Proteome analysis involves the simultaneous resolution and display of prote
ins produced by an organism, followed by the quantitation, characterisation
and identification of these proteins. As part of an ongoing study mapping
and comparing the proteins expressed by various strains of the pathogenic b
acterium Helicobacter pylori, we have resolved and identified 93 of the mos
t abundant proteins expressed by type reference strain NCTC 11637. Proteins
were separated by two-dimensional gel electrophoresis and stained with Coo
massie G250. Intensely-stained spots were excised and digested with trypsin
, and the resulting peptides were characterised by mass spectrometry. Prote
ins were then identified by correlating actual peptide profiles with theore
tical profiles generated from published nucleotide sequences. Ninety-three
of the most intensely-stained protein spots were identified as the products
of 35 genes, giving a ratio of 2.7 protein gene-products per gene. The pro
ducts of the tsaA, pfr, ureA and ureB genes were amongst several proteins p
resent in multiple isoforms. Peptide mass fingerprinting data were used to
identify probable post-translational protein modifications. These results s
uggest that H. pylori proteins are subject to a high degree of post-transla
tional modification. Comparative proteomics of H. pylori strains should gre
atly assist in investigating the pathogenic properties of this bacterium.