Unbiased, label-free proteomics is becoming a powerful technique for
measuring protein expression in almost any biological sample. The output of
these measurements after preprocessing is a collection of features and their
associated intensities for each sample. Subsets of features within the data are
from the same peptide, subsets of peptides are from the same protein, and
subsets of proteins are in the same biological pathways, therefore, there is
the potential for very complex and informative correlational structure inherent
in these data. Recent attempts to utilize this data often focus on the
identification of single features that are associated with a particular
phenotype that is relevant to the experiment. However, to date, there have been
no published approaches that directly model what we know to be multiple
different levels of correlation structure. Here we present a hierarchical
Bayesian model which is specifically designed to model such correlation
structure in unbiased, label-free proteomics. This model utilizes partial
identification information from peptide sequencing and database lookup as well
as the observed correlation in the data to appropriately compress features into
latent proteins and to estimate their correlation structure. We demonstrate the
effectiveness of the model using artificial/benchmark data and in the context
of a series of proteomics measurements of blood plasma from a collection of
volunteers who were infected with two different strains of viral influenza.Comment: Published in at http://dx.doi.org/10.1214/13-AOAS639 the Annals of
Applied Statistics (http://www.imstat.org/aoas/) by the Institute of
Mathematical Statistics (http://www.imstat.org
