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Purification of native -enolase from Streptococcus pneumoniae that binds plasminogen and is immunogenic

Department of Medical Microbiology, Royal Free and University College Medical School, London NW3 2PF

Corresponding author: Professor S.H. Gillespie (e-mail: stepheng{at}rfc.ucl.ac.uk).

Received 14 Jan. 2002; revised version received 17 May 2002; accepted 18 May 2002.

Many pathogenic bacteria express plasminogen receptors on their surface, which may play a role in the dissemination of organisms by binding plasminogen that, when converted to plasmin, can digest extracellular matrix proteins. A 45-kDa protein was purified from Streptococcus pneumoniae and confirmed as an -enolase by its ability to catalyse the dehydration of 2-phospho-D-glycerate to phosphoenolpyruvate and by N-terminal sequencing. The activity of -enolase was found in the cytoplasm and in whole cells. Activity was also demonstrated in cell wall fractions, which confirmed that -enolase is a cytoplasmic antigen also expressed on the surface of S. pneumoniae. The plasminogen-binding activity of -enolase was examined by Western blot, which showed that purified -enolase was able to bind human plasminogen. Immunoblots of the purified 45-kDa -enolase with 22 sera from patients with pneumococcal disease showed binding in 15 cases, indicating that pneumococcal enolase is immunogenic.

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