نتایج جستجو برای: outer surface protein a ospa

تعداد نتایج: 13873334  

Journal: :The Journal of clinical investigation 1997
S E Schutzer P K Coyle L B Krupp Z Deng A L Belman R Dattwyler B J Luft

Lyme disease is the major tick-borne disease, caused by Borrelia burgdorferi (Bb). Neurological involvement is common in all stages. In vivo expression of Bb antigens (Ags) and the immune response to them has not been well investigated in the cerebrospinal fluid (CSF). Upregulation of outer surface protein (Osp) C and concomitant downregulation of OspA before tick inoculation of the spirochete ...

2008
Michael E. Woodman Anne E. Cooley Brian Stevenson Patrick Brennan

The Lyme disease spirochete, Borrelia burgdorferi, produces two outer surface lipoproteins, OspA and OspB, that are essential for colonization of tick vectors. Both proteins are highly expressed during transmission from infected mammals to feeding ticks and during colonization of tick midguts, but are repressed when bacteria are transmitted from ticks to mammals. Humans and other infected mamma...

Journal: :Infection and immunity 1998
G H Giambartolomei V A Dennis M T Philipp

Heat-killed Borrelia burgdorferi spirochetes stimulate in vitro production of interleukin-10 (IL-10) at both mRNA and protein levels in peripheral blood mononuclear cells (PBMC) of uninfected rhesus monkeys. A concomitant down-modulation of IL-2 gene transcription was observed. Neither IL-4 nor gamma interferon gene expression was ostensibly affected by B. burgdorferi spirochetes. These phenome...

Journal: :Journal of immunology 1998
T J Sellati D A Bouis R L Kitchens R P Darveau J Pugin R J Ulevitch S C Gangloff S M Goyert M V Norgard J D Radolf

Lipoproteins of Treponema pallidum and Borrelia burgdorferi possess potent proinflammatory properties and, thus, have been implicated as major proinflammatory agonists in syphilis and Lyme disease. Here we used purified B. burgdorferi outer surface protein A (OspA) and synthetic lipopeptides corresponding to the N-termini of OspA and the 47-kDa major lipoprotein immunogen of T. pallidum to clar...

Journal: :Journal of clinical microbiology 1997
D E Norris B J Johnson J Piesman G O Maupin J L Clark W C Black

In Colorado, Borrelia burgdorferi sensu stricto, the etiologic agent of Lyme disease, is maintained in an enzootic cycle between Ixodes spinipalpis ticks and Neotoma mexicana rats (27). The frequencies of flagellin (fla), 66-kDa protein (p66), and outer surface protein A (ospA) alleles were examined in 71 B. burgdorferi isolates from samples from Colorado. Approximately two-thirds of these samp...

Journal: :cell journal 0

introduction: to investigate the role of borrelia infections in pathogenesis of multiple sclerosis (ms) the presence of antibody against borrelia persica (the most common species of borrelia in iran) in the serum and csf of ms patients was studied. material and methods: the presence of antibodies against borrelia persica antigens was studied in the serum and csf of 50 ms patients and 30 age and...

2014
Yanlin Shi Poonam Dadhwal Xin Li Fang Ting Liang Janakiram Seshu

The Lyme disease spirochete, Borrelia burgdorferi, must abundantly produce outer surface lipoprotein A (OspA) in the tick vector but downregulate OspA in mammals in order to evade the immune system and maintain its natural enzootic cycle. Here, we show that BosR binds two regulatory elements of the ospAB operon and that increasing BosR expression leads to downregulation of OspA. Both regulatory...

Journal: :Biochemical Society transactions 2003
T G Schwan

In the 20 years since the first agent of Lyme disease was discovered, much interest has focused on the possible biological roles of a few outer surface proteins (Osps) in the alternating life cycle that includes ticks and vertebrate hosts. Two major proteins, OspA and OspC, are differentially regulated by the spirochaete Borrelia burgdorferi during the several days when ticks feed. The reciproc...

Journal: :Infection and immunity 1993
N Margolis P A Rosa

We have characterized a Borrelia burgdorferi clone (CA-11 2A) that does not synthesize the major outer surface proteins, OspA and OspB. While the osp operon is intact and capable of expression, no mRNA transcript is detectable in this clone. These results suggest that osp operon expression in the B. burgdorferi clone can be regulated at the level of transcription.

Journal: :The Journal of biological chemistry 2001
C Eicken V Sharma T Klabunde R T Owens D S Pikas M Höök J C Sacchettini

The outer surface protein C (OspC) is one of the major host-induced antigens of Borrelia burgdorferi, the causative agent of Lyme disease. We have solved the crystal structure of recombinant OspC to a resolution of 2.5 A. OspC, a largely alpha-helical protein, is a dimer with a characteristic central four-helical bundle formed by association of the two longest helices from each subunit. OspC is...

نمودار تعداد نتایج جستجو در هر سال

با کلیک روی نمودار نتایج را به سال انتشار فیلتر کنید