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Alpha-gal and cross-reactive carbohydrate determinants in the N-glycans of salivary glands in the lone star tick, Amblyomma americanum

(2020) VACCINES. 8(1).
Author
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Abstract
Ticks are important ectoparasites and vectors of numerous human and animal pathogens. Ticks secrete saliva that contains various bioactive materials to evade the host defense system, and often facilitates the pathogen transmission. In addition, the Lone star tick saliva is thought to be the sensitizer in red meat allergy that is characterized by an allergic reaction to glycan moieties carrying terminal galactose-alpha-1,3-galactose (aGal). To assess N-glycome of Amblyomma americanum, we examined the N-glycan structures in male and female salivary glands at three different feeding stages and in carcasses of partially fed lone star ticks. We also surveyed the genes involved in the N-glycosylation in the tick species. The aGal epitopes and cross-reactive carbohydrate determinants (CCD) increases over time after the onset of blood feeding in both male and female A. americanum. These CCDs include xylosylation of the core mannose, 1,3-mono and 1,3- and 1,6-difucosylations of the basal GlcNac and mono- or diantennary aGal. Combinations of both xylosylation and aGal and fucosylation and aGal were also found on the N-glycan structures. While the enzymes required for the early steps of the N-glycosylation pathway are quite conserved, the enzymes involved in the later stages of N-glycan maturation in the Golgi apparatus are highly diverged from those of insects. Most of all, we propose that the aGal serves as a molecular mimicry of bioactive proteins during tick feedings on mammalian hosts, while it contributes as a sensitizer of allergy in atypical host human.
Keywords
alpha-gal, red meat allergy, glygosylation, xylosylation, molecular mimicry, glycan, RED MEAT ALLERGY, MOLECULAR MIMICRY, BINDING PROTEINS, IGE, HOST, TRYPANOSOMA, ASSOCIATION, ANTIBODY, XENOTRANSPLANTATION, OLIGOSACCHARIDE

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Citation

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MLA
Park, Yoonseong, et al. “Alpha-Gal and Cross-Reactive Carbohydrate Determinants in the N-Glycans of Salivary Glands in the Lone Star Tick, Amblyomma Americanum.” VACCINES, vol. 8, no. 1, 2020, doi:10.3390/vaccines8010018.
APA
Park, Y., Kim, D., Boorgula, G. D., De Schutter, K., Smagghe, G., Simo, L., … Azadi, P. (2020). Alpha-gal and cross-reactive carbohydrate determinants in the N-glycans of salivary glands in the lone star tick, Amblyomma americanum. VACCINES, 8(1). https://doi.org/10.3390/vaccines8010018
Chicago author-date
Park, Yoonseong, Donghun Kim, Gunavanthi D. Boorgula, Kristof De Schutter, Guy Smagghe, Ladislav Simo, Stephanie A. Archer-Hartmann, and Parastoo Azadi. 2020. “Alpha-Gal and Cross-Reactive Carbohydrate Determinants in the N-Glycans of Salivary Glands in the Lone Star Tick, Amblyomma Americanum.” VACCINES 8 (1). https://doi.org/10.3390/vaccines8010018.
Chicago author-date (all authors)
Park, Yoonseong, Donghun Kim, Gunavanthi D. Boorgula, Kristof De Schutter, Guy Smagghe, Ladislav Simo, Stephanie A. Archer-Hartmann, and Parastoo Azadi. 2020. “Alpha-Gal and Cross-Reactive Carbohydrate Determinants in the N-Glycans of Salivary Glands in the Lone Star Tick, Amblyomma Americanum.” VACCINES 8 (1). doi:10.3390/vaccines8010018.
Vancouver
1.
Park Y, Kim D, Boorgula GD, De Schutter K, Smagghe G, Simo L, et al. Alpha-gal and cross-reactive carbohydrate determinants in the N-glycans of salivary glands in the lone star tick, Amblyomma americanum. VACCINES. 2020;8(1).
IEEE
[1]
Y. Park et al., “Alpha-gal and cross-reactive carbohydrate determinants in the N-glycans of salivary glands in the lone star tick, Amblyomma americanum,” VACCINES, vol. 8, no. 1, 2020.
@article{8667127,
  abstract     = {Ticks are important ectoparasites and vectors of numerous human and animal pathogens. Ticks secrete saliva that contains various bioactive materials to evade the host defense system, and often facilitates the pathogen transmission. In addition, the Lone star tick saliva is thought to be the sensitizer in red meat allergy that is characterized by an allergic reaction to glycan moieties carrying terminal galactose-alpha-1,3-galactose (aGal). To assess N-glycome of Amblyomma americanum, we examined the N-glycan structures in male and female salivary glands at three different feeding stages and in carcasses of partially fed lone star ticks. We also surveyed the genes involved in the N-glycosylation in the tick species. The aGal epitopes and cross-reactive carbohydrate determinants (CCD) increases over time after the onset of blood feeding in both male and female A. americanum. These CCDs include xylosylation of the core mannose, 1,3-mono and 1,3- and 1,6-difucosylations of the basal GlcNac and mono- or diantennary aGal. Combinations of both xylosylation and aGal and fucosylation and aGal were also found on the N-glycan structures. While the enzymes required for the early steps of the N-glycosylation pathway are quite conserved, the enzymes involved in the later stages of N-glycan maturation in the Golgi apparatus are highly diverged from those of insects. Most of all, we propose that the aGal serves as a molecular mimicry of bioactive proteins during tick feedings on mammalian hosts, while it contributes as a sensitizer of allergy in atypical host human.},
  articleno    = {18},
  author       = {Park, Yoonseong and Kim, Donghun and Boorgula, Gunavanthi D. and De Schutter, Kristof and Smagghe, Guy and Simo, Ladislav and Archer-Hartmann, Stephanie A. and Azadi, Parastoo},
  issn         = {2076-393X},
  journal      = {VACCINES},
  keywords     = {alpha-gal,red meat allergy,glygosylation,xylosylation,molecular mimicry,glycan,RED MEAT ALLERGY,MOLECULAR MIMICRY,BINDING PROTEINS,IGE,HOST,TRYPANOSOMA,ASSOCIATION,ANTIBODY,XENOTRANSPLANTATION,OLIGOSACCHARIDE},
  language     = {eng},
  number       = {1},
  pages        = {16},
  title        = {Alpha-gal and cross-reactive carbohydrate determinants in the N-glycans of salivary glands in the lone star tick, Amblyomma americanum},
  url          = {http://dx.doi.org/10.3390/vaccines8010018},
  volume       = {8},
  year         = {2020},
}

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