In Selenomonas ruminantium, a strictly anaerobic and Gram-negative bacterium, cadaverine covalently linked to the peptidoglycan is required for the interaction between the peptidoglycan and the S-layer homologous (SLH) domain of the major outer membrane protein Mep45. Here, using a series of diamines with a general structure of NH3+(CH2)nNH3+ (n = 3 to 6), we found that cadaverine (n = 5) specifically serves as the most efficient constituent of the peptidoglycan in acquiring the high resistance of the cell to external damage agents and is required for effective interaction between the SLH domain of Mep45 and the peptidoglycan, facilitating the correct anchoring of the outer membrane to the peptidoglycan.
|Number of pages||4|
|Journal||Journal of bacteriology|
|Publication status||Published - 2011 May|
ASJC Scopus subject areas
- Molecular Biology