SmcL, a novel membrane-damaging virulence factor in Listeria

International Journal of Medical Microbiology

Volumn 290, Issue 4-5, 2000, Pages 369-374

  Gonzalez Zorn B ^a   Dominguez Bernal, G ^a   Suarez, M ^a   Ripio, M T ^a   Vega, Y ^a   Novella, S ^a   Rodriguez A ^a   Chico, I ^a   Tierrez, A ^a   Vazquez Boland J A ^a  

^a UNIVERSIDAD COMPLUTENSE DE MADRID   (Spain)

Author keywords

Bacterial phospholipases; CAMP reaction; LIPI 1; LIPI 2; Listeria ivanovii; Listeria virulence; Membrane damaging toxins; Pathogenicity islands; Phagosomal escape; SmcL; Sphingomyelinase C

Indexed keywords

LISTERIA; LISTERIA IVANOVII; RHODOCOCCUS EQUI;

EID: 0033744122     PISSN: 14384221     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1438-4221(00)80044-2     Document Type: Article

References (16)

1. A new PrfA-regulated gene of Listeria monocytogenes encoding a small, secreted protein which belongs to the family of internalins
2. Sequence comparison of the chromosomal regions encompassing the internalin C genes (inlC) of Listeria monocytogenes and Listeria ivanovii
3. A novel PrfA-regulated chromosomal locus, which is specific for Listeria ivanovii, encodes two small, secreted internalins and contributes to virulence in mice
4. Cooperative membrane-active (lytic) processes
5. The smcL gene of Listeria ivanovii encodes a sphingomyelinase C that mediates bacterial escape from the phagocytic vacuole
6. Listeria ivanovii is capable of cell-to-cell spread involving actin polymerization
7. The actin-polymerisation protein from Listeria ivanovii is a large protein which shows only limited amino acid sequence homology to ActA from Listeria monocytogenes
8. Virulence gene clusters and putative pathogenicity islands in Listeria
9. The broad-range phospholipase C and a metalloprotease mediate listeriolysin O-independent escape of Listeria monocytogenes from a primary vacuole in human epithelial cells
10. Lipid composition of erythrocytes in various mammalian species
11. Cellular biology of Listeria monocytogenes infection
12. The sulphydryl-activated cytolysin and a sphingomyelinase C are the major membrane-damaging factors involved in cooperative (CAMP-like) haemolysis of Listeria spp
13. The two distinct phospholipases C of Listeria monocytogenes have overlapping roles in escape from a vacuole and cell-to-cell spread
14. Bacterial phospholipases C
15. Purification and characterization of two Listeria ivanovii cytolysins, a sphingomyelinase C and a thiol-activated toxin (ivanolysin O)
16. Nucleotide sequence of the lecithinase operon of Listeria monocytogenes and possible role of lecithinase in cell-to-cell spread