Screening for Biomarkers of Actinobacteria Associated with Water-Damaged Buildings – Part 1

Main Article Content

Ryan Shoemaker D Lark

Abstract

Recent publications 1,2 have presented the view that a wider variety of microbial contaminants are responsible for adverse human health effects in susceptible individuals exposed to the microbial “soup” that results in water-damaged buildings (WDB) than previously ascribed.


Those articles presented an in-depth understanding of the expanded use of Next Generation Sequencing (NGS) to detect the bacterial taxa present in these affected environments. When correlated with data from transcriptomic assays, these studies defined specific causation of innate immune activation by a growing list of microbial colonizers. Specifically, it was reported that a correlation existed between certain Actinobacteria as shown by NGS, with differential gene activation, from a transcriptomic assay (GENIE) detecting a defined clinical response.


This review seeks to assess the published literature to find and determine the potential for candidates that could be relied upon to act as a biomarker for Actinobacteria in dust and other samples in order to indicate the likelihood of Actinobacteria dominance or prevalence, sufficient to warrant progression to confirmation by NGS, much like endotoxins are broadly accepted as a biomarker for colonization by broad spectra of Gram-negative bacilli in WDB.

Article Details

How to Cite
SHOEMAKER, Ryan; LARK, D. Screening for Biomarkers of Actinobacteria Associated with Water-Damaged Buildings – Part 1. Medical Research Archives, [S.l.], v. 10, n. 1, jan. 2022. ISSN 2375-1924. Available at: <https://esmed.org/MRA/mra/article/view/2646>. Date accessed: 14 aug. 2022. doi: https://doi.org/10.18103/mra.v10i1.2646.
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Review Articles

References

1 Shoemaker R, et al. Exposure to Actinobacteria resident in water-damaged buildings and resultant immune injury found n Chronic Inflammatory Response Syndrome. Medical Research Archives 2021; 9(11).
2 Shoemaker R, et al. Newer Molecular Methods Bring New Insights into Human- and Building- Health Risk Assessments from Water- Damaged Buildings: Defining Exposure and Reactivity, the Two Sides of Causation of CIRS-WDB Illness. Medical Research Archives 2021; 9(3): 1- 36.
3 Ikeda T, et al - Usefulness of the endotoxin activity assay as a biomarker to assess the severity of endotoxemia in critically ill patients. Innate Immun. 2014 Nov;20(8):881-7.
4 Gago G, Diacovich L, Arabolaza A, Tsai SC, Gramajo H. Fatty acid biosynthesis in actinomycetes. FEMS Microbiol Rev. 2011;35(3):475-497
5 Daffe M, Draper P. The envelope layers of mycobacteria with reference to their pathogenicity. Adv Microb Physiol. 1998; 39:131–203.
6 Collins MD, Goodfellow M, Minnikin DE. Fatty acid composition of some mycolic acid-containing coryneform bacteria. J Gen Microbiol. 1982; 128:2503–2509.
7 Minnikin DE & Goodfellow M. Lipid composition in the classification and identification of acid-fast bacteria. Soc Appl Bacteriol Symp Ser. 1980; 8:189–256.
8 Gebhardt H, et al. The key role of the mycolic acid content in the functionality of the cell wall permeability barrier in Corynebacterineae. Microbiology. 2007; 153:1424–1434
9 Liu J, et al. Mycolic acid structure determines the fluidity of the mycobacterial cell wall. J Biol Chem. 1996; 271:29545–29551.
10 Astarie-Dequeker C, et al. Phthiocerol dimycocerosates of M. tuberculosis participate in macrophage invasion by inducing changes in the organization of plasma membrane lipids. PLoS Pathog. 2009;5: e1000289
11 Camacho LR, et al. identification of a virulence gene cluster of Mycobacterium tuberculosis by signature-tagged transposon mutagenesis. Mol Microbiol. 1999; 34:257–267.
12 Cox JS, et al. Complex lipid determines tissue-specific replication of Mycobacterium tuberculosis in mice. Nature. 1999; 402:79–83.
13 Onwueme KC, et al. The dimycocerosate ester polyketide virulence factors of mycobacteria. Prog Lipid Res. 2005; 44:259–302.
14 Sirakova TD, et al. The M. tuberculosis pks2 gene encodes the synthase for the hepta- and octamethyl-branched fatty acids required for sulfolipid synthesis. J Biol Chem. 2001; 276:16833–16839.
