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Chapter 18 : Structure, Biosynthesis, and Genetics of the Mycolic Acid-Arabinogalactan-Peptidoglycan Complex

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Structure, Biosynthesis, and Genetics of the Mycolic Acid-Arabinogalactan-Peptidoglycan Complex, Page 1 of 2

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Abstract:

The cell envelope of is made up of three major components: a plasma membrane; a covalently linked complex of mycolic acid-arabinogalactan-peptidoglycan complex (MAPc); and a polysaccharide-rich capsule-like layer. It is felt that knowledge of the biosynthesis and genetics of this aspect of the cell wall biogenesis may provide insight into overall cell wall architecture, particularly the relationship between its soluble components and the insoluble MAPc. PG biosynthesis in can be divided into three stages based on subcellular localization. Of the other enzymes related to UDP-MurNAcpentapeptide synthesis in mycobacteria, the D-alanine racemase and D-alanine:D-alanine ligase from have been studied. Analysis of the genome of reveals the presence of a repertoire of putative penicillin binding proteins (PBPs), of which only a few have been characterized. The arabinogalactan (AG) biosynthetic pathway has been investigated mainly in and . The arabinofuranose (Araf ) residues of arabinan are added to the linker unit-galactan polymer from a decaprenylphosphoryl-Araf (DPA) precursor. The ligation of arabinogalactan (AG) to peptidoglycan (PG) has been demonstrated in experiments with cell-free preparations of , and the nature of in vitro-synthesized material was confirmed by the observation that the newly ligated AG can be released from PG by muramidase treatment.

Citation: Mahapatra S, Brennan P, Crick D, Basu J. 2005. Structure, Biosynthesis, and Genetics of the Mycolic Acid-Arabinogalactan-Peptidoglycan Complex, p 275-286. In Cole S, Eisenach K, McMurray D, Jacobs, Jr. W (ed), Tuberculosis and the Tubercle Bacillus. ASM Press, Washington, DC. doi: 10.1128/9781555817657.ch18

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Bacterial Genetics
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Mycobacterium tuberculosis
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Bacterial Cell Wall
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Mycobacterium leprae
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Figures

Image of Figure 1
Figure 1

Structure of a representative monomer of mycobacterial PG prior to peptide trimming. R1, N-glycolylmuramic acid residue of another monomer; R2, -acetylglucosamine residue of another monomer; R3, H or the linker unit of AG; R4, OH, NH2 or glycine; R5, OH or NH2; R6, H, or cross-linked to penultimate -Ala or to the -center of another meso-DAP residue; R7, OH or NH2.

Citation: Mahapatra S, Brennan P, Crick D, Basu J. 2005. Structure, Biosynthesis, and Genetics of the Mycolic Acid-Arabinogalactan-Peptidoglycan Complex, p 275-286. In Cole S, Eisenach K, McMurray D, Jacobs, Jr. W (ed), Tuberculosis and the Tubercle Bacillus. ASM Press, Washington, DC. doi: 10.1128/9781555817657.ch18
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Image of Figure 2
Figure 2

Schematic illustration of the cell wall AG and the Rhap-GlcNAc linker.

Citation: Mahapatra S, Brennan P, Crick D, Basu J. 2005. Structure, Biosynthesis, and Genetics of the Mycolic Acid-Arabinogalactan-Peptidoglycan Complex, p 275-286. In Cole S, Eisenach K, McMurray D, Jacobs, Jr. W (ed), Tuberculosis and the Tubercle Bacillus. ASM Press, Washington, DC. doi: 10.1128/9781555817657.ch18
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Figure 3

(A) Biosynthetic pathway leading to the formation of lipid II in E. coli. (B) Structure of lipid II from E. coli.

Citation: Mahapatra S, Brennan P, Crick D, Basu J. 2005. Structure, Biosynthesis, and Genetics of the Mycolic Acid-Arabinogalactan-Peptidoglycan Complex, p 275-286. In Cole S, Eisenach K, McMurray D, Jacobs, Jr. W (ed), Tuberculosis and the Tubercle Bacillus. ASM Press, Washington, DC. doi: 10.1128/9781555817657.ch18
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Figure 4

Hypothetical organization of the cell division apparatus of M. tuberculosis. FtsZ (Z) interacts with FtsW (W) through the C-tails of both proteins, thereby anchoring FtsZ to the membrane. FtsW is predicted to play a central role by linking cell division to PG biosynthesis through interactions with PBP1* (1*) and PBP3 (I). A putative FtsQ (Q) has also been identified. Its function is not yet known.

Citation: Mahapatra S, Brennan P, Crick D, Basu J. 2005. Structure, Biosynthesis, and Genetics of the Mycolic Acid-Arabinogalactan-Peptidoglycan Complex, p 275-286. In Cole S, Eisenach K, McMurray D, Jacobs, Jr. W (ed), Tuberculosis and the Tubercle Bacillus. ASM Press, Washington, DC. doi: 10.1128/9781555817657.ch18
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Figure 5

Schematic representation of AG biosynthesis and ligation to PG in mycobacteria.

Citation: Mahapatra S, Brennan P, Crick D, Basu J. 2005. Structure, Biosynthesis, and Genetics of the Mycolic Acid-Arabinogalactan-Peptidoglycan Complex, p 275-286. In Cole S, Eisenach K, McMurray D, Jacobs, Jr. W (ed), Tuberculosis and the Tubercle Bacillus. ASM Press, Washington, DC. doi: 10.1128/9781555817657.ch18
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Tables

Generic image for table
Table 1

The putative penicillin binding proteins of

Citation: Mahapatra S, Brennan P, Crick D, Basu J. 2005. Structure, Biosynthesis, and Genetics of the Mycolic Acid-Arabinogalactan-Peptidoglycan Complex, p 275-286. In Cole S, Eisenach K, McMurray D, Jacobs, Jr. W (ed), Tuberculosis and the Tubercle Bacillus. ASM Press, Washington, DC. doi: 10.1128/9781555817657.ch18

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