Diagnostic anti-Brachyspira hyodysenteriae Bhlp29.7 antibodies pairs and antigen for animal health (animal Swine/Porcine/Pig infectious disease Swine Dysentery/brachyspira infection) testing in ELISA, colloidal gold-based Lateral flow immunoassay (LFIA), CLIA, TINIA and POCT

Genemedi produces core animal health diagnostic ingredients-validated anti-Brachyspira hyodysenteriae Bhlp29.7 antibodies pairs and antigens for rapid test kit of animal Swine/Porcine/Pig infectious disease with Swine Dysentery/brachyspira infection to evaluate the  animal health of Swine/Porcine/Pig. The paired antibodies are both monoclonal antibody (mab). All the antibodies and antiges of animal disease test are suitable for in ELISA, colloidal gold-based Lateral flow immunoassay (LFIA), CLIA, TINIA and POCT. The antibody can act as a capture antibody and detection antibody. Antigens are validated as positive control materials. Swine Dysentery (SD) is a severe mucohaemorhagic enteric disease of pigs caused by Brachyspira hyodysenteriae, which has a large impact on pig production and causes important losses due to mortality and sub-optimal performance. Brachyspira hyodysenteriae is commonly associated with swine dysentery (SD), a disease that has an economic impact on the swine industry. B. hyodysenteriae infection results in changes to the colonic mucus niche with massive mucus induction, which substantially increases the number of B. hyodysenteriae binding sites in the mucus. We previously determined that a B. hyodysenteriae strain binds to colon mucins in a manner that differs between pigs and mucin types. Here, we investigated if adhesion to mucins is a trait observed across a broad set of B. hyodysenteriae strains and isolates and furthermore at a genus level (B. innocens, B. pilosicoli, B. murdochii, B. hampsonii, and B. intermedia strains). Our results show that binding to mucins appears to be specific to B. hyodysenteriae, and within this species, the binding ability to mucins varies between strains/isolates, increases for mucins from pigs with SD, and is associated with sialic acid epitopes on mucins. Infection with B. hyodysenteriae strain 8dII results in mucin glycosylation changes in the colon, including a shift in sialic acid-containing structures. Thus, we demonstrate through hierarchical cluster analysis and orthogonal projections to latent structures discriminant analysis (OPLS-DA) models of the relative abundances of sialic acid-containing glycans that sialic acid-containing structures in the mucin O-glycome are good predictors of B. hyodysenteriae strain 8dII infection in pigs. The results emphasize the role of sialic acids in governing B. hyodysenteriae interactions with its host, which may open perspectives for therapeutic strategies.