15 Trivedi OA, et al. Dissecting the mechanism and assembly of a complex virulence mycobacterial lipid. Mol Cell. 2005; 17:631–643.
16 Arabolaza A, et al. Multiple pathways for triacylglycerol biosynthesis in Streptomyces coelicolor. Appl Environ Microbiol. 2008; 74:2573–2582.
17 Daniel J, et al. Induction of a novel class of diacylglycerol acyltransferases and triacylglycerol accumulation in Mycobacterium tuberculosis as it goes into a dormancy-like state in culture. J Bacteriol. 2004; 186:5017–5030. [
18 De Rosa M, et al.A. Structure, biosynthesis, and physicochemical properties of archaebacterial lipids. Microbiol Rev. 1986; 50:70–80.
19 Alberts AW, et al. Acetyl CoA carboxylase, II. Demonstration of biotin-protein and biotin carboxylase subunits. Proc Natl Acad Sci U S A. 1969; 63:1319–1326
20 Greenspan MD, Alberts AW, Vagelos PR. Acyl carrier protein. 13. Beta-ketoacyl acyl carrier protein synthetase from Escherichia coli. J Biol Chem. 1969; 244:6477–6485.
21 Odriozola JM, et al. Fatty acid synthetase activity in Mycobacterium smegmatis. Characterization of the acyl carrier protein-dependent elongating system. Biochim Biophys Acta. 1977; 488:207–217
22 Pugh EL et al. Studies on the mechanism of fatty acid synthesis. 13. The role of beta-hydroxy acids in the synthesis of palmitate and cis vaccenate by the Escherichia coli enzyme system. J Biol Chem. 1966; 241:2635–2643.
23 Toomey RE, Wakil SJ. Studies on the mechanism of fatty acid synthesis. XVI. Preparation and general properties of acyl-malonyl acyl carrier protein-condensing enzyme from Escherichia coli. J Biol Chem. 1966; 241:1159–1165
24 Kremer L, et al Biochemical characterization of acyl carrier protein (AcpM) and malonyl-CoA: AcpM transacylase (mtFabD), two major components of Mycobacterium tuberculosis fatty acid synthase II. J Biol Chem. 2001; 276:27967–27974.
25 Schaeffer et al. Purification and biochemical characterization of the Mycobacterium tuberculosis beta-ketoacyl-acyl carrier protein synthases KasA and KasB. J Biol Chem. 2001; 276:47029–47037.
26 Banerjee A, et al - inhA, a gene encoding a target for isoniazid and ethionamide in Mycobacterium tuberculosis. Science. 1994; 263:227–230.
27 Quemard A, et al. Enzymatic characterization of the target for isoniazid in Mycobacterium tuberculosis. Biochemistry. 1995; 34:8235–8241.
28 Cohen-Gonsaud M, et al. Crystal structure of MabA from Mycobacterium tuberculosis, a reductase involved in long-chain fatty acid biosynthesis. J Mol Biol. 2002; 320:249–261.
29 Marrakchi H, et al. MabA (FabG1), a Mycobacterium tuberculosis protein involved in the long-chain fatty acid elongation system FAS-II. Microbiology. 2002; 148:951–960.
30 Blanchard CZ, et al. Inhibition of biotin carboxylase by a reaction intermediate analog: implications for the kinetic mechanism. Biochem Biophys Res Commun. 1999a; 266:466–471.
31 Blanchard CZ, et al. The biotin domain peptide from the biotin carboxyl carrier protein of Escherichia coli acetyl-CoA carboxylase causes a marked increase in the catalytic efficiency of biotin carboxylase and carboxyltransferase relative to free Biotin. J Biol Chem. 1999b; 274:31767–31769.
32 Janiyani K, Bordelon T, Waldrop GL, Cronan JE., Jr Function of Escherichia coli biotin carboxylase requires catalytic activity of both subunits of the homodimer. J Biol Chem. 2001; 276:29864–29870
33 Levert KL, Lloyd RB, Waldrop GL. Does cysteine 230 and lysine 238 of biotin carboxylase play a role in the activation of Biotin? Biochemistry. 2000; 39:4122–4128.
