1996
DOI: 10.1128/iai.64.8.3259-3266.1996
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Biochemical and molecular analysis of phospholipase C and phospholipase D activity in mycobacteria

Abstract: Resurgence of mycobacterial infections in the United States has led to an intense effort to identify potential virulence determinants in the genus Mycobacterium, particularly ones that would be associated with the more virulent species (e.g., Mycobacterium tuberculosis). Thin-layer chromatography (TLC) using radiolabeled phosphatidylcholine and sphingomyelin as substrates indicated that cell extracts of M. tuberculosis contain both phospholipase C (PLC) and phospholipase D (PLD) activities. In contrast, only P… Show more

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Cited by 78 publications
(46 citation statements)
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“…The mutation in 2L is predicted to truncate 486 bp from the 3P end of acpA, removing the C-terminal 162 amino acids of AcpA. This represents 31.5% of the protein and includes three of the ¢ve most highly conserved regions between AcpA and the PLCs of P. aeruginosa (Plc-N and Plc-H) [7] as well as two more recently identi¢ed PLCs of Mycobacterium tuberculosis (MpcA and MpcB) [12,13].…”
Section: Resultsmentioning
confidence: 99%
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“…The mutation in 2L is predicted to truncate 486 bp from the 3P end of acpA, removing the C-terminal 162 amino acids of AcpA. This represents 31.5% of the protein and includes three of the ¢ve most highly conserved regions between AcpA and the PLCs of P. aeruginosa (Plc-N and Plc-H) [7] as well as two more recently identi¢ed PLCs of Mycobacterium tuberculosis (MpcA and MpcB) [12,13].…”
Section: Resultsmentioning
confidence: 99%
“…The di¡erence in substrate speci¢city has been proposed to be conferred by the C-terminal one-third of the proteins, which was found to have reduced homology compared to the N-terminal two-thirds [17]. MpcA and MpcB can both direct the hydrolysis of phosphatidylcholine and sphingomyelin when expressed in Mycobacterium smegmatis, a mycobacterial strain devoid of PLC activity [13]. It is interesting to note that AcpA, MpcA, and MpcB are substantially smaller (by about 200 amino acids) than Plc-H and Plc-N, although by comparison of their amino acid sequences with the Pseudomonas PLCs and AcpA, the Mycobacterium PLCs are more similar to Plc-H and Plc-N (36^38% identical vs. 18% identical to AcpA).…”
Section: Discussionmentioning
confidence: 99%
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“…Second, the products of phospholipid hydrolysis can be converted to glycine betaine which accumulates within the bacterial cell and is thought to protect the bacterial cell from conditions of high osmolarity found in the lung (Landfald and Strom 1986;Shortridge et al 1992). The recent identification of tandemly organized genes in Mycobacterium tuberculosis (Johansen et al 1996), which would encode homologues of the Ps. aeruginosa phos-pholipases C will open new avenues of research with this pathogen.…”
Section: Invasion and Growthmentioning
confidence: 99%
“…aeruginosa (Ostroff et al 1990), only PlcH is able to hydrolyse both substrates and this enzyme is thought to play an important role in the pathogenesis of disease. In mycobacterial species, the most virulent strains © 1998 The Society for Applied Microbiology, Journal of Applied Microbiology Symposium Supplement 84, 127S-137S produce both phospholipase C and sphingomyelinase activities (Johansen et al 1996).…”
Section: Relationship Between Membrane Lateral Pressure and Hydrolysimentioning
confidence: 99%