Open AccessStazyme, a mycobacteriolytic preparation from a Staphylococcus strain, is able to break the permeability barrier in multiple drug resistant Mycobacterium avium
Author(s) -
Rastogi Nalin,
Goh Khye Seng,
ClavelSérès Sabine
Publication year - 1997
Publication title -
fems immunology & medical microbiology
Language(s) - English
Resource type - Journals
eISSN - 1574-695X
pISSN - 0928-8244
DOI - 10.1111/j.1574-695x.1997.tb01100.x
Subject(s) - mycobacterium smegmatis , microbiology and biotechnology , lytic cycle , biology , ethambutol , mycobacterium , rifampicin , mycobacterium tuberculosis , staphylococcus aureus , lysis , cefoxitin , bacilli , bacteria , antibiotics , tuberculosis , virology , medicine , pathology , virus , genetics
As a strategy to augment the potential of existing drugs against Mycobacterium avium , we investigated a mycobacteriolytic preparation (stazyme) from the Staphylococcus strain Clavelis, which results in significant mycobacterial growth inhibition. A total of 10 specific protein bands were characterized in the stazyme preparation: three bands within a major 40–60 kDa fraction, five bands within the range of 30–90 kDa, and two bands of about 12 and 14 kDa respectively. Tested at concentrations of 50 and 200 μg ml −1 of total protein, stazyme was highly bactericidal against M. smegmatis , and bacteriostatic against M. tuberculosis and M. avium . Stazyme was able to break the permeability barrier of M. avium isolates, significantly enhancing the activity of other antituberculous drugs (ethambutol, rifampicin, and amikacin), used at sub‐MIC level. Stazyme essentially possessed a lytic activity as evidenced by its ability to lyse purified M. smegmatis cell walls. This lytic activity was also confirmed on intact M. smegmatis and M. avium bacilli by transmission electron microscopy. Precise identification of this mycobacteriolytic determinant(s) in stazyme may be helpful to define novel drug targets in mycobacteria.