Sufficient for Invasion of Host Cells Fibronectin-Binding Proteins Are aureus Staphylococcus Heterologously Expressed

[1]  F. Lowy.  Staphylococcus aureus infections. , 2009, The New England journal of medicine.

[2]  S. Johansson,et al.  Cellular invasion by Staphylococcus aureus involves a fibronectin bridge between the bacterial fibronectin-binding MSCRAMMs and host cell beta1 integrins. , 2000, European journal of cell biology.

[3]  P. Francioli,et al.  Expression of Staphylococcus aureusClumping Factor A in Lactococcus lactis subsp.cremoris Using a New Shuttle Vector , 2000, Infection and Immunity.

[4]  K. Preissner,et al.  Vitronectin Interaction with Glycosaminoglycans , 1999, The Journal of Biological Chemistry.

[5]  J. Content,et al.  Listeria monocytogenes Possesses Adhesins for Fibronectin , 1999, Infection and Immunity.

[6]  T. Foster,et al.  Bacterial fibronectin-binding proteins and endothelial cell surface fibronectin mediate adherence of Staphylococcus aureus to resting human endothelial cells. , 1999, Microbiology.

[7]  P. Nuijten,et al.  The fibronectin binding proteins of Staphylococcus aureus are required for adhesion to and invasion of bovine mammary gland cells. , 1999, FEMS microbiology letters.

[8]  K. Dziewanowska,et al.  Fibronectin Binding Protein and Host Cell Tyrosine Kinase Are Required for Internalization of Staphylococcus aureus by Epithelial Cells , 1999, Infection and Immunity.

[9]  Bhanu Sinha,et al.  Fibronectin‐binding protein acts as Staphylococcus aureus invasin via fibronectin bridging to integrin α5β1 , 1999, Cellular microbiology.

[10]  B. Kreikemeyer,et al.  Role of fibronectin-binding MSCRAMMs in bacterial adherence and entry into mammalian cells. , 1999, Matrix biology : journal of the International Society for Matrix Biology.

[11]  G. Bentley,et al.  Mechanisms of Internalization ofStaphylococcus aureus by Cultured Human Osteoblasts , 1999, Infection and Immunity.

[12]  T. Foster,et al.  Surface protein adhesins of Staphylococcus aureus. , 1998, Trends in microbiology.

[13]  R. Fässler,et al.  Roles of integrins and fibronectin in the entry of Streptococcus pyogenes into cells via protein F1 , 1998, Molecular microbiology.

[14]  C. Sasakawa,et al.  Streptococcus pyogenes protein F promotes invasion of HeLa cells. , 1998, Microbiology.

[15]  P. Cleary,et al.  Streptococcus pyogenes Serotype M1 Encodes Multiple Pathways for Entry into Human Epithelial Cells , 1998, Infection and Immunity.

[16]  E. Burstein,et al.  Protein F1 is required for efficient entry of Streptococcus pyogenes into epithelial cells. , 1998, The Journal of infectious diseases.

[17]  J. V. van Putten,et al.  Entry of OpaA+ gonococci into HEp‐2 cells requires concerted action of glycosaminoglycans, fibronectin and integrin receptors , 1998, Molecular microbiology.

[18]  Pascale Cossart,et al.  The InlB protein of Listeria monocytogenes is sufficient to promote entry into mammalian cells , 1998 .

[19]  P. Cossart,et al.  Internalin of Listeria monocytogenes with an intact leucine-rich repeat region is sufficient to promote internalization , 1997, Infection and immunity.

[20]  M. Smeltzer,et al.  Prevalence and chromosomal map location of Staphylococcus aureus adhesin genes. , 1997, Gene.

[21]  J. Lissitzky,et al.  Sialic acid-dependent recognition of laminin and fibrinogen by Aspergillus fumigatus conidia , 1997, Infection and immunity.

[22]  B. Finlay,et al.  Exploitation of mammalian host cell functions by bacterial pathogens. , 1997, Science.

[23]  D. Hooper,et al.  Increased expression of fibronectin-binding proteins by fluoroquinolone-resistant Staphylococcus aureus exposed to subinhibitory levels of ciprofloxacin , 1997, Antimicrobial agents and chemotherapy.

[24]  M. Rohde,et al.  The fibronectin-binding protein of Streptococcus pyogenes, SfbI, is involved in the internalization of group A streptococci by epithelial cells , 1997, Infection and immunity.

[25]  J. Esko,et al.  Microbial adherence to and invasion through proteoglycans , 1997, Infection and immunity.

