Purification and characterization of a 58-kDa cell wall-associated protein from Listeria monocytogenes

Abstract

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.

Isolation and characterization of a Listeria monocytogenes mutant strain hyperproducing virulence factors

“…Western immunoblotting was performed by the method of Towbin et al [10]. Detection of listeriolysin O and cell wall protein Lm79/39 was performed with polyclonal rabbit antiserums raised against purified L. monocytogenes proteins [11, 12], phosphatidyl‐inositol‐specific phospholipase C (PI‐PLC) with an antiserum against purified recombinant hybrid protein Protein A::PI‐PLC [13], metalloprotease with an antiserum against purified 38 kDa metalloprotease of Legionella pneumophila [14]. Similar approach to detect metalloprotease with a serum against heterologous metalloproteinase (thermolysin) based on high degree of structural homology within the family of bacterial metalloproteinases has been reported [15].…”

Identification of a 25-kilodalton protein of Mycobacterium bovis BCG to distinguish BCG strains from Mycobacterium tuberculosis

“…BCG was grown in Sauton's broth at 37ЊC. The secretory, cytosolic, and Triton X-100-and SDS-soluble cell wall proteins were fractionated by sonication in the presence of 0.1 mM phenylmethylsulfonyl fluoride and by centrifugation (2). Proteins present in different fractions were measured and concentrated by lyophilization.…”