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Cell wall modifications during osmotic stress in Lactobacillus casei
Aims: To study the modification of the cell wall of Lactobacillus casei ATCC 393 grown in high salt conditions. Methods and Results: Differences in the overall structure of cell wall between growth in high salt (MRS + 1 mol l−1 NaCl; N condition) and control (MRS; C condition) conditions were dete...
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Published in: | Journal of applied microbiology 2005-01, Vol.98 (1), p.84-95 |
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Main Authors: | , , |
Format: | Article |
Language: | English |
Subjects: | |
Online Access: | Get full text |
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Summary: | Aims: To study the modification of the cell wall of Lactobacillus casei ATCC 393 grown in high salt conditions.
Methods and Results: Differences in the overall structure of cell wall between growth in high salt (MRS + 1 mol l−1 NaCl; N condition) and control (MRS; C condition) conditions were determined by transmission electronic microscopy and analytical procedures. Lactobacillus casei cells grown in N condition were significantly larger than cells grown under unstressed C condition. Increased sensitivity to mutanolysin and antibiotics with target in the cell wall was observed in N condition. Purified cell wall also showed the increased sensitivity to lysis by mutanolysin. Analysis of peptidoglycan (PG) from stressed cells showed that modification was at the structural level in accordance with a decreased PG cross‐link involving penicillin‐binding proteins (PBP). Nine PBP were first described in this species and these proteins were expressed in low percentages or presented a modified pattern of saturation with penicillin G (Pen G) during growth in high salt. Three of the essential PBP were fully saturated in N condition at lower Pen G concentrations than in C condition, suggesting differences in functionality in vivo.
Conclusions: The results show that growth in high salt modified the structural properties of the cell wall.
Significance and Impact of Study: Advances in understanding the adaptation to high osmolarity, in particular those involving sensitivity to lysis of lactic acid bacteria. |
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ISSN: | 1364-5072 1365-2672 |
DOI: | 10.1111/j.1365-2672.2004.02428.x |