Literature DB >> 15039372

Glyceraldehyde-3-phosphate dehydrogenase of Streptococcus pneumoniae is a surface-displayed plasminogen-binding protein.

Simone Bergmann1, Manfred Rohde, Sven Hammerschmidt.   

Abstract

The recruitment of plasminogen endows the bacterial cell surface of Streptococcus pneumoniae with proteolytic activity. In this study we demonstrate specific plasmin- and plasminogen-binding activity for the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH), which is located in the cytoplasm as well as on the surface of pneumococci. GAPDH exhibits a high affinity for plasmin and a significantly lower affinity for plasminogen.

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Year:  2004        PMID: 15039372      PMCID: PMC375162          DOI: 10.1128/IAI.72.4.2416-2419.2004

Source DB:  PubMed          Journal:  Infect Immun        ISSN: 0019-9567            Impact factor:   3.441


  27 in total

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Review 8.  Role of extracellular GAPDH in Streptococcus pyogenes virulence.

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