Role of αvβ5 integrins and vitronectin in Pseudomonas aeruginosa PAK interaction with A549 respiratory cells

Leroy-Dudal, Johanne; Gagnière, Hélène; Cossard, Elisabeth; Carreiras, Franck; Martino, Patrick Di

doi:10.1016/j.micinf.2004.05.004

Cited by 43 publications

(42 citation statements)

References 35 publications

(38 reference statements)

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“…Our findings also related to the partial inhibition of cytoadherence of isolates from asymptomatic carriers (80340-and 88641-vagina) similar to that verified by other pathogens. The reduction in both cytoadherence and uptake of Pseudomonas aeruginosa caused by previous treatment of A549 respiratory cells with cytochalasin D was reported (22). In this work, an increase was also noted on adherence of clinical isolates (90356-CSF and 90186-blood) to HUVECs.…”

Section: ------------------------------------------------------------supporting

confidence: 72%

Group B Streptococcus induces tyrosine phosphorylation of annexin V and glutathione S-transferase in human umbilical vein endothelial cells

Santos

Penha²,

Mattos‐Guaraldi³

et al. 2009

Int J Mol Med

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Abstract. Group B Streptococcus (GBS), a human pathogen that causes infection and invasive diseases in newborns, pregnant women and immunocompromised adults, has been shown to invade human umbilical vein endothelial cells (HUVECs). The objective of this study was to investigate the molecular mechanisms underlying GBS-HUVEC interaction, focusing specifically on the responsiveness of host protein tyrosine kinase (PTK). We found that GBS serotypes III and V induced actin reorganization and formation of stress fibers into HUVECs. Since rearrangements of the actin cytoskeleton into eukaryotic cells are usually associated with the activation of PTK, we decided to follow the expression of this class of kinases in the course of the interaction. Unexpectedly, treatment of HUVECs with genistein greatly increased both cytoadherence and intracellular viability, for all GBS strains studied. GBS increased tyrosine phosphorylation of two proteins with an apparent molecular mass of 35 and 23 kDa in HUVECs as demonstrated by Western blot analysis with antiphosphotyrosine antibodies. Mass spectra analysis identified these proteins as annexin V and glutathione S-transferase. Studies are in progress to identify the role of these two proteins on GBS-HUVEC interaction.

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Section: ------------------------------------------------------------supporting

confidence: 72%

Group B Streptococcus induces tyrosine phosphorylation of annexin V and glutathione S-transferase in human umbilical vein endothelial cells

Santos

Penha²,

Mattos‐Guaraldi³

et al. 2009

Int J Mol Med

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“…The vitronectin binding of Pseudomonas aeruginosa and Neisseria gonorrhoeae is involved in attachment and internalization of the bacteria into human epithelial cells (27,45). Since vitronectin also is a component of the ECM, binding of H. influenzae to exposed ECM components may contribute to bacterial adherence, which is an essential step in the bacterial pathogenesis.…”

Section: Discussionmentioning

confidence: 99%

“…Since vitronectin has been suggested to function as a receptor for bacteria (27), attachment of bacteria to immobilized vitronectin was investigated. NTHi 3655 and the isogenic PE mutant were applied to vitronectin-coated glass slides followed by standard Gram staining.…”

Section: Pe From H Influenzae Binds Human Vitronectinmentioning

confidence: 99%

NontypeableHaemophilus influenzaeProtein E Binds Vitronectin and Is Important for Serum Resistance

Hallström

Blom

Zipfel

et al. 2009

The Journal of Immunology

138

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Nontypeable Haemophilus influenzae (NTHi) commonly causes local disease in the upper and lower respiratory tract and has recently been shown to interfere with both the classical and alternative pathways of complement activation. The terminal pathway of the complement system is regulated by vitronectin that is a component of both plasma and the extracellular matrix. In this study, we identify protein E (PE; 16 kDa), which is a recently characterized ubiquitous outer membrane protein, as a vitronectin-binding protein of NTHi. A PE-deficient NTHi mutant had a markedly reduced survival in serum compared with the PE-expressing isogenic NTHi wild type. Moreover, the PE-deficient mutant showed a significantly decreased binding to both soluble and immobilized vitronectin. In parallel, PE-expressing Escherichia coli bound soluble vitronectin and adhered to immobilized vitronectin compared with controls. Surface plasmon resonance technology revealed a KD of 0.4 μΜ for the interaction between recombinant PE and immobilized vitronectin. Moreover, the PE-dependent vitronectin-binding site was located at the heparin-binding domains of vitronectin and the major vitronectin-binding domain was found in the central core of PE (aa 84–108). Importantly, vitronectin bound to the surface of NTHi 3655 reduced membrane attack complex-induced hemolysis. In contrast to incubation with normal human serum, NTHi 3655 showed a reduced survival in vitronectin-depleted human serum, thus demonstrating that vitronectin mediates a protective role at the bacterial surface. Our findings show that PE, by binding vitronectin, may play an important role in NTHi pathogenesis.

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“…Simultaneous interaction of Vn with integrins and bacterial surface proteins has been thought to result in the formation of a bridge between bacteria and host cells. This leads to internalization, as exemplified by Streptococcus pneumoniae and Pseudomonas aeruginosa, resulting in downstream signaling events (21)(22)(23). Protein E and protein F of nontypeable H. influenzae have been shown to bind Vn and enhance the serum resistance capacity (18,24).…”

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confidence: 99%

A Fine-Tuned Interaction between Trimeric Autotransporter Haemophilus Surface Fibrils and Vitronectin Leads to Serum Resistance and Adherence to Respiratory Epithelial Cells

Singh

Al-Jubair

et al. 2014

Infect Immun

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dHaemophilus influenzae type b (Hib) escapes the host immune system by recruitment of the complement regulator vitronectin, which inhibits the formation of the membrane attack complex (MAC) by inhibiting C5b-C7 complex formation and C9 polymerization. We reported previously that Hib acquires vitronectin at the surface by using Haemophilus surface fibrils (Hsf). Here we studied in detail the interaction between Hsf and vitronectin and its role in the inhibition of MAC formation and the invasion of lung epithelial cells. The vitronectin-binding region of Hsf was defined at the N-terminal region comprising Hsf amino acids 429 to 652. Moreover, the Hsf recognition site on vitronectin consisted of the C-terminal amino acids 352 to 374. H. influenzae was killed more rapidly in vitronectin-depleted serum than in normal human serum (NHS), and increased MAC deposition was observed at the surface of an Hsf-deficient H. influenzae mutant. In parallel, Hsf-expressing Escherichia coli selectively acquired vitronectin from serum, resulting in significant inhibition of the MAC. Moreover, when vitronectin was bound to Hsf, increased bacterial adherence and internalization into epithelial cells were observed. Taking our findings together, we have defined a fine-tuned protein-protein interaction between Hsf and vitronectin that may contribute to increased Hib virulence.

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Role of αvβ5 integrins and vitronectin in Pseudomonas aeruginosa PAK interaction with A549 respiratory cells

Cited by 43 publications

References 35 publications

Group B Streptococcus induces tyrosine phosphorylation of annexin V and glutathione S-transferase in human umbilical vein endothelial cells

Group B Streptococcus induces tyrosine phosphorylation of annexin V and glutathione S-transferase in human umbilical vein endothelial cells

NontypeableHaemophilus influenzaeProtein E Binds Vitronectin and Is Important for Serum Resistance

A Fine-Tuned Interaction between Trimeric Autotransporter Haemophilus Surface Fibrils and Vitronectin Leads to Serum Resistance and Adherence to Respiratory Epithelial Cells

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