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Methods for the separation and identification of mycobactins from various species of mycobacteria.

ABSTRACT: A single pure component was isolated from mycobactin P by countercurrent distribution; its side chain is n-cis-octadec-2-enoyl; its purity and molecular structure were confirmed by mass spectrometry of its aluminium complex. The separation of ferric and of aluminium complexes of mycobactins by thin-layer chromatography is described. Mycobacterium terrae, M. marinum and M. smegmatis produce mycobactins that differ among themselves and from mycobactins P and T. A nomenclature for the mycobactins and their derivatives is suggested.

SUBMITTER: White AJ

PROVIDER: S-EPMC1198856 | BioStudies | 1968-01-01

SECONDARY ACCESSION(S): 10.1042/bj1080593

REPOSITORIES: biostudies

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Chemical and biological properties of mycobactins isolated from various mycobacteria.

Project description:Nine different strains of mycobacteria grown on media deficient in iron all produced mycobactins. Most strains produced one mycobactin in great preponderance. Mycobacteria from clearly distinct taxonomic groups gave mycobactins differing in the structure of their nuclei. One group of taxonomically related mycobacteria produced mycobactins having the same nucleus but with different distributions of side chains within the homologous mixtures. Simple methods are described for identifying mycobactins on a small scale; these may be of value in classifying mycobacteria. Structures are proposed for mycobactin A from Mycobacterium aurum, mycobactin R from M. terrae, mycobactin F, produced together with mycobactin H by M. fortuitum, and mycobactins M and N from M. marinum. The first three of these differ from known mycobactins in details of substitution and configuration of asymmetric centres in the nucleus. Mycobactins M and N are substantially different, having only small acyl groups (acetyl and propionyl respectively) at the hydroxamic acid centre of the mycobactic acid moiety. Both are homologous mixtures having long-chain saturated 3-hydroxy-2-methyl acid fragments in the cobactin moiety. All mycobactins so far isolated promote almost maximal growth of M. johnei at 30ng./ml. in liquid medium. The activity of some mycobactins extends to much lower concentrations, mycobactin S showing significant growth promotion at 0.3ng./ml. Mycobactin M or N in combination with mycobactins having a long side chain in the mycobactic acid moiety exerts a mutually antagonistic effect on the growth of M. johnei, the mixture giving less growth than either mycobactin separately. Mycobactin M also decreases the growth of M. kansasii and M. tuberculosis on liquid media. These antagonistic effects are probably caused by a lengthening of the lag phase.

1969-01-01 | S-EPMC1185245 | BioStudies

Isolation and structure of mycobactin T, a growth factor from Mycobacterium tuberculosis.

Project description:1. A growth factor for Mycobacterium johnei has been isolated from Mycobacterium tuberculosis as an iron complex; it has been named ferric mycobactin T. 2. Ferric mycobactin T as isolated is a mixture of at least four closely related components differing only in their fatty acid side chains. 3. Mycobactin T resembles mycobactin P in structure but differs in the following respects: (a) the aromatic acid residue is salicylic acid in place of 2-hydroxy-6-methylbenzoic acid; (b) the hydroxy acid residue is (+)-beta-hydroxybutyric acid in place of (-)-3-hydroxy-2-methylpentanoic acid; (c) its components have fatty acid side chains that are mostly different from the side chains of the components in mycobactin P preparations. One minor component in mycobactin T has probably a cis-octadec-2-enoyl side chain. The major side-chain components correspond to acids of chain length C(18)-C(21) that are not n-saturated or n-Delta(2)-unsaturated acids. 4. The differences in biosynthesis between mycobactins T and P are discussed.

1965-01-01 | S-EPMC1264557 | BioStudies

The separation of the mycobactins from Mycobacterium smegmatis by using high-pressure liquid chromatography.

Project description:The family of mycobactins from Mycobacterium smegmatis were resolved into seven fractions by high-pressure liquid chromatography. This separation was by virtue of the differences in length and character of the long acyl substituents as shown by g.l.c. of the methyl esters of the isolated fatty acids from the fractions. As t.l.c. could also resolve the individual mycobactin fractions, it too must rely on the same differences to effect separation. As the lengths of the acyl chains were modulated by the growth conditions, a specific range of acyl groups may not be needed for mycobactin to function. This technique provides a simple means of rapidly characterizing crude mycobactins from all mycobacteria.

1978-01-01 | S-EPMC1186146 | BioStudies

Isolation of mycobactinss from various mycobacteria. The properties of mycobactin S and H.

