Breaking the Communication-Privacy-Accuracy Tradeoff with ff-Differential Privacy

We consider a federated data analytics problem in which a server coordinates the collaborative data analysis of multiple users with privacy concerns and limited communication capability. The commonly adopted compression schemes introduce information loss into local data while improving communication efficiency, and it remains an open problem whether such discrete-valued mechanisms provide any privacy protection. In this paper, we study the local differential privacy guarantees of discrete-valued mechanisms with finite output space through the lens of $f$-differential privacy (DP). More specifically, we advance the existing literature by deriving tight $f$-DP guarantees for a variety of discrete-valued mechanisms, including the binomial noise and the binomial mechanisms that are proposed for privacy preservation, and the sign-based methods that are proposed for data compression, in closed-form expressions. We further investigate the amplification in privacy by sparsification and propose a ternary stochastic compressor. By leveraging compression for privacy amplification, we improve the existing methods by removing the dependency of accuracy (in terms of mean square error) on communication cost in the popular use case of distributed mean estimation, therefore breaking the three-way tradeoff between privacy, communication, and accuracy. Finally, we discuss the Byzantine resilience of the proposed mechanism and its application in federated learning

Identification of a Novel NLRP12 Nonsense Mutation (Trp408X) in the Extremely Rare Disease FCAS by Exome Sequencing.

Familial cold autoinflammatory syndrome (FCAS) is an extremely rare autosomal dominant inherited disease. Although there are four genes that have been linked with FCAS, its molecular diagnosis has been challenging in a relatively large proportion of cases. In this study, we aimed to investigate the genetic defect of a recruited FCAS family using exome sequencing followed by in-depth bioinformatics analysis. As a result, a novel heterozygous stop-gain mutation (Trp408X) in NLRP12 was identified in autosomal dominant inherited FCAS with clinical features of recurrent fever and skin urticaria due to cold conditions. When combined with previous studies, all of the reported mutations were found to have occurred in a highly conserved region in the NACHT domain coding sequence in NLRP12 exon 3, suggesting that a screening strategy for FCAS should focus on this area of the gene. In conclusion, this study demonstrates the importance of exome sequencing for clinical diagnosis of genetic disorders and provides molecular insight into FCAS treatment and diagnosis

Anti-Inflammatory Effects of Monoammonium Glycyrrhizinate on Lipopolysaccharide-Induced Acute Lung Injury in Mice through Regulating Nuclear Factor-Kappa B Signaling Pathway

The present study aimed to investigate the therapeutic effect of monoammonium glycyrrhizinate (MAG) on lipopolysaccharide- (LPS-) induced acute lung injury (ALI) in mice and possible mechanism. Acute lung injury was induced in BALB/c mice by intratracheal instillation of LPS, and MAG was injected intraperitoneally 1 h prior to LPS administration. After ALI, the histopathology of lungs, lung wet/dry weight ratio, protein concentration, and inflammatory cells in the bronchoalveolar lavage fluid (BALF) were determined. The levels of tumor necrosis factor-α (TNF-α) and interleukin-1β (IL-1β) in the BALF were measured by ELISA. The activation of NF-κB p65 and IκB-α of lung homogenate was detected by Western blot. Pretreatment with MAG attenuated lung histopathological damage induced by LPS and decreased lung wet/dry weight ratio and the concentrations of protein in BALF. At the same time, MAG reduced the number of inflammatory cells in lung and inhibited the production of TNF-α and IL-1β in BALF. Furthermore, we demonstrated that MAG suppressed activation of NF-κB signaling pathway induced by LPS in lung. The results suggested that the therapeutic mechanism of MAG on ALI may be attributed to the inhibition of NF-κB signaling pathway. Monoammonium glycyrrhizinate may be a potential therapeutic reagent for ALI

Schematic Diagram of Mutations in the Encoded Proteins of <i>NLRP12/NLRP3/NLRC4/PLCG2</i> Genes Associated with FCAS.

<p>Rectangles with different colors indicate specific protein domains. The solid blue line indicates the position of the reported mutation, and the solid red line shows the p.Trp408* mutation related to our study.</p

Clinical Summary of the Individuals in this Study.

<p>M, Male; F, Female; +, Affected; -, Not affected.</p

Structural Difference between Wild-type and C-terminal Truncated <i>NLRP12</i> Proteins.

<p>Function predictions of the truncated protein and the wild-type (full-length) <i>NLRP12</i> were carried out. The truncated protein (p.Trp408X) is represented in green. The full length protein is represented in blue. It is clear that the mutation disrupts the integrity of the <i>NLRP12</i> protein.</p

A c.1223G>A Mutation in <i>NLRP12</i> Identified in an FCAS Family.

<p>(a) Flow diagram of the filtering analysis of the exome sequencing data. The data from the patients and controls were compared, and known SNPs and InDels were excluded as described in the Materials and Methods section. The causative mutation was identified after a comprehensive analysis. (b) The c.1223G>A mutation in patient III-5 compared to the control was confirmed by Sanger sequencing. The position is indicated by an arrow. (c) Sequence alignment of multiple species. The red line shows the position of the p.Trp408X mutation.</p