2006
DOI: 10.1099/jmm.0.46621-0
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Antigenicity of borrelial protein BBK32 fragments in early Lyme borreliosis

Abstract: Recombinantly produced borrelial BBK32 protein fragments originating from Borrelia burgdorferi sensu stricto, Borrelia garinii and Borrelia afzelii were evaluated as antigens in the serology of Lyme borreliosis (LB). In ELISA, a mid-portion hydrophilic fragment reacted with LB patient sera. Of the 23 patients with culture-or PCR-positive erythema migrans (EM), 43 % at diagnosis and 52 % at convalescence were positive for at least one Borrelia species-specific variant BBK32 fragment antigen. In parallel ELISAs … Show more

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Cited by 5 publications
(9 citation statements)
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“…In addition, studies with BBK32 indicate that protein fragments may be better suited for early Lyme disease serology. We are currently investigating that approach for RevA, using various protein fragments to eliminate possible cross-reactive epitopes and increase the specificity of this serological test (23).…”
Section: Discussionmentioning
confidence: 99%
“…In addition, studies with BBK32 indicate that protein fragments may be better suited for early Lyme disease serology. We are currently investigating that approach for RevA, using various protein fragments to eliminate possible cross-reactive epitopes and increase the specificity of this serological test (23).…”
Section: Discussionmentioning
confidence: 99%
“…qRT-PCR analyses revealed that bbk32 was expressed at substantially lower levels in the DMC-cultivated wild-type Bb (0.005 copies per 100 flaB) used for the microarray hybridizations compared with their in vitro counterparts (20.79 copies per 100 flaB). These data, however, seemed to be at odds with the demonstrated expression of BBK32 during infection (Lahdenne et al, 2006;Li et al, 2006) and its potential role in virulence , prompting us to examine RNAs from additional DMC-cultivated c162 (wild type) and c174 (rpoS mutant). Results from these subsequent analyses yielded substantially higher bbk32 transcript levels (11.13 copies per 100 flaB) in the wild-type isolate and demonstrated a level of RpoS dependence (46.5-fold, P < 0.01) comparable to that observed at 37°C in vitro (data not shown).…”
Section: The In Vitro Rpos Regulon Differs Substantially From Its Dmcmentioning
confidence: 99%
“…Fibronectin-binding protein BBK32 plays an important role in the attachment to the extracellular matrix. BBK32 is highly immunogenic and is present in sera of Lyme disease-infected patients (Heikkilä et al 2002;Lahdenne et al 2006). BBK32 antisera can interfere with borrelial transmission at various stages of the vector-host life cycle (Fikrig et al 2000).…”
Section: Prophylactic Treatment Strategiesmentioning
confidence: 99%