Project description:Mycobactin S has been isolated from Mycobacterium smegmatis and from Mycobacterium sp. Olitzky & Gershon, strain 2, and mycobactin H from M. thermoresistible; all three organisms were grown on synthetic media of low iron content. These two mycobactins are mixtures of compounds having the same nucleus but differing in their fatty side chains. The nucleus of mycobactin S has a chemical structure identical with that of mycobactin T but differs in the optical configuration at the beta-carbon atom of the hydroxy acid fragment; the configuration in mycobactin S is S whereas that in mycobactin T is R (the previous assignment of this configuration was incorrect). The cobactin fragment of mycobactin H is identical with that of mycobactin S, but the mycobactic acid moiety differs in having methyl groups at position 6 in the benzene ring and at position 5 in the oxazoline ring. The configurations of all the asymmetric centres have been established for both mycobactins. Improved and simplified methods for the extraction and purification of mycobactins are described.

1969-01-01 | S-EPMC1187608 | BioStudies

Assay of the mycobactins by measurement of the growth of Mycobacterium johnei.

Project description:A method is described for the assay of mycobactin P and T by turbidimetric measurement of the growth of Mycobacterium johnei. The assay agrees satisfactorily with spectroscopic determination of the iron complexes. The growth curves with mycobactins P and T differ somewhat in form. An approximate ratio of activities has been determined.

1966-01-01 | S-EPMC1265090 | BioStudies

Early steps in the biosynthesis of mycobactins P and S.

Project description:1. Lysine is readily incorporated into mycobactins P and S. Incorporation is into the hydroxamic acid moieties only and is equal in the mycobactic acid and cobactin portions of the molecule. 2. 2-Amino-6-hydroxyaminohexanoic acid is not taken up by cells of Mycobacterium phlei and is not detectable in extracts of cells actively synthesizing mycobactin. 3. The most abundant material derived from lysine that can be detected in such cell extracts is an N(6)-acyl-lysine. Cells grown in the presence of iron contain markedly less of this material than do those grown under conditions of iron deficiency. 4. When added to growing cultures of M. phlei the N(6)-acyl-lysine is readily incorporated into mycobactin. 5. The hydroxy acid of cobactin P is derivable from propionate.

1970-01-01 | S-EPMC1179283 | BioStudies

Identification of mycobactins by nuclear-magnetic-resonance spectroscopy.

Project description:Details are given of the n.m.r. spectra of mycobactins F, H, M, N, P, S and T, and resonances are ascribed to all the protons in these molecules. A simplified system is described for identifying known mycobactins by the n.m.r. spectrum alone. This method will not distinguish mycobactins S and T, whose nuclei differ only in the configuration at an asymmetric centre.

1969-01-01 | S-EPMC1185246 | BioStudies

THE STRUCTURE OF MYCOBACTIN P, A GROWTH FACTOR FOR MYCOBACTERIUM JOHNEI, AND THE SIGNIFICANCE OF ITS IRON COMPLEX.

Project description:1. The growth factor from Mycobacterium phlei is now named mycobactin P to distinguish it from related but chemically distinct growth factors from other species of mycobacteria. It is shown to comprise four closely similar chemical entities differing only in the fatty side chain. 2. The structure of the main component (85%) of mycobactin P has been established and the absolute configuration of all asymmetric centres determined. 3. Ferric mycobactin P has been crystallized; its structure is discussed. 4. Evidence is given for regarding ferric mycobactin P as a member of the class of compounds known as sideramines, though the mycobactins are more specialized than other sideramines.

1965-01-01 | S-EPMC1206422 | BioStudies

Syntheses of mycobactin analogs as potent and selective inhibitors of Mycobacterium tuberculosis.

Project description:Three analogs of mycobactin T, the siderophore secreted by Mycobacterium tuberculosis (Mtb) were synthesized and screened for their antibiotic activity against Mtb H(37)Rv and a broad panel of Gram-positive and Gram-negative bacteria. The synthetic mycobactins were potent (MIC(90) 0.02-0.88 ?M in 7H12 media) and selective Mtb inhibitors, with no inhibitory activity observed against any other of the microorganisms tested. The maleimide-containing analog 40 represents a versatile platform for the development of mycobactin-drug conjugates, as well as other applications.

2012-01-01 | S-EPMC3482464 | BioStudies

Purification, crystallization and preliminary X-ray studies of MbtN (Rv1346) from Mycobacterium tuberculosis.

Project description:In Mycobacterium tuberculosis, the protein MbtN (Rv1346) catalyzes the formation of a double bond in the fatty-acyl moiety of the siderophore mycobactin, which is used by this organism to acquire essential iron. MbtN is homologous to acyl-CoA dehydrogenases, whose general role is to catalyze the ?,?-dehydrogenation of fatty-acyl-CoA conjugates. Mycobactins, however, contain a long unsaturated fatty-acid chain with an unusual cis double bond conjugated to the carbonyl group of the mycobactin core. To characterize the role of MbtN in the dehydrogenation of this fatty-acyl moiety, the enzyme has been expressed, purified and crystallized. The crystals diffracted to 2.3 Å resolution at a synchrotron source and were found to belong to the hexagonal space group H32, with unit-cell parameters a = b = 139.10, c = 253.09 Å, ? = ? = 90, ? = 120°.

2013-01-01 | S-EPMC3855718 | BioStudies

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