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Literature DB >> 10595783

Use of the plasminogen activation system by microorganisms.

Abstract

The use of host-derived PAS components by invasive bacteria is an increasingly recognized mechanism for acquisition of extracellular proteolytic activity. This overview summarizes the pertinent contributions to this field and is divided into three parts: (1) the PAS, (2) the interaction of bacteria that produce their own plasminogen activators with the host's PAS, and (3) the interaction of bacteria that do not produce their own plasminogen activators but use plasminogen activators supplied by the host. The significance of these mechanisms in relation to the invasive potentials of the various organisms is discussed.

Entities: Chemical

Mesh：

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Year: 1999 PMID： 10595783 DOI： 10.1016/s0022-2143(99)90095-1

Source DB: PubMed Journal: J Lab Clin Med ISSN： 0022-2143

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Cited

32 in total

1. Cell surface antigens of Mycoplasma species bovine group 7 bind to and activate plasminogen.

Authors: Kylie Bower; Steven P Djordjevic; Nicholas M Andronicos; Marie Ranson
Journal: Infect Immun Date: 2003-08 Impact factor: 3.441

2. Enolase as a plasminogen binding protein in Leishmania mexicana.

Authors: Gilmer Vanegas; Wilfredo Quiñones; Cesar Carrasco-López; Juan Luis Concepción; Fernando Albericio; Luisana Avilán
Journal: Parasitol Res Date: 2007-07-27 Impact factor: 2.289

3. Streptococcus pneumoniae choline-binding protein E interaction with plasminogen/plasmin stimulates migration across the extracellular matrix.

Authors: Cécile Attali; Cécile Frolet; Claire Durmort; Julien Offant; Thierry Vernet; Anne Marie Di Guilmi
Journal: Infect Immun Date: 2007-12-10 Impact factor: 3.441

4. OmpL1 is an extracellular matrix- and plasminogen-interacting protein of Leptospira spp.

Authors: Luis G V Fernandes; Monica L Vieira; Karin Kirchgatter; Ivy J Alves; Zenaide M de Morais; Silvio A Vasconcellos; Eliete C Romero; Ana L T O Nascimento
Journal: Infect Immun Date: 2012-07-16 Impact factor: 3.441

5. Matrix metalloproteinase-10 is a target of T and B cell responses that correlate with synovial pathology in patients with antibiotic-refractory Lyme arthritis.

Authors: Jameson T Crowley; Klemen Strle; Elise E Drouin; Annalisa Pianta; Sheila L Arvikar; Qi Wang; Catherine E Costello; Allen C Steere
Journal: J Autoimmun Date: 2016-02-26 Impact factor: 7.094

6. Plasminogen binding by group A streptococcal isolates from a region of hyperendemicity for streptococcal skin infection and a high incidence of invasive infection.

Authors: Fiona C McKay; Jason D McArthur; Martina L Sanderson-Smith; Sandra Gardam; Bart J Currie; Kadaba S Sriprakash; Peter K Fagan; Rebecca J Towers; Michael R Batzloff; Gursharan S Chhatwal; Marie Ranson; Mark J Walker
Journal: Infect Immun Date: 2004-01 Impact factor: 3.441

Use of the plasminogen activation system by microorganisms.

1. Cell surface antigens of Mycoplasma species bovine group 7 bind to and activate plasminogen.

2. Enolase as a plasminogen binding protein in Leishmania mexicana.

3. Streptococcus pneumoniae choline-binding protein E interaction with plasminogen/plasmin stimulates migration across the extracellular matrix.

4. OmpL1 is an extracellular matrix- and plasminogen-interacting protein of Leptospira spp.

5. Matrix metalloproteinase-10 is a target of T and B cell responses that correlate with synovial pathology in patients with antibiotic-refractory Lyme arthritis.

6. Plasminogen binding by group A streptococcal isolates from a region of hyperendemicity for streptococcal skin infection and a high incidence of invasive infection.

7. Modulation of the Bacillus anthracis secretome by the immune inhibitor A1 protease.

8. Reduced thrombin generation increases host susceptibility to group A streptococcal infection.

9. In vitro identification of novel plasminogen-binding receptors of the pathogen Leptospira interrogans.

10. Surface-expressed enolase contributes to the pathogenesis of clinical isolate SSU of Aeromonas hydrophila.