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Applied and Environmental Microbiology, March 2004, p. 1336-1346, Vol. 70, No. 3
0099-2240/04/$08.00+0     DOI: 10.1128/AEM.70.3.1336-1346.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Heat Shock Response in Lactobacillus plantarum

Maria De Angelis,1,{dagger} Raffaella Di Cagno,2,{dagger} Claude Huet,3 Carmine Crecchio,4 Patrick F. Fox,5 and Marco Gobbetti2,{dagger}*

Institute of Sciences of Food Production, CNR, 70125 Bari,1 Dipartimento di Protezione delle Piante e Microbiologia Applicata and,2 Dipartimento di Biologia e Chimica Agro-Forestale ed Ambientale, University of Bari, 70126 Bari, Italy,4 Unité de Biochimie et Structure des Protéines, INRA, 78352 Jouy-en-Josas, France,3 Department of Food and Nutritional Sciences, University College, Cork, Ireland5

Received 3 July 2003/ Accepted 5 December 2003

Heat stress resistance and response were studied in strains of Lactobacillus plantarum. Stationary-phase cells of L. plantarum DPC2739 had decimal reduction times (D values) (D value was the time that it took to reduce the number of cells by 1 log cycle) in sterile milk of 32.9, 14.7, and 7.14 s at 60, 72, and 75°C, respectively. When mid-exponential-phase cells were used, the D values decreased. The temperature increases which caused a 10-fold reduction in the D value ranged from 9 to 20°C, depending on the strain. Part of the cell population treated at 72°C for 90 s recovered viability during incubation at 7°C in sterile milk for 20 days. When mid-exponential- or stationary-phase cells of L. plantarum DPC2739 were adapted to 42°C for 1 h, the heat resistance at 72°C for 90 s increased ca. 3 and 2 log cycles, respectively. Heat-adapted cells also showed increased growth at pH 5 and in the presence of 6% NaCl. Two-dimensional gel electrophoresis of proteins expressed by control and heat-adapted cells revealed changes in the levels of expression of 31 and 18 proteins in mid-exponential- and stationary-phase cells, respectively. Twelve proteins were commonly induced. Nine proteins induced in the heat-adapted mid-exponential- and/or stationary-phase cells of L. plantarum DPC2739 were subjected to N-terminal sequencing. These proteins were identified as DnaK, GroEL, trigger factor, ribosomal proteins L1, L11, L31, and S6, DNA-binding protein II HlbA, and CspC. All of these proteins have been found to play a role in the mechanisms of stress adaptation in other bacteria. Antibodies against GroES detected a protein which was induced moderately, while antibodies against DnaJ and GrpE reacted with proteins whose level of expression did not vary after heat adaptation. This study showed that the heat resistance of L. plantarum is a complex process involving proteins with various roles in cell physiology, including chaperone activity, ribosome stability, stringent response mediation, temperature sensing, and control of ribosomal function. The physiological mechanisms of response to pasteurization in L. plantarum are fundamental for survival in cheese during manufacture.

* Corresponding author. Mailing address: Dipartimento di Protezione delle Piante e Microbiologia Applicata, Facoltà di Agraria di Bari, Via G. Amendola 165/a, 70126 Bari, Italy. Phone: 39 080 5442949. Fax: 39 080 5442911. E-mail: gobbetti{at}agr.uniba.it

{dagger} Maria De Angelis and Raffaella Di Cagno contributed equally to this work.

Applied and Environmental Microbiology, March 2004, p. 1336-1346, Vol. 70, No. 3
0099-2240/04/$08.00+0     DOI: 10.1128/AEM.70.3.1336-1346.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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