34 Waldrop GL, Rayment I, Holden HM. Three-dimensional structure of the biotin carboxylase subunit of acetyl-CoA carboxylase. Biochemistry. 1994; 33:10249–10256.
35 Athappilly FK, Hendrickson WA. Structure of the biotinyl domain of acetyl-coenzyme A carboxylase determined by MAD phasing. Structure. 1995; 3:1407–1419.
36 Cronan JE, Rock CO. Biosynthesis of membrane lipids. In: Neidhardt F, editor. Escherichia coli and Salmonella typhimurium Cellular and Molecular Biology. Washington, DC: ASM Press; 1996. pp. 612–636
37 Reddy DV, Shenoy BC, Carey PR, Sonnichsen FD. High resolution solution structure of the 1.3S subunit of transcarboxylase from Propionibacterium shermanii. Biochemistry. 2000; 39:2509–2516.
38 Roberts EL, et al Solution structures of apo and holo biotinyl domains from acetyl coenzyme A carboxylase of Escherichia coli determined by triple-resonance nuclear magnetic resonance spectroscopy. Biochemistry. 1999; 38:5045–5053.
39 Yao X, et al. structure of the carboxy-terminal fragment of the apo-biotin carboxyl carrier subunit of Escherichia coli acetyl-CoA carboxylase. Biochemistry. 1997; 36:15089–15100.
40 Diacovich L, et al. Kinetic and structural analysis of a new group of Acyl-CoA carboxylases found in Streptomyces coelicolor A3(2) J Biol Chem. 2002;277:31228–31236.
41 Gago G, et al. Biochemical and structural characterization of an essential acyl coenzyme A carboxylase from Mycobacterium tuberculosis. J Bacteriol. 2006; 188:477–486.
42 Gande R, et al. Acyl-CoA carboxylases (accD2 and accD3), together with a unique polyketide synthase (Cg-pks), are key to mycolic acid biosynthesis in Corynebacterianeae such as Corynebacterium glutamicum and Mycobacterium tuberculosis.
J Biol Chem. 2004; 279:44847–44857.
43 Gande R, et al. The two carboxylases of Corynebacterium glutamicum essential for fatty acid and mycolic acid synthesis.
J Bacteriol. 2007; 189:5257–5264
44 Oh TJ, et al. Identification and characterization of Rv3281 as a novel subunit of a biotin-dependent acyl-CoA Carboxylase in Mycobacterium tuberculosis H37Rv. J Biol Chem. 2006;281:3899–3908
45 Bramwell H, et al. Propionyl-CoA carboxylase from Streptomyces coelicolor A3(2): cloning of the gene encoding the biotin-containing subunit. Microbiology. 1996; 142:649–655.
46 Diacovich L, Mitchell DL, Pham H, Gago G, Melgar MM, Khosla C, Gramajo H, Tsai SC. Crystal structure of the beta-subunit of acyl-CoA carboxylase: structure-based engineering of substrate specificity. Biochemistry. 2004; 43:14027–14036.
47 Rodriguez E, Gramajo H. Genetic and biochemical characterization of the alpha and beta components of a propionyl-CoA carboxylase complex of Streptomyces coelicolor A3(2) Microbiology. 1999;145(145):3109–3119.
48 Rodriguez E, et al. role of an essential acyl coenzyme A carboxylase in the primary and secondary metabolism of Streptomyces coelicolor A3(2) Appl Environ Microbiol. 2001; 67:4166–4176.
49 Cole ST, Brosch R, Parkhill J, et al. Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature. 1998; 393:537–544.
50 Sassetti CM, Boyd DH, Rubin EJ. Comprehensive identification of conditionally essential genes in mycobacteria. Proc Natl Acad Sci U S A. 2001; 98:12712–12717.
51 Sassetti CM, Rubin EJ. Genetic requirements for mycobacterial survival during infection. Proc Natl Acad Sci U S A. 2003; 100:12989–12994.
52 Portevin D, et al. The acyl-AMP ligase FadD32 and AccD4-containing acyl-CoA carboxylase is required for the synthesis of mycolic acids and essential for mycobacterial growth: identification of the carboxylation product and determination of the acyl-CoA carboxylase components. J Biol Chem. 2005; 280:8862–8874.
53 Trivedi OA, et al. Dissecting the mechanism and assembly of a complex virulence mycobacterial lipid. Mol Cell. 2005; 17:631–643.
