Open AccessRelatedness of penicillin‐binding proteins from various Listeria species
Author(s) -
Hakenbeck Regine,
Hof Herbert
Publication year - 1991
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.1574-6968.1991.tb04595.x
Subject(s) - penicillin binding proteins , listeria monocytogenes , listeria , penicillin , biochemistry , antibiotics , microbiology and biotechnology , peptide , binding site , biology , bacteria , peptide sequence , amino acid , chemistry , gene , genetics
The heterogeneity of penicillin‐binding proteins (PBPs) of five Listeria species was investigated. Similarities in the overall PBP pattern were found between those of L. welshimeri and L. innocua , and between L. ivanovii and L. seeligeri , and all were distinct from the PBPs of L. monocytogenes . In all species, however, the primary target for β‐lactam antibiotics, as identified in L. monocytogenes recently, appeared highly conserved. In addition, the low‐ M r PBP 5 was biochemically very similar in all strains and contained identical binding properties to β‐lactam compounds, suggesting that this protein may play an important role. All other PBPs varied considerably in their penicilloyl‐peptide pattern, indicating differences in their amino acid sequences.