This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Schachtsiek, M. Articles by Hertel, C. Search for Related Content PubMed PubMed Citation Articles by Schachtsiek, M. Articles by Hertel, C. Agricola Articles by Schachtsiek, M. Articles by Hertel, C.

 Previous Article  |  Next Article 

Applied and Environmental Microbiology, December 2004, p. 7078-7085, Vol. 70, No. 12
0099-2240/04/$08.00+0     DOI: 10.1128/AEM.70.12.7078-7085.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Characterization of Lactobacillus coryniformis DSM 20001^T Surface Protein Cpf Mediating Coaggregation with and Aggregation among Pathogens

Martina Schachtsiek, Walter P. Hammes, and Christian Hertel^*

Institute of Food Technology, University of Hohenheim, Stuttgart, Germany

Received 20 February 2004/ Accepted 30 July 2004

Phenotypic characterization of aggregation phenotypes of Lactobacillus coryniformis revealed that strain DSM 20001^T coaggregated with Escherichia coli K88, Campylobacter coli, and Campylobacter jejuni but not with other human pathogens. In addition, cells of these pathogens aggregated in the presence of the spent culture supernatant (SCS) of strain DSM 20001^T. Cells of E. coli K88 remained viable in the coaggregates and aggregates for up to 24 h. Both coaggregation and aggregation (co/aggregation) occurred at pH 3.5 to 7.5 and was sensitive to heat (85°C for 15 min) and proteinase K. The co/aggregation-promoting factor (Cpf) was purified, and the gene was identified by PCR with degenerate primers derived from internal amino acid sequences. The cpf gene encoded a 19.9-kDa preprotein with a sec-dependent leader and an isoelectric point of 4.4. The amino acid sequence had no significant similarity to proteins with known functions. Northern analysis revealed not only major transcription from the promoter of cpf but also major transcription from the promoter of the preceding insertion element, ISLco1 belonging to the IS3 family. Recombinant Cpf produced in E. coli mediated aggregation of pathogens comparable to the aggregation obtained with purified Cpf or SCS of strain DSM 20001^T. Cpf could be removed from cells of strain DSM 20001^T by treatment with 5 M LiCl and could be subsequently reattached to the cell surface by using SCS or recombinant Cpf, which resulted in restoration of the co/aggregation property. These results together with those of the amino acid sequence analysis suggest that Cpf is a novel surface protein of L. coryniformis that mediates co/aggregation of some pathogens.

---

* Corresponding author. Mailing address: Institute of Food Technology, University of Hohenheim, D-70593 Stuttgart, Germany. Phone: 49 711 459 4255. Fax: 49 711 459 4199. E-mail: hertel{at}uni-hohenheim.de.

---

Applied and Environmental Microbiology, December 2004, p. 7078-7085, Vol. 70, No. 12
0099-2240/04/$08.00+0     DOI: 10.1128/AEM.70.12.7078-7085.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

This article has been cited by other articles:

• Lebeer, S., Vanderleyden, J., De Keersmaecker, S. C. J. (2008). Genes and Molecules of Lactobacilli Supporting Probiotic Action. Microbiol. Mol. Biol. Rev. 72: 728-764 [Abstract] [Full Text]  
• Brinster, S., Furlan, S., Serror, P. (2007). C-Terminal WxL Domain Mediates Cell Wall Binding in Enterococcus faecalis and Other Gram-Positive Bacteria. J. Bacteriol. 189: 1244-1253 [Abstract] [Full Text]