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Infection and Immunity, September 2001, p. 5494-5501, Vol. 69, No. 9
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.9.5494-5501.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Novel Extracellular x-Prolyl Dipeptidyl-Peptidase (DPP) from Streptococcus gordonii FSS2: an Emerging Subfamily of Viridans Streptococcal x-Prolyl DPPs

J. M. Goldstein,1 A. Banbula,2 T. Kordula,3 J. A. Mayo,1 and J. Travis1,*

Department of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia,1 Department of Microbiology and Immunology, Jagiellonian University, Cracow, Poland,2 and Department of Biological, Geological, and Environmental Sciences, Cleveland State University, Cleveland, Ohio3

Received 20 April 2001/Returned for modification 28 May 2001/Accepted 15 June 2001

Streptococcus gordonii is generally considered a benign inhabitant of the oral microflora, and yet it is a primary etiological agent in the development of subacute bacterial endocarditis (SBE), an inflammatory state that propagates thrombus formation and tissue damage on the surface of heart valves. Strain FSS2 produced several extracellular aminopeptidase and fibrinogen-degrading activities during growth in culture. In this report we describe the purification, characterization, and cloning of a serine class dipeptidyl-aminopeptidase, an x-prolyl dipeptidyl-peptidase (Sg-xPDPP, for S. gordonii x-prolyl dipeptidyl-peptidase), produced in a pH-controlled batch culture. Purification of this enzyme by anion exchange, gel filtration, and hydrophobic interaction chromatography yielded a protein monomer of approximately 85 kDa, as shown by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (PAGE) under denaturing conditions. However, under native conditions, the protein appeared to be a homodimer on the basis of gel filtration and PAGE. Kinetic studies indicated that purified enzyme had a unique and stringent x-prolyl specificity that is comparable to both the dipeptidyl-peptidase IV/CD26 and lactococcal x-prolyl dipeptidyl-peptidase families. Nested PCR cloning from an S. gordonii library enabled the isolation and sequence analysis of the full-length gene. A 759-amino-acid polypeptide with a theoretical molecular mass of 87,115 Da and a calculated pI of 5.6 was encoded by this open reading frame. Significant homology was found with the PepX gene family from Lactobacillus and Lactococcus spp. and putative x-prolyl dipeptidyl-peptidases from other streptococcal species. Sg-xPDPP may serve as a critical factor for the sustained bacterial growth in vivo and furthermore may aid in the proteolysis of host tissue that is commonly observed during SBE pathology.

* Corresponding author. Mailing address: Department of Biochemistry and Molecular Biology, University of Georgia, Athens, GA 30602-7229. Phone: (706) 542-1713. Fax: (706) 542-3719. E-mail: jtravis{at}arches.uga.edu.

Infection and Immunity, September 2001, p. 5494-5501, Vol. 69, No. 9
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.9.5494-5501.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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