Parasitic nematodes are important pathogens that infect animals, causing significant economic losses globally. Current repeated treatments have led to widespread anthelmintic resistance in nematode populations, so vaccine development offers an alternative control approach. However, only one effective vaccine (named Barbervax) has been developed to protect animals against one of the most pathogenic nematodes of ruminants—Haemonchus contortus (the barber’s pole worm). This vaccine contains a dominant component, Concanavalin A (Con A) purified H11 antigen, which has been shown to induce high levels (>85%) of immune protection in sheep breeds, but in goat breeds, the immunoprotection test of this native protein is still lacking. Here, we evaluated the protective efficacy of low-dose Con A-purified proteins for controlling the H. contortus infection in goats. Four-month-old Boer goats were equally divided into two vaccinated groups of 5 μg and 10 μg native proteins, and one adjuvant control. Each goat was immunized subcutaneously thrice and then challenged with 7000 infective third-stage larvae (L3s). The fecal egg count (FEC), degree of anemia, antibody levels of serum and abomasum mucosa, as well as worm burdens, were detected in experimental goats. Our results showed that both 5 μg and 10 μg vaccinated groups induced the effective protection in goats, reduced mean FEC by 71.8% and 68.6%, and mean worm burdens by 69.8% and 61.6%, respectively, compared to the adjuvant control. In addition, we detected that the serum antibody responses to the Con A-purified proteins were dominated by the IgG subtype, but the mucosal antibody responses were not detected. These data demonstrate Con A-purified proteins induced effective immunoprotection in goats, and underline their significance for controlling this widespread parasite.
SMAD proteins mediate TGF-β signaling and thereby regulate the metazoan development; however, they are poorly defined in Haemonchus contortus–a common blood-sucking parasitic nematode of small ruminants. Here, we characterized an R-SMAD family protein in H. contortus termed HcSMA2, which is closely related to Caenorhabditis elegans SMA2 (CeSMA2) involved in the bone morphogenetic protein (BMP) signaling. Hcsma2 is transcribed in all developmental stages of H. contortus but highly induced in the adult male worms. The RNA interference with Hcsma2 retarded the transition of infective L3 into L4 larvae. Besides, the bimolecular fluorescence complementation revealed the interaction of HcSMA2 with a TGF-β-activated-R-SMAD (HcDAF8). Together these results show a BMP-like receptor-regulated SMAD in H. contortus that is required for larval differentiation and underscore an adaptive functional repurposing of BMP-signaling in parasitic worms.
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