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Fig. 3 | Parasites & Vectors

Fig. 3

From: The N- and C-terminal carbohydrate recognition domains of Haemonchus contortus galectin bind to distinct receptors of goat PBMC and contribute differently to its immunomodulatory functions in host-parasite interactions

Fig. 3

Co-IP assays further indicate that MNh can bind to TMEM63A and MCh can bind to TMEM147. Lane Input (a, b, c, d): Cell lysates were precipitated with rat anti-TMEM63A-NO IgG, rat anti-MNh IgG, rat anti-TMEM147-O IgG and rat anti-MCh IgG, respectively. Lane IP (a, b, c, d): Cell lysates were precipitated with rat anti-MNh IgG, rat anti-TMEM63A-NO IgG, rat anti-MCh IgG and rat anti-TMEM147-O IgG, respectively. Lane IgG (a, b, c, d): Cell lysates were precipitated with normal rat IgG. IP: immunoprecipitation. Immunoblot analysis using rat anti-MNh IgG and rat anti-MCh IgG demonstrated that rMNh can bind to TMEM63A and rMCh can bind to TMEM147. Lane M: marker

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Parasites & Vectors

ISSN: 1756-3305

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