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Applied and Environmental Microbiology, October 2000, p. 4396-4400, Vol. 66, No. 10
0099-2240/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Identification of Collagen-Binding Proteins in Lactobacillus spp. with Surface-Enhanced Laser Desorption/Ionization-Time of Flight ProteinChip Technology

Jeffrey C. Howard,1,2,3 Christine Heinemann,2 Bradley J. Thatcher,4 Brian Martin,5 Bing Siang Gan,1,2,3,6,7 and Gregor Reid2,3,8,*

Hand and Upper Limb Centre1 and Lawson Research Institute,2 London, Ontario, Canada; Ciphergen Biosystems, Inc., Palo Alto, California4; Division of Clinical Neuroscience, National Institutes of Health, Bethesda, Maryland5; and Department of Surgery,3 Department of Pharmacology & Toxicology,6 Department of Microbiology and Immunology,8 and Department of Medical Biophysics,7 The University of Western Ontario, London, Ontario, Canada

Received 4 May 2000/Accepted 27 June 2000

Biosurfactants produced by Lactobacillus fermentum RC-14, L. rhamnosus GR-1 and 36, and L. casei Shirota were found to contain proteins that bind to both collagen types III and VI, as determined by surface-enhanced laser desorption/ionization (SELDI)-time of flight mass spectrometry. Both collagen types III and VI immobilized on SELDI preactivated ProteinChip arrays detected several different sizes (2 to 48 kDa) of collagen-binding proteins. Overall, the RC-14-produced biosurfactant contained the greatest number of collagen-binding proteins (RC-14 > GR-1 > 36 > Shirota), including the mature form of a previously cloned 29-kDa collagen-binding protein (referred to in its mature 26-kDa form). Although biosurfactants isolated from L. casei Shirota and L. rhamnosus 36 and GR-1 also contain several collagen-binding proteins, they do not contain the 26-kDa collagen-binding protein. Together, these results demonstrate the utility of the SELDI system as a means of rapidly characterizing clinically important but complex biosurfactant solutions.

* Corresponding author. Mailing address: H414, Lawson Research Institute, 268 Grosvenor Street, London, Ontario N6A 4V2, Canada. Phone: (519) 646-6100, ext. 65256. Fax: (519) 646-6110. E-mail: gregor{at}julian.uwo.ca.

Applied and Environmental Microbiology, October 2000, p. 4396-4400, Vol. 66, No. 10
0099-2240/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • van Hijum, S. A. F. T., Kralj, S., Ozimek, L. K., Dijkhuizen, L., van Geel-Schutten, I. G. H. (2006). Structure-Function Relationships of Glucansucrase and Fructansucrase Enzymes from Lactic Acid Bacteria. Microbiol. Mol. Biol. Rev. 70: 157-176 [Abstract] [Full Text]  
  • Reid, G., Gan, B. S., She, Y.-M., Ens, W., Weinberger, S., Howard, J. C. (2002). Rapid Identification of Probiotic Lactobacillus Biosurfactant Proteins by ProteinChip Tandem Mass Spectrometry Tryptic Peptide Sequencing. Appl. Environ. Microbiol. 68: 977-980 [Abstract] [Full Text]  


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