Aims: Glucosaminoglucan (β-1,4-linked glucose and glucosamine) produced by a mixotrophic sulfur-oxidizing bacterium, Thiothrix nivea, is a useful cellulose-aminating agent. Lithotrophic and mixotrophic glucosaminoglucan production were examined using fed-batch techniques.
Methods And Results: A jar fermenter was used for the fed-batch cultivation.
The viral infectivity factor (Vif) of human immunodeficiency virus 1 forms a complex with host proteins, designated as Vif-CBFβ-ELOB-ELOC-CUL5 (VβBCC), initiating the ubiquitination and subsequent proteasomal degradation of the human antiviral protein APOBEC3G (A3G), thereby negating its antiviral function. Whilst recent cryo-electron microscopy (cryo-EM) studies have implicated RNA molecules in the Vif-A3G interaction that leads to A3G ubiquitination, our findings indicated that the VβBCC complex can also directly impede A3G-mediated DNA deamination, bypassing the proteasomal degradation pathway. Employing the Systematic Evolution of Ligands by EXponential enrichment (SELEX) method, we have identified RNA aptamers with high affinity for the VβBCC complex.
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