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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 phi KMV, is analyzed. Recombinant gp36C is highly thermoresistant (k = 0.595 h(-1) at 95 degrees C), but not thermostable (T-m = 50.2 degrees C, Delta H-cal = 6.86 x 10(4) cal mol(-1)). However, aggregation influences kinetic stability in an unusual manner since aggregation is more pronounced at 55 degrees 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 degrees C. These properties are in agreement with gp36C being part of the extensible tail which is ejected in an unfolded state during phage infection.
Keywords
lysin, phiKMV, kinetic stability, thermoresistance, aggregation, phage infection, T4 LYSOZYME, PSEUDOMONAS-AERUGINOSA, LYTIC ENZYME, PROTEIN, PENETRATION, INITIATION, RESOLUTION, MEMBRANE, VIRIONS, T7

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Citation

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MLA
Briers, Yves et al. “Stability Analysis of the Bacteriophage φKMV Lysin gp36C and Its Putative Role During Infection.” CELLULAR AND MOLECULAR LIFE SCIENCES 63.16 (2006): 1899–1905. Print.
APA
Briers, Y., Lavigne, R., Plessers, P., Hertveldt, K., Hanssens, I., Engelborghs, Y., & Volckaert, G. (2006). Stability analysis of the bacteriophage φKMV lysin gp36C and its putative role during infection. CELLULAR AND MOLECULAR LIFE SCIENCES, 63(16), 1899–1905.
Chicago author-date
Briers, Yves, R Lavigne, P Plessers, K Hertveldt, I Hanssens, Y Engelborghs, and G Volckaert. 2006. “Stability Analysis of the Bacteriophage φKMV Lysin gp36C and Its Putative Role During Infection.” Cellular and Molecular Life Sciences 63 (16): 1899–1905.
Chicago author-date (all authors)
Briers, Yves, R Lavigne, P Plessers, K Hertveldt, I Hanssens, Y Engelborghs, and G Volckaert. 2006. “Stability Analysis of the Bacteriophage φKMV Lysin gp36C and Its Putative Role During Infection.” Cellular and Molecular Life Sciences 63 (16): 1899–1905.
Vancouver
1.
Briers Y, Lavigne R, Plessers P, Hertveldt K, Hanssens I, Engelborghs Y, et al. Stability analysis of the bacteriophage φKMV lysin gp36C and its putative role during infection. CELLULAR AND MOLECULAR LIFE SCIENCES. 2006;63(16):1899–905.
IEEE
[1]
Y. Briers et al., “Stability analysis of the bacteriophage φKMV lysin gp36C and its putative role during infection,” CELLULAR AND MOLECULAR LIFE SCIENCES, vol. 63, no. 16, pp. 1899–1905, 2006.
@article{6846517,
  abstract     = {The kinetic, thermodynamic and structural stability of gp36C, the virion-associated peptidoglycan hydrolase domain of bacteriophage phi KMV, is analyzed. Recombinant gp36C is highly thermoresistant (k = 0.595 h(-1) at 95 degrees C), but not thermostable (T-m = 50.2 degrees C, Delta H-cal = 6.86 x 10(4) cal mol(-1)). However, aggregation influences kinetic stability in an unusual manner since aggregation is more pronounced at 55 degrees 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 degrees C. These properties are in agreement with gp36C being part of the extensible tail which is ejected in an unfolded state during phage infection.},
  author       = {Briers, Yves and Lavigne, R and Plessers, P and Hertveldt, K and Hanssens, I and Engelborghs, Y and Volckaert, G},
  issn         = {1420-682X},
  journal      = {CELLULAR AND MOLECULAR LIFE SCIENCES},
  keywords     = {lysin,phiKMV,kinetic stability,thermoresistance,aggregation,phage infection,T4 LYSOZYME,PSEUDOMONAS-AERUGINOSA,LYTIC ENZYME,PROTEIN,PENETRATION,INITIATION,RESOLUTION,MEMBRANE,VIRIONS,T7},
  language     = {eng},
  number       = {16},
  pages        = {1899--1905},
  title        = {Stability analysis of the bacteriophage φKMV lysin gp36C and its putative role during infection},
  url          = {http://dx.doi.org/10.1007/s00018-006-6183-7},
  volume       = {63},
  year         = {2006},
}

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