B. burgdorferi P41 (DAG2709)

B. burgdorferi P41 (aa 158-296), recombinant protein from E. coli

Product Overview
The E. coli derived recombinant protein contains the p41 immunodominant regions, 158-296 amino acids.
Nature
Recombinant
Tag/Conjugate
Unconjugated
Procedure
None
Purity
Purified by proprietary chromatographic technique. Protein is > 95% pure as determined by 10% PAGE (coomassie staining) and RP-HPLC.
Preservative
None
Storage
2-8°C short term, -20°C long term
Introduction
Borrelia burgdorferi is a bacterial species of the spirochete class of the genus Borrelia. B. burgdorferi is predominant in North America, but also exists in Europe, and is the agent of Lyme disease. All Borrelia are considered diderm (double-membrane) rather than gram positive or negative.
Keywords
B. burgdorferi p41; BB P41; Lyme disease spirochete; B. burgdorferi p41; Borrelia burgdorferi p41

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References


Development of enzyme-linked immunosorbent assays using recombinant borrelial antigens for serodiagnosis of Borrelia burgdorferi infection

MEDICAL MICROBIOLOGY AND IMMUNOLOGY

Authors: Burkert, S; Rossler, D; Munchhoff, P; Wilske, B

To improve Ige antibody detection in the serodiagnosis of Borrelia burgdorferi infection, indirect enzyme-linked immunosorbent assays (ELISAs) were developed utilizing purified recombinant antigens of B. burgdorferi sensu late: the chromosomally encoded proteins p100 of strain PKo (B. afzelii) and p41i (internal flagellin fragments) derived from strains PKo, PBi (B. garinii), and B31 (B. burgdorferi sensu stricto). In Western blot analysis, these proteins have proved to be highly specific and sensitive for IgG antibody detection, especially in late manifestations of Lyme borreliosis. Sera from 464 forest workers, a high-risk group for infections with B. burgdorferi, were investigated and the results compared with those obtained by a commercial ELISA using an octyl-beta-D-glucopyranoside (OGP) extract from B. afzelii (PKo) cells as the antigenic substrate. Sera derived from 200 blood donors served for determination of the 95% specific cut-off level. The number of positive test results using OGP-ELISA (23.9%) was only slightly higher than that using p100-ELISA (19.8%); corresponding results were observed in 84.7% of all sera (14.2% positive, 70.5% negative). The frequency and interassay correspondence of positive results increased with the age of the forest workers, as most markedly demonstrated by p100 and OGP assays (P<0.0001). Using the p41i-ELISAs, generally no significant strain-dependent differences in sensitivity were found (PKo, 13.8%; PBi, 14.2%; B31, 12.9%). Compared with the p100-ELISA, the p41i-assays showed significantly lower detection rates for IgG antibodies (P<0.03) and a reduced capacity for quantitative discrimination between seropositive individuals and negative controls (P<0.0007). At a 95% specificity, the IgG antibody detection rate could be increased to 23.1% when the p100-ELISA was evaluated in combination with the assays using p41i/PBi and P41i/B31. Due to its high sensitivity, the specific recombinant p100-ELISA might be a suitable test for detection of late immune responses to B. burgdorferi, thus being especially useful for epidemiological investigations.

COMPARISON OF WHOLE-CELL ANTIBODIES AND AN ANTIGENIC FLAGELLAR EPITOPE OF BORRELIA-BURGDORFERI IN SEROLOGIC TESTS FOR DIAGNOSIS OF LYME BORRELIOSIS

JOURNAL OF CLINICAL MICROBIOLOGY

Authors: MAGNARELLI, LA; FIKRIG, E; BERLAND, R; ANDERSON, JF; FLAVELL, RA

A recombinant protein (p41-G) of an antigenic region of flagellin was used in a standard and amplified enzyme-linked immunosorbent assay (ELISA) to detect antibodies to Borrelia burgdorferi, the causative agent of Lyme borreliosis. Comparable sensitivities (88 to 94%) were noted when sera from 17 persons who had erythema migrans and antibodies to whole-cell B. burgdorferi were tested against the p41-G antigen. In tests of a second study group of 36 persons who had erythema migrans but no detectable antibodies to whole-cell B. burgdorferi, 3 (8%) were positive when the p41-G antigen was used. Assay specificity likewise increased when the p41-G fragment was included in an ELISA with human sera containing treponemal antibodies. Recombinant flagellar proteins of B. burgdorferi, such as the p41-G antigen, can be used in an ELISA and may

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