In this paper, we present an information-theoretic approach to obtain an estimate of the number of bits that can be hidden in still images, or, the capacity of the data-hiding channel.We show how the addition of the message signal or signature in a suitable transform domain rather than the spatial domain can significantly increase the channel capacity. Most of the state-of-the-art schemes developed thus far for data-hiding have embedded bits in some transform domain, as it has always been implicitly understood that a decomposition would help. Though most methods reported in the literature use DCT or wavelet decomposition for data embedding, the choice of the transform is not obvious.We compare the achievable data-hiding capacities for different decompositions like DCT, DFT, Hadamard, and subband transforms and show that the magnitude DFT decomposition performs best among the ones compared.
Understanding the growth of bacterial pathogens in a micronutrient restricted host environment can identify potential virulence proteins that help overcome this nutritional barrier to productive infection. In this study, we investigated the pneumococcal protein expression response to iron limitation using an in vitro model. We identified S. pneumoniae TIGR4 proteins by 2-D LC ESI MS/MS and determined significant changes in protein expression in response to iron restriction using computer-intensive random resampling methods. Differential protein expression was studied in the context of a S. pneumoniae TIGR4 protein interaction network using Pathway Studio. Our analysis showed that pneumococcal iron restriction response was marked by increased expression of known virulence factors like PsaA. It involved changes in the expression of stress response, and phase variation and biofilm formation proteins. The net effect of changes in all these biological processes could increase the virulence of S. pneumoniae TIGR4 during in vivo infection.
Subminimum inhibitory concentrations (sub-MICs) of antibiotics can be therapeutically effective, but the underlying molecular mechanisms are not well-characterized. We analyzed the Pasteurella multocida proteome response to sub-MICs of amoxicillin, chlortetracycline, and enrofloxacin using isotope-coded affinity tags (ICAT). There were parallel effects on inhibition of growth kinetics and suppression of protein expression by clusters of orthologous groups (COG) categories. Potential compensatory mechanisms enabling antibiotic adaptation were identified, including increased RecA expression caused by enrofloxacin.
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