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1.
Fig 6

Fig 6. From: Multiplex Assay Detection of Immunoglobulin G Antibodies That Recognize Babesia microti Antigens.

Reproducibility of the rBmSA1/GST MBA assay. (A) MBA values (MFI−BG) for assay plates that were run consecutively on two different Bio-Plex instruments on the same day; (B) MBA values (MFI−BG) for samples that were independently assayed approximately 2 weeks apart. Note that the values in panel B are plotted on a logarithmic scale to allow visualization of a wider range of values. Least-squares regression lines are given in both plots. The positive cutoff value for the rBmSA1/GST MBA was determined to be 1,122 MFI−BG units.

Jeffrey W. Priest, et al. Clin Vaccine Immunol. 2012 September;19(9):1539-1548.
2.
Fig 4

Fig 4. From: Multiplex Assay Detection of Immunoglobulin G Antibodies That Recognize Babesia microti Antigens.

Deduced amino acid sequence of the Bm17N clone. The deduced amino acid sequence of clone Bm17N is presented in a manner to highlight the repeat structure of the protein. The sequence contains two 47-amino-acid repeats and a substructure of six 32-amino-acid repeats. Compared to the published BMN1-17 and BMN1-20 sequences (35), the Bm17N sequence contained four base substitutions that resulted in three amino acid substitutions (indicated in the sequence by boldface italic letters) and the introduction of an in-frame stop codon (#, position 239) in the third repeat. The immunodominant 26-amino-acid peptide sequence identified by Houghton et al. (22) is indicated in boldface with an underline.

Jeffrey W. Priest, et al. Clin Vaccine Immunol. 2012 September;19(9):1539-1548.
3.
Fig 2

Fig 2. From: Multiplex Assay Detection of Immunoglobulin G Antibodies That Recognize Babesia microti Antigens.

Membrane-associated antigen identified by detergent extraction. A postsonication particulate fraction from B. microti-infected hamster red blood cells was extracted using Triton X-114 detergent as described in Materials and Methods. Extracted proteins were resolved on a 10 to 22.5% polyacrylamide gel and transferred to PVDF. Strips of membrane were incubated with sera from an infected hamster (A), sera from a babesiosis-positive patient (B), or AuroDye Forte colloidal gold stain (C). Bound IgG antibodies were visualized as described for Fig. 1. The positions of molecular mass markers (in thousands) are indicated on the left. A major immunodominant band is indicated by an arrow just above the 36-kDa marker.

Jeffrey W. Priest, et al. Clin Vaccine Immunol. 2012 September;19(9):1539-1548.
4.
Fig 1

Fig 1. From: Multiplex Assay Detection of Immunoglobulin G Antibodies That Recognize Babesia microti Antigens.

Identification of reactive B. microti antigens. Proteins from a hypotonic saponin lysate of B. microti-infected hamster red blood cells were resolved on a 12% polyacrylamide gel and electrotransferred to a PVDF membrane as described in Materials and Methods. Strips of membrane were incubated with sera from presumed-negative patients or with sera from confirmed-babesiosis patients at a dilution of 1:100. Bound IgG antibodies were visualized using a biotinylated monoclonal mouse anti-human IgG and the streptavidin-alkaline phosphatase system described in Materials and Methods. Reactive antigen bands unique to positive sera are identified with arrows. The positions of molecular mass markers (in thousands) are indicated on the left.

Jeffrey W. Priest, et al. Clin Vaccine Immunol. 2012 September;19(9):1539-1548.
5.
Fig 3

Fig 3. From: Multiplex Assay Detection of Immunoglobulin G Antibodies That Recognize Babesia microti Antigens.

The immunodominant membrane-associated antigen is found only in B. microti-infected red blood cells. Triton X-114-extracted proteins (3.5 μg/lane) from uninfected (U) and B. microti-infected (I) red blood cell membranes were resolved on an 8 to 16% polyacrylamide gel and transferred to PVDF. PVDF sections were incubated with either serum from a confirmed-babesiosis patient (Human Serum) or a mouse monoclonal antibody raised against rBmSA1 protein (mAb 3A6D). Bound IgG antibodies were visualized as described for Fig. 1. The positions of molecular mass markers (in thousands) are indicated on the left. Monoclonal antibody reactivity confirmed the identity of the immunodominant protein band in the parasitized red blood cell detergent extract as BMN1-9/BmSA1 (indicated by the arrow).

Jeffrey W. Priest, et al. Clin Vaccine Immunol. 2012 September;19(9):1539-1548.
6.
Fig 5

Fig 5. From: Multiplex Assay Detection of Immunoglobulin G Antibodies That Recognize Babesia microti Antigens.

MBA detection of IgG antibodies among presumed-negative cases and confirmed-babesiosis and malaria cases. MBA was conducted as described in Materials and Methods using beads coated with rBmSA1/GST (A) or rBm17N/GST (B). Bound IgG antibodies were detected using a biotinylated mouse monoclonal anti-human IgG and R-phycoerythrin-labeled streptavidin. Distributions for the presumed-negative sample set (Control; n = 82), B. microti-positive samples (n = 78), B. duncani- and B. divergens-positive samples (n = 25), P. ovale- and P. malariae-positive samples (n = 13), P. falciparum-positive samples (n = 33), and P. vivax-positive samples (n = 35) are presented. Boxes include values between the 25th and 75th percentiles, whiskers include values between the 10th and 90th percentiles, and outliers are indicated by data points. The median values are indicated within the boxes by a line. The respective cutoff values determined by ROC analysis for rBmSA1/GST (MFI−BG = 1,122) and rBm17N/GST (MFI−BG = 5,849) are indicated by horizontal lines in panel A and panel B, respectively.

Jeffrey W. Priest, et al. Clin Vaccine Immunol. 2012 September;19(9):1539-1548.

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