Comparative proteome analysis of Mycobacterium tuberculosis grown under aerobic and anaerobic conditions.
Data are presented from two-dimensional (2-D) PAGE analysis of Mycobacterium tuberculosis strain Harlingen grown during aerobic and anaerobic culture, according to a modified Wayne dormancy model. M. tuberculosis cultures were grown to the transition point between exponential growth and stationary phase in the presence of oxygen (7 days) and then part of the cultures was shifted to anaerobic conditions for 16 days. Growth declined similarly during aerobic and anaerobic conditions, whereas the ATP consumption rapidly decreased in the anaerobic cultures. 2-D PAGE revealed 50 protein spots that were either unique to, or more abundant during, anaerobic conditions and 16 of these were identified by MALDI-TOF. These proteins were the alpha-crystalline homologue (HspX), elongation factor Tu (Tuf), GroEL2, succinyl-CoA : 3-oxoacid-CoA transferase (ScoB), mycolic acid synthase (CmaA2), thioredoxin (TrxB2), beta-ketoacyl-ACP synthase (KasB), l-alanine dehydrogenase (Ald), Rv2005c, Rv2629, Rv0560c, Rv2185c and Rv3866. Some protein spots were found to be proteolytic fragments, e.g. HspX and GroEL2. These data suggest that M. tuberculosis induces expression of about 1 % of its genes in response to dormancy.
Starck
Joakim
J
Department of Bacteriology, Swedish Institute for Infectious Disease Control, S-17182, Solna, Sweden.
Källenius
Gunilla
G
Microbiology and Tumour Biology Centre, Karolinska Institute, S-17177, Stockholm, Sweden.|Department of Bacteriology, Swedish Institute for Infectious Disease Control, S-17182, Solna, Sweden.
Marklund
Britt-Inger
BI
Department of Chemistry and Biomedical Sciences, University of Kalmar, SE-39182, Kalmar, Sweden.
Andersson
Dan I
DI
Microbiology and Tumour Biology Centre, Karolinska Institute, S-17177, Stockholm, Sweden.|Department of Bacteriology, Swedish Institute for Infectious Disease Control, S-17182, Solna, Sweden.
Åkerlund
Thomas
T
Department of Bacteriology, Swedish Institute for Infectious Disease Control, S-17182, Solna, Sweden.
D015099:3-Oxoacyl-(Acyl-Carrier-Protein) Synthase / Q000032:analysis / Q000302:isolation & purification; D000222:Adaptation, Physiological; D000255:Adenosine Triphosphate / Q000378:metabolism; D000332:Aerobiosis; D050788:Alanine Dehydrogenase; D000594:Amino Acid Oxidoreductases / Q000032:analysis / Q000302:isolation & purification; D000693:Anaerobiosis; D000942:Antigens, Bacterial / Q000032:analysis / Q000302:isolation & purification; D001426:Bacterial Proteins / Q000032:analysis / Q000302:isolation & purification; D018834:Chaperonin 60 / Q000032:analysis / Q000302:isolation & purification; D015256:Coenzyme A-Transferases / Q000032:analysis / Q000302:isolation & purification; D015180:Electrophoresis, Gel, Two-Dimensional; D064429:Fatty Acid Synthases / Q000032:analysis / Q000302:isolation & purification; D015964:Gene Expression Regulation, Bacterial; D009169:Mycobacterium tuberculosis / Q000737:chemistry* / Q000254:growth & development* / Q000378:metabolism; D010444:Peptide Elongation Factor Tu / Q000032:analysis / Q000302:isolation & purification; D020543:Proteome / Q000032:analysis* / Q000302:isolation & purification; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D013879:Thioredoxins / Q000032:analysis / Q000302:isolation & purification
D000942:Antigens, Bacterial; D001426:Bacterial Proteins; D018834:Chaperonin 60; C118127:HspX protein, Mycobacterium tuberculosis; D020543:Proteome; D013879:Thioredoxins; D000255:Adenosine Triphosphate; D000594:Amino Acid Oxidoreductases; D050788:Alanine Dehydrogenase; D015099:3-Oxoacyl-(Acyl-Carrier-Protein) Synthase; D064429:Fatty Acid Synthases; D015256:Coenzyme A-Transferases; C021460:3-ketoacid CoA-transferase; D010444:Peptide Elongation Factor Tu; C023926:mycolate synthetase