesicle ◽  
Outer Membrane Proteins ◽  
Indirect Evidence ◽  
Membrane Vesicles ◽  
Outer Membrane Vesicles ◽  
Surface Proteins ◽  
Brachyspira Pilosicoli ◽  
Variable Surface

AbstractLittle is known about the outer membrane structure ofBrachyspira hyodysenteriae and Brachyspira pilosicolior the role of outer membrane proteins (OMPs) in host colonization and the development of disease. The isolation of outer membrane vesicles fromB. hyodysenteriaehas confirmed that cholesterol is a significant outer membrane constituent and that it may impart unique characteristics to the lipid bilayer structure, including a reduced density. Unique proteins that have been identified in theB. hyodysenteriaeouter membrane include the variable surface proteins (Vsp) and lipoproteins such as SmpA and BmpB. While the function of these proteins remains to be determined, there is indirect evidence to suggest that they may be involved in immune evasion. These data may explain the ability of the organism to initiate chronic infection. OMPs may be responsible for the unique attachment ofB. pilosicolito colonic epithelial cells; however, the onlyB. pilosicoliOMPs that have been identified to date are involved in metabolism. In order to identify furtherB. pilosicoliOMPs we have isolated membrane vesicle fractions from porcine strain 95–1000 by osmotic lysis and isopycnic centrifugation. The fractions were free of contamination by cytoplasm and fla-gella and contained outer membrane. Inner membrane contamination was minimal but could not be completely excluded. An abundant 45-kDa, heat-modifiable protein was shown to have significant homology withB. hyodysenteriaeVsp, and monoclonal antibodies were produced that reacted with fiveB. pilosicoli-specificmembrane protein epitopes. The first of these proteins to be characterized is a unique surface-exposed lipoprotein.

scholarly journals Comparison in the immunological properties ofBorrelia burgdorferiisolates fromIxodes ricinusderived from three endemic areas in Switzerland

1994 ◽  
Vol 112 (3) ◽  
pp. 533-542 ◽  
Author(s):  
C. M. Hu ◽  
S. Leuba-Garcia ◽  
M. D. Kramer ◽  
A. Aeschlimann ◽  
L. Gern
Keyword(s):  
Monoclonal Antibody ◽  
Borrelia Burgdorferi ◽  
Lyme Borreliosis ◽  
Ixodes Ricinus ◽  
Outer Surface ◽  
Surface Proteins ◽  
Immunological Properties ◽  
Outer Surface Proteins ◽  
Sds Page ◽  
Further Development

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.

scholarly journals Complement Receptor 3 Binds the Borrelia burgdorferi Outer Surface Proteins OspA and OspB in an iC3b-Independent Manner

2005 ◽  
Vol 73 (9) ◽  
pp. 6138-6142 ◽  
Author(s):  
Rodolfo C. Garcia ◽  
Rossella Murgia ◽  
Marina Cinco
Keyword(s):  
Borrelia Burgdorferi ◽  
Outer Surface ◽  
Surface Proteins ◽  
Vertebrate Host ◽  
Target Cells ◽  
Complement Receptor ◽  
Independent Manner ◽  
Outer Surface Proteins ◽  
Direct Binding ◽  
Complement Receptor 3

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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