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The role of F1 ATP synthase beta subunit in WSSV infection in the shrimp, Litopenaeus vannamei.

ABSTRACT: BACKGROUND: Knowledge of the virus-host cell interaction could inform us of the molecular pathways exploited by the virus. Studies on viral attachment proteins (VAPs) and candidate receptor proteins involved in WSSV infection, allow a better understanding of how these proteins interact in the viral life cycle. In this study, our aim was to find some host cellular membrane proteins that could bind with white spot syndrome virus (WSSV). RESULTS: Two proteins were evident by using a virus overlay protein binding assay (VOPBA) with WSSV. A protein with molecular weight 53 kDa, named BP53, was analyzed in this study, which was homologous with the F1-ATP synthase beta subunit by mass spectrometry analysis. Rapid amplification of cDNA ends (RACE) PCR was performed to identify the full-length cDNA of the bp53 gene. The resulting full-length gene consisted of 1836 bp, encoding 525 amino acids with a calculated molecular mass of 55.98 kDa. The deduced amino acid sequence contained three conserved domains of the F1-ATP synthase beta subunit. BP53 was therefore designated the F1-ATP synthase beta subunit of L. vannamei. The binding of WSSV to BP53 were also confirmed by competitive ELISA binding assay and co-immunoprecipitation on magnetic beads. To investigate the function of BP53 in WSSV infection, it was mixed with WSSV before the mixture was injected intramuscularly into shrimp. The resulting mortality curves showed that recombinant (r) BP53 could attenuate WSSV infection. CONCLUSIONS: The results revealed that BP53 is involved in WSSV infection. Here is the first time showed the role of shrimp F1-ATP synthase beta subunit in WSSV infection.

SUBMITTER: Liang Y

PROVIDER: S-EPMC2906456 | biostudies-literature | 2010

REPOSITORIES: biostudies-literature

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The role of F1 ATP synthase beta subunit in WSSV infection in the shrimp, Litopenaeus vannamei.

Liang Yan Y Cheng Jun-Jun JJ Yang Bing B Huang Jie J

Virology journal 20100630

<h4>Background</h4>Knowledge of the virus-host cell interaction could inform us of the molecular pathways exploited by the virus. Studies on viral attachment proteins (VAPs) and candidate receptor proteins involved in WSSV infection, allow a better understanding of how these proteins interact in the viral life cycle. In this study, our aim was to find some host cellular membrane proteins that could bind with white spot syndrome virus (WSSV).<h4>Results</h4>Two proteins were evident by using a vi ...[more]

PMID: 20591132

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Project description:The functional diversity of crustacean hemocyanins is broad, encompassing O2 delivery, innate immune response, metabolite storage, and osmolyte balance, all in a heterogeneous protein structure. As such, the sequence diversity of this class of proteins and its subunit composition are the focus of many studies on crustacean adaptation to environmental challenges. Recent transcriptomic and genomic sequencing on the Pacific whiteleg shrimp Litopenaeus vannamei has identified unique isoforms of hemocyanin including an ancestral β-type subunit thought to be lost in penaeid shrimp. However, it is unknown the degree to which these isoforms are translated as proteins, and whether they differ in function. The present study uses proteomic approaches to characterize the protein-level abundance and organization of these hemocyanin isoforms within their native oligomeric structures. Fractions of each hemocyanin oligomeric form were purified by size-exclusion high performance liquid chromatography for identification of subunit isoforms using tandem mass spectrometry at <1% protein false discovery rate. Relative abundances of hemocyanin oligomers and monomeric subunits from hemolymph and fractions were also quantified by polyacrylamide gel electrophoresis with and without denaturation for comparison of relative abundance. Ten hemocyanin isoforms were identified by tandem mass spectrometry in both hemocyanin oligomer fractions including a single small subunit, eight large subunits, and the first protein-level evidence of a β-type subunit in penaeid shrimp. Hemocyanin subunits were organized primarily as hexamers (95-99% relative abundance) as opposed to dodecamers. Hexamers utilized a significantly higher ratio (2.05:1) of small subunit to large subunit compared to dodecamers (1.04:1), and the relative abundances of the large subunit isoforms was dominated by HcL1 in both fractions. The ability to distinguish and quantify hemocyanin isoforms within oligomeric structures will aid future studies linking hemocyanin genes to function and physiology as well as offer insight into the evolutionary history of crustaceans.

Dataset Information

The role of F1 ATP synthase beta subunit in WSSV infection in the shrimp, Litopenaeus vannamei.

Publications

The role of F1 ATP synthase beta subunit in WSSV infection in the shrimp, Litopenaeus vannamei.

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