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Stability analysis of the bacteriophage ϕKMV lysin gp36C and its putative role during infection

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Abstract.

The kinetic, thermodynamic and structural stability of gp36C, the virion-associated peptidoglycan hydrolase domain of bacteriophage ϕKMV, is analyzed. Recombinant gp36C is highly thermoresistant (k = 0.595 h−1 at 95°C), but not thermostable (Tm  =  50.2°C, ΔHcal = 6.86 ×  104 cal mol−1). However, aggregation influences kinetic stability in an unusual manner since aggregation is more pronounced at 55°C than at higher temperatures. Furthermore, gp36C reversibly unfolds in a two-state endothermic transition, and circular dichroism analysis shows that gp36C almost completely refolds after a 3-h heat treatment at 85°C. These properties are in agreement with gp36C being part of the extensible tail which is ejected in an unfolded state during phage infection.

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Authors and Affiliations

  1. Division of Gene Technology, Katholieke Universiteit Leuven, Kasteelpark Arenberg 21, Leuven, 3001, Belgium

    Y. Briers, R. Lavigne, P. Plessers, K. Hertveldt & G. Volckaert

  2. Interdisciplinary Research Center, Katholieke Universiteit Leuven, Campus Kortrijk, E. Sabbelaan 53, 8500, Kortrijk, Belgium

    I. Hanssens

  3. Laboratory of Biomolecular Dynamics, Katholieke Universiteit Leuven, Celestijnenlaan 200 D, 3001, Leuven, Belgium

    Y. Engelborghs

Authors
  1. Y. Briers
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  2. R. Lavigne
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  3. P. Plessers
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  4. K. Hertveldt
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  5. I. Hanssens
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  6. Y. Engelborghs
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  7. G. Volckaert
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Corresponding author

Correspondence to Y. Briers.

Additional information

Received 24 April 2006; received after revision 26 May 2006; accepted 10 June 2006

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Briers, Y., Lavigne, R., Plessers, P. et al. Stability analysis of the bacteriophage ϕKMV lysin gp36C and its putative role during infection. Cell. Mol. Life Sci. 63, 1899–1905 (2006). https://doi.org/10.1007/s00018-006-6183-7

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  • DOI: https://doi.org/10.1007/s00018-006-6183-7

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