54 Hall PR, et al. Transcarboxylase 12S crystal structure: hexamer assembly and substrate binding to a multienzyme core. EMBO J. 2003; 22:2334–2347.
55 Xiang S, Tong L. Crystal structures of human and Staphylococcus aureus pyruvate carboxylase and molecular insights into the carboxyl transfer reaction. Nat Struct Mol Biol. 2008; 15:295–302.
56 Yu LP, Xiang S, Lasso G, Gil D, Valle M, Tong L. A symmetrical tetramer for S. aureus pyruvate carboxylase in complex with coenzyme A. Structure. 2009; 17:823
57 Wendt KS, Schall I, Huber R, Buckel W, Jacob U. Crystal structure of the carboxyltransferase subunit of the bacterial sodium ion pump glutaconyl-coenzyme A decarboxylase. EMBO J. 2003; 22:3493–3502.
58 Zhang H, Yang Z, Shen Y, Tong L. Crystal structure of the carboxyltransferase domain of acetyl-coenzyme A carboxylase. Science. 2003; 299:2064–2067
59 Minnikin DE, Goodfellow M. Lipid composition in the classification and identification of acid-fast bacteria. Soc Appl Bacteriol Symp Ser. 1980; 8:189–256.
60 Takayama K, Wang C, Besra GS. Pathway to synthesis and processing of mycolic acids in Mycobacterium tuberculosis.
Clin Microbiol Rev. 2005; 18:81–101.
61 Gronwald JW. Herbicides inhibiting acetyl-CoA carboxylase. Biochem Soc Trans. 1994; 22:616–621.
62 Heath RJ, White SW, Rock CO. Lipid biosynthesis as a target for antibacterial agents. Prog Lipid Res. 2001; 40:467–497.
63 Pacheco-Alvarez D, Solorzano-Vargas RS, Del Rio AL. Biotin in metabolism and its relationship to human disease. Arch Med Res. 2002; 33:439–447. [
64 Shen Y, Volrath SL, Weatherly SC, Elich TD, Tong L. A mechanism for the potent inhibition of eukaryotic acetyl-coenzyme A carboxylase by soraphen A, a macrocyclic polyketide natural product. Mol Cell. 2004; 16:881–891.
65 Tong L. Acetyl-coenzyme A carboxylase: crucial metabolic enzyme and attractive target for drug discovery. Cell Mol Life Sci. 2005; 62:1784–1803.
66 Tong L, Harwood HJ., Jr Acetyl-coenzyme A carboxylases: versatile targets for drug discovery. J Cell Biochem. 2006; 99:1476–1488.
67 Freiberg C, et al. identification and characterization of the first class of potent bacterial acetyl-CoA carboxylase inhibitors with antibacterial activity. J Biol Chem. 2004; 279:26066–26073.
68 Pohlmann J, et al. Pyrrolidinedione derivatives as antibacterial agents with a novel mode of action. Bioorg Med Chem Lett. 2005; 15:1189–1192. [
69 Chen J, et al, A public database of small molecules and related chemoinformatics resources. Bioinformatics. 2005; 21:4133–4139.
70 Lin TW, et al. Structure-based inhibitor design of AccD5, an essential acyl-CoA carboxylase carboxyltransferase domain of Mycobacterium tuberculosis. Proc Natl Acad Sci U S A. 2006; 103:3072–3077.
71 Cronan JE, Jr, Subrahmanyam S. FadR, transcriptional co-ordination of metabolic expediency. Mol Microbiol. 1998; 29:937–943.
72 DiRusso CC, Nystrom T. The fats of Escherichia coli during infancy and old age: regulation by global regulators, alarmones and lipid intermediates. Mol Microbiol. 1998; 27:1–8.
73 Rock CO, Cronan JE. Escherichia coli as a model for the regulation of dissociable (type II) fatty acid biosynthesis. Biochim Biophys Acta. 1996; 1302:1–16
74 Zhang YM, White SW, Rock CO. Inhibiting bacterial fatty acid synthesis. J.Biol.Chem. 2006;281:17541–17544
75 Lu YJ, Rock CO. Transcriptional regulation of fatty acid biosynthesis in Streptococcus pneumoniae. Mol Microbiol. 2006; 59:551–566.
76 Schujman GE, Paoletti L, Grossman AD, de Mendoza D. FapR, a bacterial transcription factor involved in global regulation of membrane lipid biosynthesis. Dev Cell. 2003; 4:663–672.
