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• W2022175879 abstract "To The Editor Recent review articles have presented advances and strategies for tick vaccine discovery(1–5). However, the importance of sugar epitopes as tick vaccine antigens, briefly discussed by Nuttall et al. (1) and Willadsen (3), has been little investigated and largely overlooked. Recent studies of tick–pathogen interactions suggest that the glycan–protein conjugates are involved in pathogen infection of tick cells (6). Although sugar epitopes have been recognized as potential immunogens for pathogen transmission-blocking vaccines (6,7), their role in tick vaccine development and performance is poorly understood. The first preliminary evidence that sugar epitopes may be involved in protective immunity against ticks was provided by Lee et al. (8) using Boophilus microplus midgut membrane antigens treated with periodate. Recent experiments provide additional evidence that the glycosylated proteins may be useful as tick vaccine antigens. The only commercially available tick vaccines contain recombinant Bm86 and Bm95 proteins (1–5). Bm86 is a glycoprotein expressed by midgut cells of B. microplus (9). Recombinant Bm86 and Bm95 proteins, when expressed in Pichia pastoris and insect cells, are also glycosylated (10–12). In a series of experiments, Tellam et al. (10) demonstrated that vaccine preparations containing the baculovirus-expressed Bm86 have higher efficacy for the control of tick infestations than those made from Escherichia coli-expressed antigens. In addition, glycosylated recombinant Bm86 preparations purified from P. pastoris were found to be more immunogenic that non-glycosylated ones (unpublished results). These differences could have resulted because antigen produced in eukaryotic systems more closely resembles the properties of the native tick protein, one of which may be the glycosylation. The antigen BMA7 is a 63 kDa mucin-like glycoprotein that was isolated from B. microplus (13). Although the protective epitopes were never characterized, immunization experiments with native BMA7 resulted in partial immunity against tick infestations and suggested that both polypeptide and oligosaccharide were antigenic (13). Willadsen and McKenna (14) presented a series of results demonstrating the production of antibodies against sugar epitopes on tick glycoproteins in cattle exposed to ticks. They provided evidence that the reaction of bovine antibodies with tick glycoproteins is at least partially blocked by low molecular weight carbohydrates and that antibodies directed against carbohydrate determinants of Bm86 are not protective. Their interpretation of these results is that the reaction of concealed antigens such as Bm86 with antibodies produced as a result of tick infestation appears to be due to a relatively non-specific reaction with carbohydrate determinants on tick glycoprotein. However, these results do not contradict the enhancing effect of sugar moieties on the protective properties of glycosylated Bm86 discussed above. Collectively, these results suggest that sugar moieties on tick proteins may be important for enhancing the protective capacity of tick vaccine antigen preparations. Tick sugar epitopes, which may contribute to control of tick infestations and the prevention of transmission of tick-borne pathogens, should be further investigated. One way to approach this problem is through the identification and characterization of tick receptor(s) and pathogen ligand(s). For example, the results on the characterization of Anaplasma marginale MSP1a adhesin support the role of carbohydrates in the infection of tick cells (15), and encourage the identification of tick receptor(s) to test the role of sugar moieties in tick–pathogen interactions and protection against tick infestations and the transmission of tick-borne pathogens." @default.
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• W2022175879 date "2006-07-06" @default.
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• W2022175879 title "The importance of protein glycosylation in development of novel tick vaccine strategies" @default.
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• W2022175879 doi "https://doi.org/10.1111/j.1365-3024.2006.00902.x" @default.
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