Isolation and characterization of two Campylobacter glycine-extracted proteins that bind to HeLa cell membranes

Abstract

Two immunogenic proteins of 27 (CBF1) and 29 (CBF2) kDa from enteropathogenic Campylobacter species appear to bind to mammalian cells. We purified these two proteins from a pathogenic and adherent Campylobacter jejuni strain to homogeneity by using acid extraction, preparative gel electrophoresis, and electroelution. Polyclonal rabbit antisera to these proteins were prepared. Immunologic studies indicate that

The Campylobacter jejuni PEB1a adhesin is an aspartate/glutamate‐binding protein of an ABC transporter essential for microaerobic growth on dicarboxylic amino acids

“…In addition to a periplasmic location, some PEB1a must be exposed on the cell surface in order for the protein to act as an adhesin. Previous evidence for this has been obtained from immunogold labelling studies (Kervella et al, 1993) and the fact the protein was originally isolated from acidic glycine extracts (a treatment thought to preferentially release surface proteins; Pei et al, 1991;Kervella et al, 1993). However, the presence of a signal peptidase II recognition site (predicted by LipoP v1.0 at the sequence 13-FALGA//CVAFS with a log-odds score of 2.6) may result in the protein being anchored in the inner or outer membrane via acylation of Cys18.…”

Relaxation of DNA supercoiling leads to increased invasion of epithelial cells and protein secretion by Campylobacter jejuni

“…A number of C. jejuni virulence factors have been shown to contribute to C. jejuni adhesion and invasion in-vitro ( O Cr oin ın and Backert, 2012). It is clear that production of Peb1 and Peb4 are important for the ability of C. jejuni to adhere to the epithelial cell boundary but their influence on C. jejuni adhesion/invasion appears to be indirect (Pei et al, 1991;Kervella et al, 1993;Burucoa et al, 1995;Pei et al, 1998;Kale et al, 2011). JlpA is a 42 kDa C. jejuni specific adhesin, which is surface exposed.…”

Identification of a fibronectin‐binding domain within the Campylobacter jejuni CadF protein

“…The ability of C. jejuni to colonize the intestinal tract of humans is proposed to play an early role in the development of C. jejunimediated enteritis. C. jejuni must overcome the forces of peristaltic motion and fluid flow to colonize and invade the cells lining the intestinal lumen (McSweegan and Walker, 1986;Fauchère et al , 1989;de Melo and Pechère, 1990;Moser et al , 1992;1997;Kervella et al , 1993;Pei and Blaser, 1993;Moser and Schröder, 1995;Konkel et al , 1997;Schröder and Moser, 1997;Kelle et al , 1998;Pei et al , 1998;Jin et al , 2001). Colonization is thought to be dependent on numerous properties inherent to the bacterium, including the organism's motility, chemotactic behaviour and an assortment of adhesins.…”