[26]  P. Cossart,et al.  E-Cadherin Is the Receptor for Internalin, a Surface Protein Required for Entry of L. monocytogenes into Epithelial Cells , 1996, Cell.

[27]  K. Yamada,et al.  A two‐domain mechanism for group A streptococcal adherence through protein F to the extracellular matrix. , 1996, The EMBO journal.

[28]  E. Deitch,et al.  Caco-2 and IEC-18 intestinal epithelial cells exert bactericidal activity through an oxidant-dependent pathway. , 1995, Shock.

[29]  P. François,et al.  Adhesion properties of mutants of Staphylococcus aureus defective in fibronectin‐binding proteins and studies on the expression of fnb genes , 1995, Molecular microbiology.

[30]  M. Wilks,et al.  Detection by PCR and analysis of the distribution of a fibronectin-binding protein gene (fbn) among staphylococcal isolates. , 1995, Journal of medical microbiology.

[31]  P. François,et al.  Molecular characterization of the clumping factor (fibrinogen receptor) of Staphylococcus aureus , 1994, Molecular microbiology.

[32]  D. Pittet,et al.  Fibronectin is more active than fibrin or fibrinogen in promoting Staphylococcus aureus adherence to inserted intravascular catheters. , 1993, The Journal of infectious diseases.

[33]  R. Isberg,et al.  The integrin-binding domain of invasin is sufficient to allow bacterial entry into mammalian cells , 1992, Infection and immunity.

[34]  S. Eykyn,et al.  Increase in native valve endocarditis caused by coagulase negative staphylococci: an Anglo-French clinical and microbiological study. , 1990, British heart journal.

[35]  R. Isberg,et al.  Multiple β 1 chain integrins are receptors for invasin, a protein that promotes bacterial penetration into mammalian cells , 1990, Cell.

[36]  I. Nes,et al.  High-Frequency Transformation, by Electroporation, of Lactococcus lactis subsp. cremoris Grown with Glycine in Osmotically Stabilized Media , 1989, Applied and environmental microbiology.

[37]  G. Bukholm,et al.  Adhesiveness and invasiveness of staphylococcal species in a cell culture model , 1989, APMIS : acta pathologica, microbiologica, et immunologica Scandinavica.

[38]  A. Chopin,et al.  Construction of a vector plasmid family and its use for molecular cloning in Streptococcus lactis. , 1988, Biochimie.

[39]  T. Drake,et al.  Staphylococcus aureus induces tissue factor expression in cultured human cardiac valve endothelium. , 1988, The Journal of infectious diseases.

[40]  S. Falkow,et al.  Identification of invasin: A protein that allows enteric bacteria to penetrate cultured mammalian cells , 1987, Cell.

[41]  F. Lowy,et al.  Bacterial adherence to human endothelial cells in vitro , 1985, Infection and Immunity.

[42]  F. Waldvogel,et al.  Adsorption of fibronectin onto polymethylmethacrylate and promotion of Staphylococcus aureus adherence , 1984, Infection and immunity.

[43]  M. Gasson,et al.  Plasmid complements of Streptococcus lactis NCDO 712 and other lactic streptococci after protoplast-induced curing , 1983, Journal of bacteriology.

[44]  K. Schleifer,et al.  Description of a New Species of the Genus Staphylococcus: Staphylococcus carnosus , 1982 .

[45]  R. Novick.  Properties of a cryptic high-frequency transducing phage in Staphylococcus aureus. , 1967, Virology.

[46]  J. Marmur.  A procedure for the isolation of deoxyribonucleic acid from micro-organisms , 1961 .

[47]  P. François,et al.  Identification of plasma proteins adsorbed on hemodialysis tubing that promote Staphylococcus aureus adhesion. , 2000, The Journal of laboratory and clinical medicine.

[48]  J. C. Lee.  Electrotransformation of Staphylococci. , 1995, Methods in molecular biology.

[49]  E. A. Elsinghorst.  Measurement of invasion by gentamicin resistance. , 1994, Methods in enzymology.

[50]  D. Letourneur,et al.  Inhibition by heparin and derivatized dextrans of Staphylococcus aureus adhesion to fibronectin-coated biomaterials. , 1992, Journal of biomaterials science. Polymer edition.

[51]  M. Lindberg,et al.  Nucleotide sequence of the gene for a fibronectin-binding protein from Staphylococcus aureus: use of this peptide sequence in the synthesis of biologically active peptides. , 1989, Proceedings of the National Academy of Sciences of the United States of America.