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Molecular cloning and characterization of two Helicobacter pylori genes coding for plasminogen-binding proteins
Jönsson, K., Department of Laboratory Medicine, Division of Clinical Microbiology, Karolinska Hospital, S-171 76 Stockholm, Sweden.
Dept. of Microbiol./Molec. Genet., Harvard Medical School, 200 Longwood Avenue, Boston, MA 02115, United States.
Linköping University, Faculty of Health Sciences. Linköping University, Department of Clinical and Experimental Medicine, Clinical Microbiology . Östergötlands Läns Landsting, Centre for Laboratory Medicine, Department of Molecular Biological Techniques.
Dept. of Microbiol./Molec. Genet., Harvard Medical School, 200 Longwood Avenue, Boston, MA 02115, United States.
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2004 (English)In: Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, E-ISSN 1091-6490, Vol. 101, no 7, 1852-1857 p.Article in journal (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
2004. Vol. 101, no 7, 1852-1857 p.
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Medical and Health Sciences
Identifiers
URN: urn:nbn:se:liu:diva-45817DOI: 10.1073/pnas.0307329101OAI: oai:DiVA.org:liu-45817DiVA: diva2:266713
Available from: 2009-10-11 Created: 2009-10-11 Last updated: 2017-12-13

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Monstein, Hans-Jurg

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