High‐frequency intracellular invasion of epithelial cells by serotype M1 group A streptococci: M1 protein‐mediated invasion and cytoskeletal rearrangements

Dombek, Priscilla E.; Cue, David; Sedgewick, Jerry; Lam, Hong; Ruschkowski, Sharon; Finlay, B. Brett; Cleary, P. Patrick

doi:10.1046/j.1365-2958.1999.01223.x

Cited by 127 publications

(135 citation statements)

References 46 publications

(84 reference statements)

Supporting

Mentioning

132

Contrasting

Unclassified

Order By: Relevance

“…The capacity to bind Fn renders these bacteria capable of employing integrins as receptors for efficient internalization. Extensive studies established that ␣5␤1 integrin is the primary receptor for M1-mediated (8,34) and PrtF1-mediated GAS invasion of epithelial cells (9,11). Integrin signaling required for Streptococcus internalization has only recently been investigated (10,12,35).…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Streptococcal modulation of cellular invasion via TGF-β1 signaling

Wang

Southern

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

Group A Streptococcus (GAS) and other bacterial pathogens are known to interact with integrins as an initial step in a complex pathway of bacterial ingestion by host cells. Efficient GAS invasion depends on the interaction of bound fibronectin (Fn) with integrins and activation of integrin signaling. TGF-␤1 regulates expression of integrins, Fn, and other extracellular matrix proteins, and positively controls the integrin signaling pathway. Therefore, we postulated that TGF-␤1 levels could influence streptococcal invasion of mammalian cells. Pretreatment of HEp-2 cells with TGF-␤1 increased their capacity to ingest GAS when the bacteria expressed fibronectin-binding proteins (M1 or PrtF1). Western blots revealed significant induction of ␣5 integrin and Fn expression by HEp-2 cells in response to TGF-␤1. Increased ingestion of streptococci by these cells was blocked by a specific inhibitor of the TGF-␤1 receptor I and antibodies directed against ␣5 integrin and Fn, indicating that increased invasion depends on TGF-␤1 up-regulation of both the ␣5 integrin and Fn. The capacity of TGF-␤1 to up-regulate integrin expression and intracellular invasion by GAS was reproduced in primary human tonsil fibroblasts, which could be a source of TGF-␤1 in chronically infected tonsils. The relationship between TGF-␤1 and GAS invasion was strengthened by the observation that TGF-␤1 production was stimulated in GASinfected primary human tonsil fibroblasts. These findings suggest a mechanism by which GAS induce a cascade of changes in mammalian tissue leading to elevated expression of the ␣5␤1 receptor, enhanced invasion, and increased opportunity for survival and persistence in their human host.integrin ͉ fibronectin ͉ fibronectin binding protein ͉ tonsils

show abstract

Section: Discussionmentioning

confidence: 99%

“…Invasion assays were performed as described (7,10,34) with some modifications. Briefly, streptococci grown to stationary phase were washed with PBS and resuspended in DMEM.…”

Section: Methodsmentioning

confidence: 99%

Streptococcal modulation of cellular invasion via TGF-β1 signaling

Wang

Southern

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

show abstract

“…As per previously published methods (Molinari et al, 1997;Dombek et al, 1999), latex beads (3 µm; Sigma-Aldrich, St. Louis, MO) were coated with purified recombinant P159 fragments F1 P159 -F4 P159 . Briefly, 10 8 bead particles in 50 µl of PBS were incubated with 5 µg of purified proteins in PBS overnight at 4°C.…”

Section: Latex Bead Preparation and Pk15 Cell Culturementioning

confidence: 99%

P159 is a proteolytically processed, surface adhesin ofMycoplasma hyopneumoniae: defined domains of P159 bind heparin and promote adherence to eukaryote cells

Burnett

Dinkla

Rohde

et al. 2006

Molecular Microbiology

185

View full text Add to dashboard Cite

SummaryMycoplasma hyopneumoniae , the causative agent of porcine enzootic pneumonia, colonizes the respiratory cilia of affected swine causing significant economic losses to swine production worldwide. Heparin is known to inhibit adherence of M. hyopneumoniae to porcine respiratory epithelial cilia. M. hyopneumoniae cells bind heparin but the identity of the heparinbinding proteins is limited. Proteomic analysis of M. hyopneumoniae lysates identified 27 kDa (P27), 110 kDa (P110) and 52 kDa (P52) proteins representing different regions of a 159 kDa (P159) protein derived from mhp494. These cleavage fragments were surface located and present at all growth stages.

show abstract

“…This is not to exclude other possible roles. Certainly, there is a multitude of studies suggesting that Fg-and\or IgG-binding M proteins of group A streptococci are involved in adhesion, invasion and colonization (Cleary & Retnoningrum, 1994 ;Dombek et al, 1999 ;Molinari & Chhatwal, 1999 ;Navarre & Schneewind, 1999). Furthermore, wall-anchored M protein has recently been implicated in the maturation of cysteine proteinase (Collin & Olse!…”

Section: Fgbp Contributes To Virulence In Micementioning

confidence: 99%

The fibrinogen-binding protein (FgBP) of Streptococcus equi subsp. equi additionally binds IgG and contributes to virulence in a mouse model

et al. 2001

View full text Add to dashboard Cite

The major cell-wall-associated protein of the equine pathogen Streptococcus equi subsp. equi is an M-like fibrinogen-binding protein (FgBP) which binds equine fibrinogen (Fg) avidly, through residues located at the extreme Nterminus of the molecule. In this study, it is shown that FgBP additionally binds equine IgG-Fc. When tested against polyclonal IgG from ten other animal species, it was found that FgBP binds human, rabbit, pig and cat IgG, but does not bind mouse, rat, goat, sheep, cow or chicken IgG. Through the use of a panel of recombinant FgBP truncates containing defined deletions of sequence, it was shown that residues in the central regions of FgBP are important in IgG binding. An fbp knockout mutant which does not express FgBP on the cell surface was also constructed. Mutant cells failed to autoaggregate, bound no detectable equine Fg or IgG-Fc, were rapidly killed in horse blood, and showed greatly decreased virulence in a mouse model. Results suggest that FgBP is the major surface structure responsible for binding either Fg or IgG, that the molecule has pronounced antiphagocytic properties, and that it is a likely factor contributing to the virulence of wild-type S. equi subsp. equi.

show abstract

High‐frequency intracellular invasion of epithelial cells by serotype M1 group A streptococci: M1 protein‐mediated invasion and cytoskeletal rearrangements

Cited by 127 publications

References 46 publications

Streptococcal modulation of cellular invasion via TGF-β1 signaling

Streptococcal modulation of cellular invasion via TGF-β1 signaling

P159 is a proteolytically processed, surface adhesin ofMycoplasma hyopneumoniae: defined domains of P159 bind heparin and promote adherence to eukaryote cells

The fibrinogen-binding protein (FgBP) of Streptococcus equi subsp. equi additionally binds IgG and contributes to virulence in a mouse model

Contact Info

Product

Resources

About