The autolysin Ami contributes to the adhesion of Listeria monocytogenes to eukaryotic cells via its cell wall anchor

A Phosphorylated Cytoplasmic Autoantigen, GW182, Associates with a Unique Population of Human mRNAs within Novel Cytoplasmic Speckles

“…Deletion of this domain impaired adherence to host cells, whereas addition of GW repeats improved the binding to the cell surface. Similarly, the autolysin Ami in L. monocytogenes contains a N-terminal catalytic domain and a Cterminal domain that is homologous to the GW domain in InIB but contains 8 GW modules arranged in tandem (Braun et al, 1997;Milohanic et al, 2001). Similar six to eight tandem repeat motifs have been described in the S. caprae atlC gene product (Alligent et al, 2001) and the surface protective antigen (SpaA) of E. rhusiopathiae (Makino et al, 1998).…”

“…Although ESTs that contain this motif are in the database, to date no other mammalian proteins with this motif have been reported. A clue to the function of GW repeats may come from studies of bacteria such as Listeria monocytogenes, Staphylococcus caprae, and Erysipelothrix rhusiopathiae, where it has been suggested that proteins bearing these repeats play an important role in anchoring bacterial proteins to the surface of the cell (Makino et al, 1998) and anchoring bacteria to target cells (Braun et al, 1997;Milohanic et al, 2001). The mode of binding is not clearly understood, but is thought to occur via interaction with lipoteichoic acid or with specific cell surface proteins.…”

The arsenal of virulence factors deployed byListeria monocytogenesto promote its cell infection cycle

“…[35][36][37] The CWA domain of Ami has been shown to mediate bacterial adhesion to human epithelial cells. 38,39 In addition, an ami mutant is attenuated in the liver of intravenously infected mice, suggesting a role in L. monocytogenes virulence. 40 dltA is part of a L. monocytogenes operon made up of four genes (dltA, dltB, dltC and dltD) and is implicated in the integration of D-alanine residues into LTAs.…”

Acd, a peptidoglycan hydrolase of Clostridium difficile with N-acetylglucosaminidase activity

“…Like most of the previously described bacterial PGHs (Heilmann et al, 1997;Hell et al, 1998;Milohanic et al, 2001;Oshida et al, 1995), Acd has a modular structure with two main domains. The first 22 aa of the N-terminal domain of the deduced Acd sequence might constitute a putative signal peptide, or a retention signal with a transmembrane domain as described for a few proteins like cell-wall hydrolases in B. subtilis (Tjalsma et al, 2004).…”

“…These repeated sequences contain four putative GW modules, which constitute another motif for cell-surface anchoring. GW modules might interact with cell-wall polymers such as teichoic or lipoteichoic acids and are present in many surface proteins produced by Gram-positive bacteria, including L. monocytogenes InlB and Ami (Braun et al, 1997;Cabanes et al, 2002;Milohanic et al, 2001) and the four staphylococcal surface autolysins, S. aureus Atl (Oshida et al, 1995), S. caprae AtlC (Allignet et al, 2001), S. epidermidis AtlE (Heilmann et al, 1997) and S. saprophyticus Aas (Hell et al, 1998).…”