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Journal of Bacteriology, December 2002, p. 6786-6795, Vol. 184, No. 24
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.24.6786-6795.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Isolation of Three New Surface Layer Protein Genes (slp) from Lactobacillus brevis ATCC 14869 and Characterization of the Change in Their Expression under Aerated and Anaerobic Conditions

Miia Jakava-Viljanen,1,{dagger} Silja Åvall-Jääskeläinen,1 Paul Messner,2 Uwe B. Sleytr,2 and Airi Palva1*

Department of Basic Veterinary Sciences, Division of Microbiology, FIN-00014 University of Helsinki, Finland,1 Center for Ultrastructure Research, University of Agricultural Sciences Vienna, A-1180 Vienna, Austria2

Received 22 July 2002/ Accepted 17 September 2002

Two new surface layer (S-layer) proteins (SlpB and SlpD) were characterized, and three slp genes (slpB, slpC, and slpD) were isolated, sequenced, and studied for their expression in Lactobacillus brevis neotype strain ATCC 14869. Under different growth conditions, L. brevis strain 14869 was found to form two colony types, smooth (S) and rough (R), and to express the S-layer proteins differently. Under aerobic conditions R-colony type cells produced SlpB and SlpD proteins, whereas under anaerobic conditions S-colony type cells synthesized essentially only SlpB. Anaerobic and aerated cultivations of ATCC 14869 cells in rich medium also resulted in S-layer protein patterns similar to those of the S- and R-colony type cells, respectively. Electron microscopy suggested the presence of only a single S-layer with an oblique structure on the cells of both colony forms. The slpB and slpC genes were located adjacent to each other, whereas the slpD gene was not closely linked to the slpB-slpC gene region. Northern analyses confirmed that both slpB and slpD formed a monocistronic transcription unit and were effectively expressed, but slpD expression was induced under aerated conditions. slpC was a silent gene under the growth conditions tested. The amino acid contents of all the L. brevis ATCC 14869 S-layer proteins were typical of S-layer proteins, whereas their sequence similarities with other S-layer proteins were negligible. The interspecies identity of the L. brevis S-layer proteins was mainly restricted to the N-terminal regions of those proteins. Furthermore, Northern analyses, expression of a PepI reporter protein under the control of the slpD promoter, and quantitative real-time PCR analysis of slpD expression under aerated and anaerobic conditions suggested that, in L. brevis ATCC 14869, the variation of S-layer protein content involves activation of transcription by a soluble factor rather than DNA rearrangements that are typical for most of the S-layer phase variation mechanisms known.

* Corresponding author. Mailing address: Department of Basic Veterinary Sciences, P.O. Box 57, FIN 00014 University of Helsinki, Finland. Phone: 358 9 191 49531. Fax: 358 9 191 49799. E-mail: Airi.Palva{at}helsinki.fi.

{dagger} Present address: National Veterinary and Food Research Institute, 00580 Helsinki, Finland.

Journal of Bacteriology, December 2002, p. 6786-6795, Vol. 184, No. 24
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.24.6786-6795.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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