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Chapter 6 : Cell Wall-Anchored Surface Proteins and Lipoproteins of Gram-Positive Bacteria

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Abstract:

The cell wall envelope of gram-positive bacteria is composed of the peptidoglycan macromolecule that functions to protect microbes from osmotic lysis. Small molecules can diffuse through the peptidoglycan layer; however, cellular uptake requires dedicated mechanisms for transport across the cytoplasmic membrane. These and other functions in gram-positive bacteria require lipoproteins, polypeptides that are tethered to the cytoplasmic membrane by an N-terminal lipid modification. This chapter summarizes what is known about the cell wall-anchored surface proteins as well as the targeting mechanism of lipoproteins. Furthermore, some of the many biological functions that these polypeptides fulfill are described. Cell wall sorting signals from surface proteins of other gram-positive bacteria display similar functions. Gram-positive bacteria cannot recycle degraded peptidoglycan fragments and release these compounds into the extracellular medium. A database search using the lipobox of lipoproteins revealed 114 lipoprotein genes in the genome of as compared with 89 lipoproteins encoded in the genome. Several proteins that are periplasmic carbohydrate binding proteins in gram-negative bacteria were observed to be lipid-modified in gram-positive bacteria. These lipoproteins function to capture specific import substrates and deliver them to the membrane-embedded transport machinery. Several lipoproteins are required for sporulation or geimination of , while the PrsA lipoprotein is a peptidyl-prolyl isomerase that assists the folding of secreted polypeptides. Other lipoproteins are thought to be involved in DNA binding or uptake, oxidative phosphorylation, cell wall biogenesis, and autolysis.

Citation: Mazmanian S, Schneewind O. 2002. Cell Wall-Anchored Surface Proteins and Lipoproteins of Gram-Positive Bacteria, p 57-70. In Sonenshein A, Losick R, Hoch J (ed), and Its Closest Relatives. ASM Press, Washington, DC. doi: 10.1128/9781555817992.ch6

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Figures

Image of FIGURE 1
FIGURE 1

Cell wall anchor structure of staphylococcal protein A. The C-terminal threonine of protein A is amide-linked to the pentaglycine cross bridge within the staphylococcal cell wall. Cell wall anchor peptides are generally composed of a murein tetrapeptide [L-Ala-D-iGln-L-Lys (Glys)-D-Ala] tethered to the glycan strands [(MurNac-GlcNac)] and cross-linked via the D-Ala at position four. The neighboring wall subunit shown is a non-cross-linked murein pentapeptide [MurNac-(L-Ala-D-iGln-L-Lys(Gly)-D-Ala-D-Ala)-GlcNac].

Citation: Mazmanian S, Schneewind O. 2002. Cell Wall-Anchored Surface Proteins and Lipoproteins of Gram-Positive Bacteria, p 57-70. In Sonenshein A, Losick R, Hoch J (ed), and Its Closest Relatives. ASM Press, Washington, DC. doi: 10.1128/9781555817992.ch6
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Image of FIGURE 2
FIGURE 2

Phenotypes of protein A cell wall sorting signal mutants. Wild-type protein A is cleaved at the LPXTG motif and linked to the peptidoglycan (cell wall anchored). Deletions of the charged tail, the charged tail and the hydrophobic domain, or the entire sorting signal of protein A result in secretion of the uncleaved polypeptide into the extracellular medium. Deletion of the LPXTG motif of the C-terminal abolishes cleavage of the polypeptide, and the mutant protein A is loosely associated with the bacterial envelope.

Citation: Mazmanian S, Schneewind O. 2002. Cell Wall-Anchored Surface Proteins and Lipoproteins of Gram-Positive Bacteria, p 57-70. In Sonenshein A, Losick R, Hoch J (ed), and Its Closest Relatives. ASM Press, Washington, DC. doi: 10.1128/9781555817992.ch6
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Image of FIGURE 3
FIGURE 3

Surface protein anchoring in gram-positive bacteria, (i) (Export) Precursor proteins with an N-terminal signal peptide are initiated into the secretory (Sec) pathway, and the signal pep-tide is removed, (ii) (Retention) The C-terminal sorting signal retains polypeptides within the secretory pathway, (iii) (Cleavage) Sortase cleaves between the threonine and the glycine of the LPXTG motif, resulting in the formation of a thioester enzyme intermediate, (iv) (Linkage) Nucle-ophilic attack of the free amino group of lipid II at the thioester bond resolves the acyl enzyme intermediate, synthesizing the amide bond between surface proteins and the pentaglycine cross bridge and regenerating the active site sulfhydryl. (v) (cell wall incorporation) Lipid-linked surface protein is first incorporated into the cell wall via the transglycosylation reaction. The murein pentapeptide subunit with attached surface protein is then cross-linked to other cell wall peptides, generating the mature murein tetrapeptide anchor structure.

Citation: Mazmanian S, Schneewind O. 2002. Cell Wall-Anchored Surface Proteins and Lipoproteins of Gram-Positive Bacteria, p 57-70. In Sonenshein A, Losick R, Hoch J (ed), and Its Closest Relatives. ASM Press, Washington, DC. doi: 10.1128/9781555817992.ch6
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Image of FIGURE 4
FIGURE 4

Lipoprotein biosynthesis. After ribosomal synthesis and membrane translocation of the lipoprotein precursor (pro-lipoprotein), the cysteine residue of the lipobox (Leu-Ala-Gly-Cys) is modified by diacylglyceride. The reaction is catalyzed by lipoprotein diacylglyceride transferase (Lgt) in a manner requiring phosphatidylglycerol as a substrate. Diacylglyceride-modified lipoprotein is cleaved at the lipobox by lipoprotein signal peptidase (Lsp). The liberated amino group of the N-terminal cysteine is amide linked to fatty acid by lipoprotein -acyltransferase (Lnt) in a reaction that can utilize phosphatidylethanolamine (PE), phosphatidylglycerol (PG), or cardiolipin (CL) as a substrate. This reaction has been described for gram-negative species but not for gram-positive bacteria.

Citation: Mazmanian S, Schneewind O. 2002. Cell Wall-Anchored Surface Proteins and Lipoproteins of Gram-Positive Bacteria, p 57-70. In Sonenshein A, Losick R, Hoch J (ed), and Its Closest Relatives. ASM Press, Washington, DC. doi: 10.1128/9781555817992.ch6
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Tables

Generic image for table
TABLE 1

Surface proteins containing cell wall sorting signals

ORF, open reading frame; TIGR, The Institute for Genomic Research. Boldface sequence indicates LPXTG motif.

Citation: Mazmanian S, Schneewind O. 2002. Cell Wall-Anchored Surface Proteins and Lipoproteins of Gram-Positive Bacteria, p 57-70. In Sonenshein A, Losick R, Hoch J (ed), and Its Closest Relatives. ASM Press, Washington, DC. doi: 10.1128/9781555817992.ch6

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