Penicillin-binding Proteins in Listeria monocytogenes

GUTKIND G; MOLLERACH M; DE TORRES RA

Acta Pathol Microbiol Immunol Scand [B]

Munksgaard International Publishers

Año: 1989 vol. 97 p. 1013 - 1017

0108-0180

The Penicillin-binding Proteins (PBPs) of Listeria monocytogenes 29-CCM-A 454 (ATCC 15313) are described by the use of 125-I-Penicillin X as radiotracer. The membranes of this tolerant bacilli contained at least five proteins with different affinities for the radiotracer or dicloxacillin. The molecular weights of these proteins were estimated as 76, 74, 67, 66, and 47 kDa. Dicloxacillin induced the formation of straight filaments when present at subinhibitoy concentrations, while penicillin G did not induce any visible alteration in the morphology of this microorganism.