Genome-Wide Analysis of Oceanimonas sp. GK1 Isolated from Gavkhouni Wetland [Iran] demonstrates presence of genes for virulence and pathogenicity

Objective: The bacterium Oceanimonas sp. [O. sp.] GK1 is a member of the Aeromonadaceae family and its genome represents several virulence genes involved in fish and human pathogenicity. In this original research study we aimed to identify and characterize the putative virulence factors and pathogenicity of this halotolerant marine bacterium using genome wide analysis

Materials and Methods: The genome data of O. sp. GK1 was obtained from NCBI. Comparative genomic study was done using MetaCyc database

Results: Whole genome data analysis of the O. sp. GK1 revealed that the bacterium possesses some important virulence genes [e.g. ZOT, RTX toxin, thermostable hemolysin, lateral flagella and type IV pili] which have been implicated in adhesion and biofilm formation and infection in some other pathogenic bacteria

Conclusion: This is the first report of the putative pathogenicity of O. sp.GK1. The genome wide analysis of the bacterium demonstrates the presence of virulence genes causing infectious diseases in many warm- and cold-blooded animals

Cloning, expression and functional characterization of in-house prepared human basic fibroblast growth factor

Human basic fibroblast growth factor [bFGF] plays an important role in cellular proliferation, embryonic development, and angiogenesis as well as in several signaling pathways of various cell types. bFGF is an essential growth factor for the maintenance of undifferentiated human embryonic stem cells [hESCs] and human induced pluripotent stem cells [hiPSCs]. In this experimental study, we present a straightforward method to produce biologically active recombinant human bFGF protein in E. coli that has long-term storage ability. This procedure provides a rapid, cost effective purification of a soluble human bFGF protein that is biologically active and functional as measured in hESCs and hiPSCs in vitro and in vivo. The results show no significant difference in function between our in-house produced and commercialized bFGF

Cloning, expression, and functional characterization of in-house prepared human leukemia inhibitory factor

Leukemia inhibitory factor [LIF] plays important roles in cellular proliferation, growth promotion and differentiation of various types of target cells. In addition, LIF influences bone metabolism, cachexia, neural development, embryogenesis and inflammation. Human LIF [hLIF] is an essential growth factor for the maintenance of mouse embryonic stem cells [ESCs] and induced pluripotent stem cells [iPSCs] in a pluripotent, undifferentiated state. In this experimental study, we cloned hLIF into the pENTR-D/TOPO entry vector by a TOPO reaction. Next, hLIF was subcloned into the pDEST17 destination vector by the LR reaction, which resulted in the production of a construct that was transferred into E. coli strain Rosetta-gami[TM] 2[DE3] pLacI competent cells to produce the His6-hLIF fusion protein. This straightforward method produced a biologically active recombinant hLIF protein in E. coli that has long-term storage ability. This procedure has provided rapid, cost effective purification of a soluble hLIF protein that is biologically active and functional as measured in mouse ESCs and iPSCs in vitro. Our results showed no significant differences in function between laboratory produced and commercialized hLIF