77 Schujman GE, Guerin M, Buschiazzo A, Schaeffer F, Llarrull LI, Reh G, Vila AJ, Alzari PM, de Mendoza D. Structural basis of lipid biosynthesis regulation in Gram-positive bacteria. EMBO J. 2006; 25:4074–4083.
78 Schujman GE, de Mendoza D. Regulation of type II fatty acid synthase in Gram-positive bacteria. Curr Opin Microbiol. 2008; 11:148–152.
79 Zhang YM, Rock CO. Transcriptional regulation in bacterial membrane lipid synthesis. J Lipid Res. 2009;50 Suppl: S115–S119.
80 Arabolaza A, D'Angelo M, Comba S, Gramajo H. FasR, a novel class of transcriptional regulator, governs the activation of fatty acid biosynthesis genes in Streptomyces coelicolor. Mol Microbiol. 2010a; 78:47–63.
81 Salzman V, et al. Transcriptional regulation of lipid homeostasis in mycobacteria. Mol Microbiol. 2010; 78:64–77.
82 Butler WR, Guthertz LS. Mycolic acid analysis by high-performance liquid chromatography for identification of Mycobacterium species. Clin Microbiol Rev. 2001;14(4):704-726.
83 Kubica G P. Differential identification of mycobacteria. VII. Key features for identification of clinically significant mycobacteria. Am Rev Respir Dis. 1973; 107:9–21
84 Kubica G P. Classification and nomenclature of the mycobacteria. Ann Microbiol (Inst Pasteur) 1978; 129:7–12
85 Kubica G P. Clinical microbiology. In: Kubica G P, Wayne L G, editors. The mycobacteria: a sourcebook. New York, N.Y: Marcel Dekker, Inc; 1984. pp. 133–175
86 Runyon E H. Anonymous mycobacteria in pulmonary disease. Med Clin North Am. 1959; 43:273–290
87 Timpe A, Runyon E H. The relationship of “atypical” acid-fast bacteria to human disease. J Lab Clin Med. 1954; 44:202–209
88 Goodfellow M, Minnikin D E. Circumscription of the genus. In: Kubica G P, Wayne L G, editors. The mycobacteria: a sourcebook. New York, N.Y: Marcel Dekker, Inc; 1984. pp. 1–24.
89 Wayne L G. Mycobacterial speciation. In: Kubica G P, Wayne L G, editors. The mycobacteria: a sourcebook. New York, N.Y: Marcel Dekker, Inc; 1984. pp. 25–65.
90 Wayne L G, et al. Highly reproducible techniques for use in systematic bacteriology in the genus Mycobacterium: tests for pigment, urease, resistance to sodium chloride, hydrolysis of Tween 80 and β-galactosidase. Int J Syst Bacteriol. 1974; 24:412–419.
91 Wayne L G, et al. Highly reproducible techniques for use in systematic bacteriology in the genus Mycobacterium: tests for niacin and catalase and for resistance to isoziazid, thiophene 2-carboxylic hydrazide, hydroxylamine and p-nitrobenzoate. Int J Syst Bacteriol. 1976; 26:311–318.
92 Raman K, Rajagopalan P, Chandra N. Flux balance analysis of mycolic acid pathway: targets for anti-tubercular drugs. PLoS Comput Biol. 2005;1(5): e46.
93 Molecular Genetic Methods
94 Wayne L G. Mycobacterial speciation. In: Kubica G P, Wayne L G, editors. The mycobacteria: a sourcebook. New York, N.Y: Marcel Dekker, Inc; 1984. pp. 25–65.
95 Wayne L G, et al Highly reproducible techniques for use in systematic bacteriology in the genus Mycobacterium: tests for pigment, urease, resistance to sodium chloride, hydrolysis of Tween 80 and β-galactosidase. Int J Syst Bacteriol. 1974; 24:412–419.
96 Wayne L G et al. Highly reproducible techniques for use in systematic bacteriology in the genus Mycobacterium: tests for niacin and catalase and for resistance to isoziazid, thiophene 2-carboxylic hydrazide, hydroxylamine and p-nitrobenzoate. Int J Syst Bacteriol. 1976; 26:311–318.
