Molecular characterization, expression, and function of Vitellogenin genes in Phytoseiulus persimilis.

Vitellogenin (Vg) is an important factor that impacts oocyte maturation, egg formation and embryonic development in Arthropoda. Two orthologs of Vg gene were obtained from the genome of Phytoseiulus persimilis and termed as PpVg1 and PpVg2. Both orthologs belong to the large lipid transfer protein superfamily. The expression of PpVg1 and PpVg2 was low in immatures and male adults, and increased rapidly in female adults after mating, and reached a peak before the first egg was laid (168×  and 20.5×  the level in virgin females, respectively). When PpVg1 and PpVg2 were interfered with dsRNA, the relative expression decreased by 81.0 and 30.9%, respectively, and 7.8 and 31.4% interfered individuals died within 24 h. Among surviving individuals, ca. 51.1 and 44.8% are infertile. Factors that might be related to expression of Vg genes are also discussed.

The first description of complete invertebrate arginine metabolism pathways implies dose-dependent pathogen regulation in Apostichopus japonicus.

In this study, three typical members representative of different arginine metabolic pathways were firstly identified from Apostichopus japonicus, including nitric oxide synthase (NOS), arginase, and agmatinase. Spatial expression analysis revealed that the AjNOS transcript presented negative expression patterns relative to those of Ajarginase or Ajagmatinase in most detected tissues. Furthermore, Vibrio splendidus-challenged coelomocytes and intestine, and LPS-exposed primary coelomocytes could significantly induce AjNOS expression, followed by obviously inhibited Arginase and AjAgmatinase transcripts at the most detected time points. Silencing the three members with two specific siRNAs in vivo and in vitro collectively indicated that AjNOS not only compete with Ajarginase but also with Ajagmatinase in arginine metabolism. Interestingly, Ajarginase and Ajagmatinase displayed cooperative expression profiles in arginine utilization. More importantly, live pathogens of V. splendidus and Vibrio parahaemolyticus co-incubated with primary cells also induced NO production and suppressed arginase activity in a time-dependent at an appropriate multiplicity of infection (MOI) of 10, without non-pathogen Escherichia coli. When increasing the pathogen dose (MOI = 100), arginase activity was significantly elevated, and NO production was depressed, with a larger magnitude in V. splendidus co-incubation. The present study expands our understanding of the connection between arginine's metabolic and immune responses in non-model invertebrates.