Interaction of Haemophilus infiuenzae with the Mammalian Extracellular Matrix

Virkola, Ritva; Lähteenmäki, Kaarina; Eberhard, Thomas; Kuusela, Pentti; Alphen, Loek van; Ullberg, Måns; Korhonen, Timo

doi:10.1093/infdis/173.5.1137

Cited by 50 publications

(71 citation statements)

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“…In a similar way, streptokinase secreted by group A streptococci activates plasminogen and could be shown to be a key virulence factor in vivo (58). Binding of plasminogen to Haemophilus influenzae and Streptococcus pneumoniae has been shown to result in degradation of the ECM and enhanced penetration of the bacteria (7,22,63).…”

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confidence: 98%

Cytosolic Proteins Contribute to Surface Plasminogen Recruitment ofNeisseria meningitidis

et al. 2007

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Plasminogen recruitment is a common strategy of pathogenic bacteria and results in a broad-spectrum surface-associated protease activity. Neisseria meningitidis has previously been shown to bind plasminogen. In this study, we show by several complementary approaches that endolase, DnaK, and peroxiredoxin, which are usually intracellular proteins, can also be located in the outer membrane and act as plasminogen receptors. Internal binding motifs, rather than C-terminal lysine residues, are responsible for plasminogen binding of the N. meningitidis receptors. Recombinant receptor proteins inhibit plasminogen association with N. meningitidis in a concentration-dependent manner. Besides binding purified plasminogen, N. meningitidis can also acquire plasminogen from human serum. Activation of N. meningitidis-associated plasminogen by urokinase results in functional activity and allows the bacteria to degrade fibrinogen. Furthermore, plasmin bound to N. meningitidis is protected against inactivation by ␣ 2 -antiplasmin.

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confidence: 98%

Cytosolic Proteins Contribute to Surface Plasminogen Recruitment ofNeisseria meningitidis

et al. 2007

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“…The adherence of L. crispatus ST1 cells to the basement membrane (BM) preparation Matrigel (BD Biosciences) was tested as described previously (60). Briefly, Matrigel (diluted 1:10 in PBS) and bovine serum albumin (BSA) (25 g/ml) were coated onto diagnostic slides overnight at 22°C in a moist chamber.…”

Section: Methodsmentioning

confidence: 99%

Glutamine Synthetase and Glucose-6-Phosphate Isomerase Are Adhesive Moonlighting Proteins of Lactobacillus crispatus Released by Epithelial Cathelicidin LL-37

Kainulainen

Loimaranta

Pekkala

et al. 2012

Journal of Bacteriology

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c Glutamine synthetase (GS) and glucose-6-phosphate isomerase (GPI) were identified as novel adhesive moonlighting proteins of Lactobacillus crispatus ST1. Both proteins were bound onto the bacterial surface at acidic pHs, whereas a suspension of the cells to pH 8 caused their release into the buffer, a pattern previously observed with surface-bound enolase and glyceraldehyde-3-phosphate dehydrogenase (GAPDH) of L. crispatus. The pH shift was associated with a rapid and transient increase in cell wall permeability, as measured by cell staining with propidium iodide. A gradual increase in the release of the four moonlighting proteins was also observed after the treatment of L. crispatus ST1 cells with increasing concentrations of the antimicrobial cationic peptide LL-37, which kills bacteria by disturbing membrane integrity and was here observed to increase the cell wall permeability of L. crispatus ST1. At pH 4, the fusion proteins His 6 -GS, His 6 -GPI, His 6 -enolase, and His 6 -GAPDH showed localized binding to cell division septa and poles of L. crispatus ST1 cells, whereas no binding to Lactobacillus rhamnosus GG was detected. Strain ST1 showed a pH-dependent adherence to the basement membrane preparation Matrigel. Purified His 6 -GS and His 6 -GPI proteins bound to type I collagen, and His 6 -GS also bound to laminin, and their level of binding was higher at pH 5.5 than at pH 6.5. His 6 -GS also expressed a plasminogen receptor function. The results show the strain-dependent surface association of moonlighting proteins in lactobacilli and that these proteins are released from the L. crispatus surface after cell trauma, under conditions of alkaline stress, or in the presence of the antimicrobial peptide LL-37 produced by human cells.

