A cell wall protein (P58) was purified from Listeria monocytogenes by detergent extraction and Superose 6 gel chromatography. It had a molecular mass of 58 kDa, was strongly hydrophobic, contained reactive thiol group(s) and was located at least partially on the surface of bacterial cells. Production of this protein varied among different Listeria, being the most prominent in NCTC 7973 of L. monocytogenes, weaker in four other strains of this species and undetectable in tested strains of L. seeligeri and L. innocua. Mice that survived experimental listerial infection produced antibodies against P58. This fact allowed us to speculate that the described protein can be used as a marker for sero-diagnosing of listeriosis.
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