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Figure 4 | Journal of Biomedical Science

Figure 4

From: EEVD motif of heat shock cognate protein 70 contributes to bacterial uptake by trophoblast giant cells

Figure 4

Binding of TPR proteins to Hsc70. (A) TPR proteins binding capacity for Hsc70 with or without EEVD or scrambled EEVD (sEEVD: CAPISEDGSGETV) peptides as measured by ELISA. Immunoplates were coated with TPR-Ba, TPR-Lm1, TPR-Lm2 proteins or BSA (Cont.) and then Hsc70 was added. Data are the averages of triplicate samples from three identical experiments, and the error bars represent standard deviations. Statistically significant differences between control and TPR proteins are indicated by asterisks (*, P < 0.01). (B) Interaction between TPR proteins and Hsc70 interferes with bacterial uptake by TG cells. Recombinant TPR proteins or BSA (Control) were added in the culture medium of TG cells at the indicated concentration and then bacteria were deposited onto TG cells. Data are the averages of triplicate samples from three identical experiments, and the error bars represent standard deviations. Statistically significant differences between control and TPR proteins are indicated by asterisks (*, P < 0.01). (C) B. abortus and L. monocytogenes binding capacity for Hsc70 with or without TPR proteins as measured by ELISA. Bacteria or BSA were coated on immunoplates and then TPR-Ba, TPR-Lm1, TPR-Lm2 proteins or BSA (Cont.) was added. After that, Hsc70 was added. Bacterial binding to Hsc70 were inhibited by addition of TPR proteins. Data are the averages of triplicate samples from three identical experiments, and the error bars represent standard deviations. Statistically significant differences between control and TPR proteins are indicated by asterisks (*, P < 0.01).

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