Tyrosine sulfation is an important post-translational modification in anti-inflammatory peptides from blood-feeding organisms. — ASN Events
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  3. Tyrosine sulfation is an important post-translational modification in anti-inflammatory peptides from blood-feeding organisms.

Tyrosine sulfation is an important post-translational modification in anti-inflammatory peptides from blood-feeding organisms. (#177)

Joshua W Maxwell 1 , Anneliese S Ashhurst 2 , Scott N Byrne 2 , Richard J Payne 1
  1. School of Chemistry, University of Sydney, Sydney, New South Wales, Australia
  2. Infectious Diseases and Immunology, Faculty of Medicine and Health, Sydney, NSW, Australia

Haematophagous organisms represent one of the largest vectors of human diseases of the animal kingdom. Their saliva contains a cocktail of proteins and peptides to suppress the human immune system to prolong their feeding time and harvest more blood.1 Compromising the immune system at the site of the bite provides the optimal conditions for establishing an infection of an opportunistic blood-borne pathogen. Tyrosine sulfation has been demonstrated to be a vital PTM on many anti-coagulant salivary proteins of haematophagous organisms.2-5 However, there has been limited exploration on the prevalence and effect of tyrosine sulfation on immunomodulatory peptides. This work has focused on the synthesis of a library of immunomodulatory peptides from blood-feeding organisms to explore the effect of tyrosine sulfation on their activity.

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  3. Hsieh, Y. S.; Wijeyewickrema, L. C.; Wilkinson, B. L.; Pike, R. N.; Payne, R. J. Angewandte Chemie International Edition 2014, 53, 3947-3951.
  4. Watson, E. E. et al. Mosquito derived Anophelin sulfoproteins are potent antithrombotics. ACS central science, 4, 468-476 (2018).
  5. Watson, E. E. et al. Rapid assembly and profiling of an anticoagulant sulfoprotein library. Proceedings of the National Academy of Sciences, (DOI:10.1073/pnas.1905177116).