The monitoring of gene expression via the technologies encompassed under th
e term 'proteomics' allows proteins of significance to be related to phenot
ypes associated with strain variability, environmental influences and the e
ffects of genetic manipulation. The characterisations of these molecules ar
e routinely performed utilising two-dimensional (2-D) gel electrophoresis i
n association with mass spectrometry for the identification of proteins. Pa
thogenic bacteria are suitable for proteomic comparisons in the aim of eluc
idating proteins with vaccine and diagnostic applications, as well as deter
mining novel targets for drug design and the effects of these drugs on cell
ular physiology. Strains exhibiting diverse phenotypes including antibiotic
or chemical resistances, altered mode of pathogencity, or differential cap
ability of growth in similar environments, can be compared via protein diff
erential display to correlate relative protein abundances associated with t
hese conditions. Technically, proteins are 'mapped' on 2-D arrays under 'st
andard' conditions and visually compared to arrays of proteins from a varie
ty of test conditions. High-throughput technologies allow molecules of sign
ificance to be elucidated rapidly from within complex mixtures using a comb
ination of cellular pre fractionation to determine cellular location and pa
thway predictions to aid in overcoming the limitations of 2-D gel technolog
y for the analysis of whole proteomes.