Characterization of the free form of murein‐lipoprotein from the outer membrane of <i>Escherichia coli</i> B/r

Braun, Volkmar; Hantke, Klaus

doi:10.1016/0014-5793(75)80410-8

Cited by 14 publications

(7 citation statements)

References 11 publications

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“…We previously reported that a fraction of Lpp, the most abundant lipoprotein in E. coli, is exposed on the cell surface (11), whereas the other fraction remains in the periplasm where it is covalently bound to PG (12,13). It is hard to determine whether RcsF, like Lpp, exists in two different cellular locations.…”

Section: Discussionmentioning

confidence: 97%

“…Recently we have shown that a fraction of Braun's lipoprotein or Lpp, the most abundant protein in E. coli, is exposed on the cell surface (11). Lpp exists in two forms: a bound form in which Lpp is covalently linked to peptidoglycan (PG) and a free form, the function of which is not understood (12,13). We discovered that the free form of Lpp adopts an unusual conformation with its C terminus exposed on the cell surface (11).…”

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confidence: 99%

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Transmembrane domain of surface-exposed outer membrane lipoprotein RcsF is threaded through the lumen of β-barrel proteins

Konovalova

Perlman

Cowles

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

114

173

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RcsF (regulator of capsule synthesis) is an outer membrane (OM) lipoprotein that functions to sense defects such as changes in LPS. However, LPS is found in the outer leaflet, and RcsF was thought to be tethered to the inner leaflet by its lipidated N terminus, raising the question of how it monitors LPS. We show that RcsF has a transmembrane topology with the lipidated N terminus on the cell surface and the C-terminal signaling domain in the periplasm. Strikingly, the short, unstructured, charged transmembrane domain is threaded through the lumen of β-barrel OM proteins where it is protected from the hydrophobic membrane interior. We present evidence that these unusual complexes, which contain one protein inside another, are formed by the Bam complex that assembles all β-barrel proteins in the OM. The ability of the Bam complex to expose lipoproteins at the cell surface underscores the mechanistic versatility of the β-barrel assembly machine.membrane biogenesis | protein folding | signal transduction | envelope stress response

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Section: Discussionmentioning

confidence: 97%

mentioning

confidence: 99%

Transmembrane domain of surface-exposed outer membrane lipoprotein RcsF is threaded through the lumen of β-barrel proteins

Konovalova

Perlman

Cowles

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

114

173

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“…The biosynthetic anchoring pathway of lipoproteins in Gram-negative bacteria has been elucidated in considerable detail (Braun & Hantke, 1975;Chattopadhyay & Wu, 1977;Dev & Ray, 1984;Hantke & Braun, 1973;Hussain et al, 1982;Innis et al, 1984;Inukai et al, 1984;Lee et al, 1983;Tokunaga et al, 1982Tokunaga et al, , 1985Yamagata, 1983;Yamagata et al, 1982;Yamaguchi et al, 1988). In Grampositive bacteria, Lgt was first reported in Staph.…”

Section: Introductionmentioning

confidence: 99%

In the absence of Lgt, lipoproteins are shed from Streptococcus uberis independently of Lsp

Denham

Ward²,

Leigh

2009

Microbiology

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The role of lipoprotein diacylglyceryl transferase (Lgt) and lipoprotein signal peptidase (Lsp) responsible for processing lipoproteins was investigated in Streptococcus uberis, a common cause of bovine mastitis. In the absence of Lgt, three lipoproteins [MtuA (SUB0473), Hap (SUB1625) and an extracellular solute-binding protein (SUB0365)] were detected in extracellular locations. All were shown by Edman degradation analysis to be cleaved on the carboxy side of the LXXC lipobox. Detection of MtuA, a lipoprotein shown previously to be essential for infectivity and virulence, was used as a surrogate lipoprotein marker to locate and assess processing of lipoproteins. The absence of Lgt did not prevent location of MtuA to the cell membrane, its location in the wild-type strain but, in contrast to the situation with wild-type, did result in a widespread location of this protein. In the absence of both Lgt and Lsp, MtuA was similarly released from the bacterial cell. In such strains, however, the cell-associated MtuA represented the full-length gene product, indicating that Lsp was able to cleave non-lipidated (lipo)proteins but was not responsible for their release from this bacterium.

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“…Examples of diacylated forms are the M161Ag lipoprotein of Mycoplasma fermentans from which the macrophage-activating lipopeptide (MALP)-2 is derived [45, 46], the LP44 lipoprotein from Mycoplasma salivarium from which the fibroblast-stimulating lipopeptide (FSL)-1 is derived [47], and the synthetic lipopeptide di-palmitoyl-S-glyceryl cysteine (Pam 2 C) SK 4 . The Braun's lipoprotein from Escherichia coli is the prototype of the outer membrane triacylated lipoproteins from Gram-negative bacteria and some synthetic lipopeptides used as TLR2 stimulators, for example, tri-palmitoyl-S-glyceryl cysteine (Pam 3 C) SK 4 , have a lipid modification analogue to this lipoprotein [48–50]. Other examples of triacylated lipoproteins are OspA from Borrelia burgdorferi [51] and the 19 kDa lipoprotein from Mycobacterium tuberculosis [52, 53].…”

Section: Tlr2mentioning

confidence: 99%

Targeting TLR2 for Vaccine Development

Basto

Leitão

2014

Journal of Immunology Research

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Novel and more effective immunization strategies against many animal diseases may profit from the current knowledge on the modulation of specific immunity through stimulation of innate immune receptors. Toll-like receptor (TLR)2-targeting formulations, such as synthetic lipopeptides and antigens expressed in fusion with lipoproteins, have been shown to have built-in adjuvant properties and to be effective at inducing cellular and humoral immune mechanisms in different animal species. However, contradictory data has arisen concerning the profile of the immune response elicited. The benefits of targeting TLR2 for vaccine development are thus still debatable and more studies are needed to rationally explore its characteristics. Here, we resume the main features of TLR2 and TLR2-induced immune responses, focusing on what has been reported for veterinary animals.

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Characterization of the free form of murein‐lipoprotein from the outer membrane of Escherichia coli B/r

Cited by 14 publications

References 11 publications

Transmembrane domain of surface-exposed outer membrane lipoprotein RcsF is threaded through the lumen of β-barrel proteins

Transmembrane domain of surface-exposed outer membrane lipoprotein RcsF is threaded through the lumen of β-barrel proteins

In the absence of Lgt, lipoproteins are shed from Streptococcus uberis independently of Lsp

Targeting TLR2 for Vaccine Development

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