Zoocin A is a streptococcolytic enzyme produced by Streptococcus equi subsp. zooepidemicus 4881 that has an unknown site of action on the peptidoglycans of susceptible organisms. Analysis of a mutant strain in which the genes for zoocin A and resistance to zoocin A were inactivated revealed that this strain was more susceptible to beta-lactam antibiotics than the parental organism. Purified zoocin A had weak beta-lactamase activity, bound radioactive penicillin covalently, and its streptococcolytic activity was inhibited by penicillin. Thus, zoocin A is a penicillin-binding protein and presumably is a D-alanyl endopeptidase.
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Zoocin A facilitates the entry of antisense constructs into Streptococcus mutans.
FEMS Microbiol Lett
April 2011
Department of Microbiology and Immunology, University of Otago, Dunedin, New Zealand.
The use of antisense oligodeoxyribonucleotides (asODNs) to inhibit gene function has proven to be an extremely powerful tool for establishing gene-function relationships. Diffusion limitations imposed by the thick peptidoglycan layer of Gram-positive bacteria have proven difficult to overcome for permeability of asODNs. Typically, introduction of the asODN is achieved by cloning the antisense sequence into a vector downstream of an inducible promoter and transforming this construct into the cell of interest.
View Article and Find Full Text PDFZif, the zoocin A immunity factor, is a FemABX-like immunity protein with a novel mode of action.
Appl Environ Microbiol
October 2009
Department of Biological Sciences, The University of Alabama, Tuscaloosa, Alabama 35487-0334, USA.
Producer cell immunity to the streptococcolytic enzyme zoocin A, which is a D-alanyl-L-alanine endopeptidase, is due to Zif, the zoocin A immunity factor. Zif has high degrees of similarity to MurM and MurN (members of the FemABX family of proteins), which are responsible for the addition of amino acids to cross bridges during peptidoglycan synthesis in streptococci. In this study, purified peptidoglycans from strains with and without zif were compared to determine how Zif modifies the peptidoglycan layer to cause resistance to zoocin A.
View Article and Find Full Text PDFPrevalence and acquisition of the genes for zoocin A and zoocin A resistance in Streptococcus equi subsp. zooepidemicus.
J Mol Evol
May 2009
Department of Biological Sciences, The University of Alabama, Box 870334, Tuscaloosa, AL 35487-0334, USA.
Zoocin A is a streptococcolytic enzyme produced by Streptococcus equi subsp. zooepidemicus strain 4881. The zoocin A gene (zooA) and the gene specifying resistance to zoocin A (zif) are adjacent on the chromosome and are divergently transcribed.
View Article and Find Full Text PDFUse of 4-sulfophenyl isothiocyanate labeling and mass spectrometry to determine the site of action of the streptococcolytic peptidoglycan hydrolase zoocin A.
Appl Environ Microbiol
January 2009
Department of Biological Sciences, Box 870334, The University of Alabama, Tuscaloosa, AL 35487-0334, USA.
Zoocin A is a streptococcolytic peptidoglycan hydrolase with an unknown site of action that is produced by Streptococcus equi subsp. zooepidemicus 4881. Zoocin A has now been determined to be a d-alanyl-l-alanine endopeptidase by digesting susceptible peptidoglycan with a combination of mutanolysin and zoocin A, separating the resulting muropeptides by reverse-phase high-pressure liquid chromatography, and analyzing them by mass spectrometry (MS) in both the positive- and negative-ion modes to determine their compositions.
View Article and Find Full Text PDFThe metal binding site of zoocin A.
J Biol Inorg Chem
August 2008
Department of Chemistry, University of Alabama, Tuscaloosa, AL 35487-0336, USA.
Direct metal analysis of the bacteriolytic exoenzyme zoocin A failed to unequivocally identify a putative metal cofactor; hence, indirect experiments utilizing NMR were undertaken to settle this question. Cd(2+) as a surrogate metal ion was reconstituted into EDTA-treated, metal-free recombinant zoocin, and (113)Cd-NMR was employed to explore binding in the protein for this ion. The Cd-substituted enzyme was found to have 80-85% of native streptococcolytic activity.
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