97 Wayne L G et al. Sematide - and chemotaxonomy-based analyses of some problematic phenotypic clusters of slowly growing mycobacteria: a cooperative study of the International Working Group on Mycobacterial Taxonomy. Int J Syst Bacteriol. 1996; 46:280–297
98 Wayne L G, et al. Serovar determination and molecular taxonomic correlation in Mycobacterium avium, Mycobacterium intracellulare, and Mycobacterium scrofulaceum: a cooperative study of the International Working Group on Mycobacterial Taxonomy. Int J Syst Bacteriol. 1993; 43:482–489.
99 Wolinsky E. Nontuberculous mycobacteria and associated diseases. In: Kuciba G P, Wayne L G, editors. The mycobacteria: a sourcebook. New York, N.Y: Marcel Dekker, Inc; 1984. pp. 1141–1207.
100 Butler WR, Guthertz LS. Mycolic acid analysis by high-performance liquid chromatography for identification of Mycobacterium species. Clin Microbiol Rev. 2001;14(4):704-726.
101 Dixon P F, Stoll M S, Lim C K. High pressure liquid chromatography in clinical chemistry. Ann Clin Biochem. 1976; 13:409–432.
102 Gerson B. HPLC monitoring improves drug therapy. Lab World. 1981; 1:43–45.
103 Horváth C. High-performance liquid chromatography: advances and perspectives. New York, N.Y: Academic Press, Inc.; 1980.
104 Kent P T, Kubica G P. Public health mycobacteriology: a guide for the level III laboratory. Atlanta, Ga: Centers for Disease Control, USS Department of Health and Human Services; 1985.
105 Shinnick T M, Good R C. Diagnostic mycobacteriology laboratory practices. Clin Infect Dis. 1995; 21:291–299.
106 Butler W R, Jost K C, Jr, Kilburn J O. Identification of mycobacteria by high-performance liquid chromatography. J Clin Microbiol. 1991; 29:2468–2472
107 Cage G D. Direct identification of Mycobacterium species in BACTEC 7H12B medium by use of high-performance liquid chromatography. J Clin Microbiol. 1994; 32:521–524.
108 Dünges W. 4-Bromomethyl-7-methoxycoumarin as a new fluorescence label for fatty acids. Anal Chem. 1977; 49:442–445.
109 Guthertz L S, Lim S D, Jang Y, Duffey P S. Curvilinear-gradient high-performance liquid chromatography for identification of mycobacteria. J Clin Microbiol. 1993; 31:1876–1881.
110 Jost K C, et al. Identification of Mycobacterium tuberculosis and M. avium complex directly from smear-positive sputum specimens and Bactec 12B cultures by high-performance liquid chromatography with fluorescence detection and computer-driven pattern recognition models. J Clin Microbiol. 1995; 33:1270–1277.
111 Thibert L, LaPierre S. Routine application of high-performance liquid chromatography for identification of mycobacteria. J Clin Microbiol. 1993; 31:1759–1763.
112 Tortoli E, et al. High-performance liquid chromatography for identification of mycobacterial species rarely encountered in clinical laboratories. Eur J Clin Microbiol Infect Dis. 1995; 14:240–243.
113 Kanetsuna F. Chemical analyses of mycobacterial cell walls. Biochim Biophys Acta. 1968; 158:130–143.
115 Lechevalier M P, Horan A C, Lechevalier H. Lipid composition in the classification of nocardiae and mycobacteria. J Bacteriol. 1971; 105:313–318.
116 Embley T M, Stackebrandt E. The molecular phylogeny and systematics of the actinomycetes. Annu Rev Microbiol. 1994; 48:257–289.
117 Goodfellow M, Minnikin D E. Circumscription of the genus. In: Kubica G P, Wayne L G, editors. The mycobacteria: a sourcebook. New York, N.Y: Marcel Dekker, Inc; 1984. pp. 1–24.
118 Kanetsuna F, Bartoli A. A simple chemical method to differentiate Mycobacterium from Nocardia. J Gen Microbiol. 1972; 70:209–212.
119 Minnikin D E, Goodfellow M. Lipid composition in the classification and identification of acid-fast bacteria. In: Goodfellow M, Board R G, editors. Microbiological classification and identification. London, United Kingdom: Academic Press, Ltd.; 1980. pp. 189–256.
120 Alshamaony L, Goodfellow M, Minnikin D E. Free mycolic acids as criteria in the classification of Nocardia and the “rhodochrous” complex. J Gen Microbiol. 1976; 92:188–199.
