Depleting proteins from the growth medium of Mycoplasma capricolum unmasks bacterium-derived enzymatic activities.
Mycoplasma constitutes a unique group of bacteria best characterized as lacking peptidoglycan and having one of the smallest genomes of all free-living prokaryotes. Members of this group also represent important pathogens of humans, animals, and plants. Our understanding of the interaction between these pathogens and their hosts is limited, partly due to our inadequate knowledge of the secreted enzymes and virulence factors of these pathogens. Analysis of secreted proteins of mycoplasma has been hampered by their fastidious growth requirements where protein-rich growth supplements are required. Simple ultrafiltration of the complete medium through a 10kDa cut-off membrane successfully removed virtually all of the polypeptides in the medium and supported the growth of Mycoplasma capricolum (type California kid). This modification (AM medium) exposed the activities of a number of enzymes produced by this bacterium during growth including; acid and alkaline phosphatase, gelatinase, and beta-lactamase activities. We also show that the spent culture medium contained hemolysin activity.
Voros
Amanda
A
Department of Biology, Laurentian University, Sudbury, ON, Canada.
Dunnett
Ashley
A
Leduc
Leo G
LG
Saleh
Mazen T
MT
D000818:Animals; D001426:Bacterial Proteins / Q000378:metabolism*; D001431:Bacteriological Techniques; D003470:Culture Media / Q000737:chemistry*; D015964:Gene Expression Regulation, Bacterial / Q000502:physiology*; D015971:Gene Expression Regulation, Enzymologic / Q000502:physiology; D045623:Mycoplasma capricolum / Q000201:enzymology*
D001426:Bacterial Proteins; D003470:Culture Media