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Bartonella henselae, an infectious agent causing cat-scratch disease and  vasculoproliferative disorders in humans, is a fastidious facultative  intracellular pathogen. The outer membrane proteins of B. henselae are  key molecules that play a primary role in host-cell interactions. We isolated B.  henselae outer membrane proteins, using the ionic detergent N-lauroyl  sarcosine sodium salt and sodium carbonate, purification by two-dimensional  (2-D) gel electrophoresis, and protein identification using mass spectrometry.  Treatment with buffers containing ASB-14 and ZWITTERGENT 3-10 increased  solubilization of B. henselae proteins, particularly proteins with  basic pI. Three hundred and sixty-eight spots were detected from the  sarcosine-insoluble outer membrane fraction; 94 distinct protein species were  identified from 176 spots. In the outer membrane fraction from carbonate  incubation, 471 spots were calculated and 259 spots were identified, which  included 139 protein entries. There were six outer membrane proteins in the  sarcosine-insoluble outer membrane fraction compared with nine outer membrane  proteins from samples subjected to carbonate incubation. We used bioinformatic  analysis to identify 44 outer membrane proteins by prediction of their domains  and tertiary structures and documented the potential virulence factors. We  established the 2-D reference maps of the outer membrane subproteome of B.  henselae using the two different extraction methods, which were partly  complementary to each other. Sodium carbonate extraction isolated low-abundance  and basic proteins better than the lauroyl sarcosine sodium salt extraction,  which enriched high-abundance porins.

Proteomic and bioinformatic analysis of outer membrane proteins of the protobacterium Bartonella henselae (Bartonellaceae)