Open AccessL isteria monocytogenes tyrosine phosphatases affect wall teichoic acid composition and phage resistance
Author(s) -
NirPaz Ran,
Eugster Marcel R.,
Zeiman Einat,
Loessner Martin J.,
Calendar Richard
Publication year - 2012
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2011.02445.x
Subject(s) - teichoic acid , listeria monocytogenes , listeria , mutant , biology , protein tyrosine phosphatase , virulence , phosphatase , microbiology and biotechnology , cell wall , biochemistry , cell envelope , bacteria , tyrosine , phosphorylation , escherichia coli , genetics , peptidoglycan , gene
Abstract Tyrosine phosphatase ( PTP )‐like proteins exist in many bacteria and are segregated into two major groups: low molecular weight and conventional. The latter group also has activity as phosphoinositide phosphatases. These two kinds of PTP are suggested to be involved in many aspects of bacterial physiology including stress response, DNA binding proteins, virulence, and capsule/cell wall production. By annotation, L isteria monocytogenes possesses two potential low molecular weight and two conventional PTP s. Using L. monocytogenes wild‐type ( WT ) strain 10403S, we have created an in‐frame deletion mutant lacking all four PTP s, as well as four additional complemented strains harboring each of the PTP s. No major physiological differences were observed between the WT and the mutant lacking all four PTP s. However, the deletion mutant strain was resistant to Listeria phages A511 and P35 and sensitive to other Listeria phages. This was attributed to reduced attachment to the cell wall. The mutant lacking all PTP s was found to lack N ‐acetylglucosamine in its wall teichoic acid. Phage sensitivity and attachment was rescued in a complemented strain harboring a low molecular weight PTP ( LMRG 1707).