Cyanobacterium Synechocystis sp. PCC 6803 lacking adc1 gene produces higher polyhydroxybutyrate accumulation under modified nutrients of acetate supplementation and nitrogen-phosphorus starvation.

Increased polyhydroxybutyrate production in cyanobacterium Synechocystis sp. PCC 6803 lacking adc1 gene (Δadc1) is first-timely reported in this study. We constructed the mutant by disrupting adc1 gene encoding arginine decarboxylase, thereby exhibiting a partial blockade of polyamine synthesis. This Δadc1 mutant had a proliferative growth and certain contents of intracellular pigments including chlorophyll a and carotenoids as similar as those of wild type (WT). Highest PHB production was certainly induced by BG11-N-P+A condition in both WT and Δadc1 mutant of about 24.9 %w/DCW at day 9 and 36.1 %w/DCW at day 7 of adaptation time, respectively. Abundant PHB granules were also visualized under both BG11-N-P and BG11-N-P+A conditions. All pha transcript amounts of Δadc1 mutant grown at 7 days-adaptation time were clearly upregulated corresponding to its PHB content under BG11-N-P+A condition. Our finding indicated that this adc1 perturbation is alternatively achieved for PHB production in Synechocystis sp. PCC 6803.

Monoclonal antibodies specific to human Δ42PD1: A novel immunoregulator potentially involved in HIV-1 and tumor pathogenesis.

We recently reported the identification of Δ42PD1, a novel alternatively spliced isoform of human PD1 that induces the production of pro-inflammatory cytokines from human peripheral blood mononuclear cells and enhances HIV-specific CD8(+) T cell immunity in mice when engineered in a fusion DNA vaccine. The detailed functional study of Δ42PD1, however, has been hampered due to the lack of a specific monoclonal antibody (mAb). In this study, we generated 2 high-affinity mAbs, clones CH34 (IgG2b) and CH101 (IgG1), from Δ42PD1-immunized mice. They recognize distinct domains of Δ42PD1 as determined by a yeast surface-displaying assay and ELISA. Moreover, they recognize native Δ42PD1 specifically, but not PD1, on cell surfaces by both flow cytometry and immunohistochemical assays. Δ42PD1 appeared to be expressed constitutively on healthy human CD14(+) monocytes, but its level of expression was down-regulated significantly during chronic HIV-1 infection. Since the level of Δ42PD1 expression on CD14(+) monocytes was negatively correlated with the CD4 count of untreated patients in a cross-sectional study, Δ42PD1 may play a role in HIV-1 pathogenesis. Lastly, when examining Δ42PD1 expression in human esophageal squamous-cell carcinoma tissues, we found high-level expression of Δ42PD1 on a subset of tumor-infiltrating T cells. Our study, therefore, resulted in 2 Δ42PD1-specific mAbs that can be used to further investigate Δ42PD1, a novel immune regulatory protein implicated in HIV-1 and tumor pathogenesis as well as other immune diseases.