Screening of proteins interacting with vhvp-2 protein from Vibrio parahaemolyticus causing translucent post-larvae disease in Pacific white shrimp Litopenaeus vannamei
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Assays for Studying the Role of Vitronectin in Bacterial Adhesion and Serum Resistance
Published on: October 16, 2018
Na An1, Li Jiang1, Yilin Wang1
1MOE Key Laboratory of Marine Genetics and Breeding, College of Marine Life Science, Ocean University of China, Qingdao 266003, China; Hainan Key Laboratory of Tropical Aquatic Germplasm, Sanya Oceanographic Institution, Ocean University of China, Sanya 572024, China.
Abstract:
Litopenaeus vannamei, as one of the core species in global aquaculture, holds a pivotal position in the marine aquaculture industry in terms of industrial scale and economic value. However, the shrimp aquaculture has long been plagued by diseases and infections. A variety of highly contagious and lethal pathogens frequently trigger disease outbreaks, causing devastating economic losses. Translucent Post-larvae Disease (TPD) is a major disease threatening the shrimp aquaculture industry in recent years. This disease is caused by a certain strain of Vibrio parahaemolyticus (VpTPD) harboring three virulence genes vhvp-1, vhvp-2 and vhvp-3, among which vhvp-2 is the key virulence factor. In this study, yeast two-hybrid (Y2H) technology was used to screen for proteins interacting with vhvp-2 protein from L. vannamei. Gene Ontology (GO) and Kyoto Encyclopedia of Genes and Genomes (KEGG) enrichment analyses revealed that these interacting proteins are involved in multiple biological processes, including immune response, disease, cell growth and apoptosis, transport, catabolism, and signal transduction. Ten potential interacting proteins were selected for pairwise validation, and the results confirmed that all of them interact with vhvp-2 protein. Notably, laminin receptor, 40S ribosomal protein SA-like, mitochondrial ATPase inhibitor factor 1 precursor, actin 2, and phosphopyruvate hydratase are associated with immune regulation. In summary, these interacting proteins provide important references for analyzing TPD-host interactions and revealing the molecular mechanisms underlying infection regulation.
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