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Infection and Immunity, October 1999, p. 5206-5214, Vol. 67, No. 10
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Streptococcus parasanguis pepO Encodes an Endopeptidase with Structure and Activity Similar to Those of Enzymes That Modulate Peptide Receptor Signaling in Eukaryotic Cells

Eunice H. Froeliger,1 Joyce Oetjen,1 Jeffrey P. Bond,1,2 and Paula Fives-Taylor1,*

Department of Microbiology and Molecular Genetics, University of Vermont,1 and Vermont Cancer Center,2 Burlington, Vermont 05405

Received 27 April 1999/Returned for modification 14 June 1999/Accepted 16 July 1999

Studies in our laboratory have identified two fimbria-associated adhesins, FimA and Fap1, of Streptococcus parasanguis FW213. In this study, we isolated and sequenced DNA fragments linked to fimA to determine if they contained additional factors associated with adherence, virulence, or survival in the host. An open reading frame just upstream and divergently transcribed from the fimA operon was identified and named pepO. Northern hybridization indicated that pepO is transcribed as a monocistronic message. pepO encodes a predicted 631-amino-acid protein with a molecular mass of approximately 70.6 kDa. PepO contains the essential motif HEXXH, typical of many zinc-dependent metalloproteases and metallopeptidases. PepO has significant sequence identity to mammalian metallopeptidases, including endothelin-converting enzyme, which converts a potent vasoconstrictor into its active form, and neutral endopeptidase (NEP), which is involved in terminating the activity of opioid peptides. The opioid peptide metenkephalin is a natural substrate of NEP. Cell extracts of FW213 cleaved metenkephalin at the same site as does NEP, while an extract from an insertionally inactivated pepO mutant did not. These results indicate that FW213 pepO encodes an enzyme with activity similar to that of known mammalian endopeptidases. Phylogenetic analysis of PepO and its homologues suggests lateral genetic exchange between bacteria and eukaryotes.

* Corresponding author. Mailing address: University of Vermont, Department of Microbiology and Molecular Genetics, Stafford Hall, Burlington, VT 05405. Phone: (802) 656-1121. Fax: (802) 656-8749. E-mail: pfivesta{at}zoo.uvm.edu.

Infection and Immunity, October 1999, p. 5206-5214, Vol. 67, No. 10
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

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