C.-Y. Chen, G. W. Nace and P. L. Irwin, “A 6 × 6 Drop Plate Method for Simultaneous Colony Counting and MPN Enumeration of Campylobacter jejuni, Listeria monocytogenes and Escherichia coli,” Journal of Microbiological Methods, Vol. 55, No. 2, 2003, pp. 475-479. doi:10.1016/S0167-7012(03)00194-5

has been cited by the following article:

• TITLE: Over-Production of P60 Family Proteins, Glycolytic and Stress Response Proteins Characterizes the Autolytic Profile of Listeria monocytogenes

  AUTHORS: Elsa Pinto, Natália Marques, Peter W. Andrew, M. Leonor Faleiro

  KEYWORDS: Listeria monocytogenes; Autolysis Proteome; Stress Proteins

  JOURNAL NAME: Advances in Microbiology, Vol.2 No.2, June 13, 2012

  ABSTRACT: Listeria monocytogenes is a foodborne pathogen capable of surviving under challenging conditions both outside and inside the host. During the transition from exponential to stationary phase it experiences a series of environmental changes that require an appropriate response to maintain cell viability. In this study the autolytic behaviour of a L. monocytogenes strain was investigated by two-dimensional electrophoresis. The study was done at the permissive autolysis temperature, 30℃ and at 20℃, an autolysis non-permissive temperature. An autolytic strain proteome was also compared to a non-autolytic strain at the permissive autolysis temperature. The autolytic strain proteome at 30℃ in comparison to 20℃ evidenced increased synthesis of the P60 autolysin, glycolytic enzymes and proteins related with environmental stress responses. The over-production of P45 autolysin, was observed when the autolytic strain proteome was compared with the non-autolytic strain. The proteomes at the non-permissive temperature and the proteome of the non-autolytic strain were characterized by a diminished synthesis of several stress related proteins. The lack of autolysis seems to be associated to the over-production of proteins linked to fatty acid and amino acid synthesis, transcription regulation and cell morphogenesis as evidenced by the proteome at the non-permissive temperature and the non-autolytic strain. Autolysis proteome evidenced the over-production of P60 autolysins, glycolysis and stress proteins whereas the proteome obtained in conditions of absence of autolysis reveal a completely different group of proteins. Possible targets to activate listerial autolysis were identified.