A study of the interaction between Helicobacter pylori and components of the human fibrinolytic system

Yarzábal, Andrés; Avilán, Luisana; Hoelzl, K.; Muñoz, M.; Puig, Juan; Kansau, Imad

doi:10.1590/s0100-879x2000000900004

Cited by 6 publications

(3 citation statements)

References 37 publications

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“…Binding is sensitive to lysine analogs, and bound Plg is activated by tPA [222]. H. pylori produces a dodecameric neutrophil activating protein (HP-NAP) that can potentially inhibit fibrinolytic activities [18].…”

Section: Mechanisms Of Pathogen Invasion Using Host and Bacterial mentioning

confidence: 99%

Bacterial Plasminogen Receptors Utilize Host Plasminogen System for Effective Invasion and Dissemination

Bhattacharya

Ploplis

Castellino

2012

Journal of Biomedicine and Biotechnology

116

118

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In order for invasive pathogens to migrate beyond the site of infection, host physiological barriers such as the extracellular matrix, the basement membrane, and encapsulating fibrin network must be degraded. To circumvent these impediments, proteolytic enzymes facilitate the dissemination of the microorganism. Recruitment of host proteases to the bacterial surface represents a particularly effective mechanism for enhancing invasiveness. Plasmin is a broad spectrum serine protease that degrades fibrin, extracellular matrices, and connective tissue. A large number of pathogens express plasminogen receptors which immobilize plasmin(ogen) on the bacterial surface. Surface-bound plasminogen is then activated by plasminogen activators to plasmin through limited proteolysis thus triggering the development of a proteolytic surface on the bacteria and eventually assisting the spread of bacteria. The host hemostatic system plays an important role in systemic infection. The interplay between hemostatic processes such as coagulation and fibrinolysis and the inflammatory response constitutes essential components of host defense and bacterial invasion. The goal of this paper is to highlight mechanisms whereby pathogenic bacteria, by engaging surface receptors, utilize and exploit the host plasminogen and fibrinolytic system for the successful dissemination within the host.

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Section: Mechanisms Of Pathogen Invasion Using Host and Bacterial mentioning

confidence: 99%

Bacterial Plasminogen Receptors Utilize Host Plasminogen System for Effective Invasion and Dissemination

Bhattacharya

Ploplis

Castellino

2012

Journal of Biomedicine and Biotechnology

116

118

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“…pylori Pg-binding proteins (Pgbs) have been identified (20,21), but the genes were not identified. This study identifies the H. pylori 26695 genes HP0508 and HP0863 (pgbA and pgbB, respectively) as responsible for H. pylori Pg-binding activity, and the characterization of these gene products suggests that they may be important virulence factors.…”

mentioning

confidence: 99%

Molecular cloning and characterization of two Helicobacter pylori genes coding for plasminogen-binding proteins

Jönsson

Guo

Monstein

et al. 2004

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

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Helicobacter pylori binds a number of host cell proteins, including the plasma protein plasminogen, which is the proenzyme of the serine protease plasmin. Two H. pylori plasminogen-binding proteins have been described; however, no genes were identified. Here we report the use of a phage display library to clone two genes from the H. pylori CCUG 17874 genome that mediate binding to plasminogen. DNA sequence analysis of one of these genes revealed 96.6% homology with H. pylori 26695 HP0508. A subsequent database search revealed that the amino acid sequence of a lysine-rich C-terminal segment of HP0508 is identical to the C terminus of HP0863. Recombinant proteins expressed from HP0508 and HP0863 bound plasminogen specifically and in a lysine-dependent manner. We designate these genes pgbA and pgbB, respectively. These proteins are expressed by a variety of H. pylori strains, have surface-exposed domains, and do not inhibit plasminogen activation. These results indicate that pgbA and pgbB may allow H. pylori to coat its exterior with plasminogen, which subsequently can be activated to plasmin. The surface acquisition of protease activity may enhance the virulence of H. pylori.

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“…Many events in the host may be responsible for the exposition of the basal lamina: (a) it can occur because of the B. fragiles itself (Oyston & Handley, 1990), (b) because of changes in the microbiota of the host and (c) or due to physical traumas (Tally & Ho, 1987). Recently, it has been established that binding and activation of human plasminogen on the surface of bacterial cells may be a common mechanism used by invasive bacteria to facilitate movement through normal tissue barriers (Yarzabal et al , 2000). Indeed, many pathogens interact with host plasminogen, contributing to their pathogenicity (Sun, 2006).…”

Section: Discussionmentioning

confidence: 99%

The interaction ofBacteroides fragiliswith components of the human fibrinolytic system

Ferreira¹,

Carvalho²,

Peixoto³

et al. 2009

FEMS Immunology &Amp; Medical Microbiology

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Bacteroides fragilis is a minor component of the intestinal microbiota and the most frequently isolated from intra-abdominal infections and bacteremia. Previously, our group has shown that molecules involved in laminin-1 (LMN-1) recognition were present in outer membrane protein extracts of B. fragilis MC2 strain. One of these proteins was identified and showed 98% similarity to a putative B. fragilis plasminogen-binding protein precursor, deposited in the public database. Thus, the objective of this work was to overexpress and further characterize this novel adhesin. The ability of B. fragilis MC2 strain and purified protein to convert plasminogen into plasmin was tested. Our results showed that B. fragilis strain MC2 strain adhered to both LMN-1 and plasminogen and this adhesion was inhibited by either LMN-1 or plasminogen. Regarding the plasminogen activation activity, both the whole bacterial cell and the purified protein converted plasminogen into plasmin similar to streptokinase used as a positive control. Bacterial receptors that recognize plasminogen bind to it and enhance its activation, transforming a nonproteolytic bacterium into a proteolytic one. We present in vitro evidence for a pathogenic function of the plasminogen receptor in promoting adherence to laminin and also the formation of plasmin by B. fragilis.

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A study of the interaction between Helicobacter pylori and components of the human fibrinolytic system

Cited by 6 publications

References 37 publications

Bacterial Plasminogen Receptors Utilize Host Plasminogen System for Effective Invasion and Dissemination

Bacterial Plasminogen Receptors Utilize Host Plasminogen System for Effective Invasion and Dissemination

Molecular cloning and characterization of two Helicobacter pylori genes coding for plasminogen-binding proteins

The interaction ofBacteroides fragiliswith components of the human fibrinolytic system

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