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

Abstract

The kinetic, thermodynamic and structural stability of gp36C, the virion-associated peptidoglycan hydrolase domain of bacteriophage phiKMV, 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, DeltaH(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.

• Authors: Y Briers, R Lavigne, P Plessers, K Hertveldt, I Hanssens, Y Engelborghs, G Volckaert
• Journal: Cellular and molecular life sciences : CMLS (Cell Mol Life Sci) Vol. 63 Issue 16 Pg. 1899-905 (Aug 2006) ISSN: 1420-682X [Print] Switzerland
• PMID: 16847574 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Viral Proteins
• lysin gp36C, bacteriophage phiKMV

Topics

• Amino Acid Sequence
• Bacteriophages (pathogenicity)
• Calorimetry, Differential Scanning
• Circular Dichroism
• Kinetics
• Molecular Sequence Data
• Pseudomonas (virology)
• Sequence Alignment
• Sequence Homology, Amino Acid
• Spectrophotometry
• Thermodynamics
• Viral Proteins (chemistry, pharmacology)