121 Etémadi A-H. The use of pyrolysis gas chromatography and mass spectroscopy in the study of the structure of mycolic acids. J Gas Chromatogr. 1967; 5:447–456.
122 Lechevalier M P, Horan A C, Lechevalier H. Lipid composition in the classification of nocardiae and mycobacteria. J Bacteriol. 1971; 105:313–318.
123 Lanéelle G. Nature des acides mycoliques de Mycobacterium paratuberculosis : application de la chromatographie sur couche mince à leur fractionnement. C R Hebd Sciences Acad Sci Paris. 1963; 257:781–783.
124 Minnikin D E, Alshamaony L, Goodfellow M. Differentiation of Mycobacterium, Nocardia, and related taxa by thin-layer chromatographic analysis of whole-organism methanolysates. J Gen Microbiol. 1975; 88:200–204.
125 Minnikin D E, et al, Analysis of mycobacteria mycolic acids. In: Klein R, Schmitz B, editors. Topics in lipid research: from structural elucidation to biological function. London, United Kingdom: Royal Society of Chemistry; 1986. pp. 139–143.
126 Qureshi N, et al. analysis of the purified components of a new homologous series of α-mycolic acids from Mycobacterium tuberculosis H37Ra. J Biol Chem. 1978;253:5411–5417.
127 Steck P A, Schwartz B A, Rosendahl M S, Gray G R. Mycolic acids: a reinvestigation. J Biol Chem. 1978; 253:5625–5629.
128 Takayama K, Qureshi N, Jordi H C, Schnoes H K. Separation of homologous series of mycolic acids from Mycobacterium tuberculosis H37Ra by high performance liquid chromatography. Chromatogr Sci. 1979; 10:91–101.
129 Pei P T, Kossa W C, Ramachandran S, Henly R S. High pressure reverse phase liquid chromatography of fatty acid p-bromophenacyl esters. Lipids 11:814–816
130 Wong M Y H, Steck P A, Gray G R. The major mycolic acids of Mycobacterium smegmatis: characterization of their homologous series. J Biol Chem. 1979; 254:5734–5740.
131 Takayama K, Jordi H C, Benson F. Separation of fatty acids as their p-bromophenacyl esters on a C30-bonded silica column by high performance liquid chromatography. J Liq Chromatogr. 1980; 3:61–69.
132 Borch R F. Separation of long chain fatty acids as phenacyl esters by high pressure liquid chromatography. Anal Chem. 1975; 47:2437–2439.
133 Durst H D, Milano M, Kikta E J, Jr, Connelly S A, Grushka E. Phenacyl esters of fatty acids via crown ether catalysts for enhanced ultraviolet detection in liquid chromatography. Anal Chem. 1975; 47:1797–1801.
134 Jordi H C. Separation of long and short chain fatty acids as naphthacyl and substituted phenacyl esters by high performance liquid chromatography. J Liquid Chromatogr. 1978; 1:215–230.
135 Roggero J P, Coen S V. Isocratic separation of fatty acid derivatives by reversed phase liquid chromatography. Influence of the solvent on selectivity and rules for elution order. J Liquid Chromatogr. 1981; 4:1817–1829.
136 Baba T, et al. Thermally adaptive changes of mycolic acids in Mycobacterium smegmatis. J Biochem. 1989; 106:81–86.
137 Toriyama et al. Regulation of cell wall mycolic acid biosynthesis in acid-fast bacteria. I. Temperature-induced changes in mycolic acid molecular species and related compounds in Mycobacterium phlei. J Biochem. 1980; 88:211–221
138 Tamoutounour S, Han S, Deckers J, Constantinides M, Belkaid Y, et.al. Keratinocyte-intrinsic MHCII expression controls microbiota-induced Th1 cell responses. PNAS 2019; 116: 23643- 23652.
139 Harrison O, Linehan J, Shih H, Bouladoux N, Han S, Belkaid Y, et.al. Commensal-specific T cell plasticity promotes rapid tissue adaptation to injury. Science 2019; 363: doi: 10.1126/science. aat6280
140 Hurabielle C, Link V, Bouladoux N, Belkaid Y, et.al. Immunity to commensal skin fungi promotes psoriasiform skin inflammation. PNAS 2020; 117: 16465- 16474