2. Academic Validation
  3. Deacetylation of K481 and K484 on Penaeid Shrimp Hemocyanin Is Critical for Antibacterial Activity

Deacetylation of K481 and K484 on Penaeid Shrimp Hemocyanin Is Critical for Antibacterial Activity

  • J Immunol. 2022 Jul 18;ji2200078. doi: 10.4049/jimmunol.2200078.
Junjie Nie 1 2,  Jude Juventus Aweya 1 3,  Zhixue Yu 1,  Hui Zhou 1,  Fan Wang 1 2,  Defu Yao 1 2,  Zhihong Zheng 1 2,  Shengkang Li 1 2 4,  Hongyu Ma 1 2,  Yueling Zhang 5 2 4
Affiliations

Affiliations

  • 1 Institute of Marine Sciences and Guangdong Provincial Key Laboratory of Marine Biotechnology, Shantou University, Shantou, China.
  • 2 Shantou University-Universiti Malaysia Terengganu Joint Shellfish Research Laboratory, Shantou University, Shantou, China.
  • 3 College of Ocean Food and Biological Engineering, Fujian Provincial Key Laboratory of Food Microbiology and Enzyme Engineering, Jimei University, Xiamen, Fujian, China.
  • 4 Southern Marine Science and Engineering Guangdong Laboratory, Guangzhou, China; and.
  • 5 Institute of Marine Sciences and Guangdong Provincial Key Laboratory of Marine Biotechnology, Shantou University, Shantou, China; zhangyl@stu.edu.cn.
PMID: 35851542 DOI: 10.4049/jimmunol.2200078
Abstract

Although invertebrates' innate immunity relies on several immune-like molecules, the diversity of these molecules and their immune response mechanisms are not well understood. Here, we show that Penaeus vannamei hemocyanin (PvHMC) undergoes specific deacetylation under Vibrio parahaemolyticus and LPS challenge. In vitro deacetylation of PvHMC increases its binding capacity with LPS and Antibacterial activity against Gram-negative bacteria. Lysine residues K481 and K484 on the Ig-like domain of PvHMC are the main acetylation sites modulated by the acetyltransferase TIP60 and deacetylase HDAC3. Deacetylation of PvHMC on K481 and K484 allows PvHMC to form a positively charged binding pocket that interacts directly with LPS, whereas acetylation abrogates the positive charge to decrease PvHMC-LPS attraction. Besides, V. parahaemolyticus and LPS challenge increases the expression of Pvhdac3 to induce PvHMC deacetylation. This work indicates that, during Bacterial infections, deacetylation of hemocyanin is crucial for binding with LPS to clear Gram-negative bacteria in crustaceans.

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