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“…Bacterial suspensions of 1 ϫ 10 8 to 5 ϫ 10 9 cells/ml in PBS were incubated on saturated slides for 2 h at 22°C. Methylene blue-stained adherent bacteria were examined using a Jenaval (Carl Zeiss Jena) microscope equipped with a charge-coupled device camera, and the images were digitized using the National Institutes of Health Image 1.55 program as detailed previously (49). The number of bacteria in 24 randomly chosen microscopic fields of 1.6 ϫ 10 4 m 2 was determined.…”

Section: Methodsmentioning

confidence: 99%

Expression ofpls, a Gene Closely Associated with themecAGene of Methicillin-ResistantStaphylococcus aureus, Prevents Bacterial Adhesion In Vitro

Savolainen¹,

Paulín

Westerlund-Wikström³

et al. 2001

Infect Immun

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The pls gene, coding for a large surface protein of methicillin-resistant Staphylococcus aureus, was cloned from a strain which adheres poorly to several mammalian proteins. The structure of pls revealed three distinct repeat regions, one of which was a serine-aspartate repeat characteristic of the Clf-Sdr family of surface proteins in staphylococci. The lengths of the repeat regions varied in different clinical strains and could be used as epidemiological markers. pls was found to be closely associated with the mecA gene by pulsed-field gel electrophoresis analysis of SmaI-digested DNA. A pls mutant constructed by allele replacement adhered well to immobilized fibronectin and immunoglobulin G, in contrast to the parental strain, suggesting that Pls could have a role in preventing adhesion at some stages during an infection.Bacterial adhesion to host cells or extracellular matrices in damaged tissues is a prerequisite for colonization of the host by infecting bacteria. Implanted biomaterial also becomes coated with host proteins, enabling a pathogen to adhere and initiate a device-related infection. Staphylococcus aureus expresses a number of surface proteins that promote binding to the host extracellular matrix or plasma proteins. Several have been characterized at the molecular level, namely, protein A (SpA), binding the Fc part of immunoglobulins and von Willebrand factor (12,16,43,46); the fibronectin-binding proteins FnBPA and FnBPB (11,14,24,42); the fibrinogen-binding proteins ClfA, ClfB, and Efb (previously Fib) (7,32,33); the collagenbinding protein Cna (44); the elastin-binding protein EbpS (37); and the bone sialoprotein-binding protein Bbp (45). S. aureus can bind a number of other host proteins, such as vitronectin, laminin, mucin, and thrombospondin, but the molecular bases of these interactions are still poorly understood.Some methicillin-resistant S. aureus (MRSA) strains show poor in vitro adherence to surfaces coated with several host plasma or extracellular matrix proteins. They were originally identified as strains giving a negative result in rapid S. aureus identification assays using particles coated with immunoglobulin G (IgG) and/or fibrinogen (27). These strains express a novel surface protein called Pls. The protein was originally purified from lysostaphin digests of a clinical MRSA strain, 1061, by affinity chromatography on immobilized wheat germ agglutinin (WGA) (17). Pls is sensitive to proteolysis by plasmin and trypsin. Similarly, the activation of receptor-bound plasminogen to plasmin on the S. aureus surface (28) leads to cleavage of the apparently 230-kDa Pls protein into 175-and 68-kDa segments-hence the name Pls for plasmin sensitive. Also, without prior proteolytic treatments, part of Pls exists as 175-and 68-kDa fragments in lysostaphin digests of Pls-expressing strains (17).Methicillin resistance is caused by the mecA gene, coding for a low-affinity penicillin-binding protein, PBP2a. mecA is part of a large mec DNA region which lacks a homolog in methicillinsensitive stra...

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Interaction of Haemophilus infiuenzae with the Mammalian Extracellular Matrix

Cited by 50 publications

References 51 publications

Cytosolic Proteins Contribute to Surface Plasminogen Recruitment ofNeisseria meningitidis

Cytosolic Proteins Contribute to Surface Plasminogen Recruitment ofNeisseria meningitidis

Glutamine Synthetase and Glucose-6-Phosphate Isomerase Are Adhesive Moonlighting Proteins of Lactobacillus crispatus Released by Epithelial Cathelicidin LL-37

Expression ofpls, a Gene Closely Associated with themecAGene of Methicillin-ResistantStaphylococcus aureus, Prevents Bacterial Adhesion In Vitro

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