Structural insight into the formation of lipoprotein-β-barrel complexes

Rodríguez-Alonso, Raquel; Létoquart, Juliette; Nguyen, Van Son; Louis, Gwennaelle; Calabrese, Antonio N.; Iorga, Bogdan I.; Radford, Sheena E.; Cho, Seung-Hyun; Remaut, Han; Collet, Jean-François

doi:10.1038/s41589-020-0575-0

Cited by 38 publications

(44 citation statements)

References 53 publications

(62 reference statements)

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“…Thus, these values confirm that IgaA has substantially more affinity for RcsF than OmpA (see Discussion). Interestingly, we noted that the BamA-RcsF complex was not modified by the increased expression of IgaA (lanes 7–10 in Figure 5B ), which is consistent with the fact that BamA has a much higher affinity for RcsF ( K D ~400 nM; Rodríguez-Alonso et al, 2020 ) than OmpA.…”

Section: Resultssupporting

confidence: 81%

“…The complex also formed when DiZPK was incorporated in other regions of the signaling domain, such as α-helix 1 (N54), α-helix 2 (R89 and K98), β-strand 2 (E110), and β-strand 3 (Q121) ( Figure 1 ). Noteworthy, residues Q79, R89 and P116 are part of the binding interface between RcsF and the luminal wall of the BamA β-barrel in the recently published structure of the BamA-RcsF complex ( Rodríguez-Alonso et al, 2020 ). Taken together, these observations substantially enlarge the region of RcsF known to interact with OmpA.…”

Section: Resultsmentioning

confidence: 99%

“…A complex between RcsF and BamA, the core component of the β- b arrel a ssembly m achinery (BAM), was identified ( Cho et al, 2014 ; Konovalova et al, 2014 ) and its structure solved ( Rodríguez-Alonso et al, 2020 ). This complex forms as an intermediate ( Cho et al, 2014 ; Konovalova et al, 2014 ): delivery of unfolded OM β-barrels (OMPs) to BAM triggers the release of RcsF from BamA and its transfer to OMP partners ( Rodríguez-Alonso et al, 2020 ). Three abundant OMPs (OmpA, OmpC and OmpF) have been identified as RcsF partners ( Cho et al, 2014 ; Konovalova et al, 2014 ).…”

Section: Introductionmentioning

confidence: 99%

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Defining the function of OmpA in the Rcs stress response

Dekoninck

Létoquart

Laguri

et al. 2020

eLife

Self Cite

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OmpA, a protein commonly found in the outer membrane of Gram-negative bacteria, has served as a paradigm for the study of b-barrel proteins for several decades. In Escherichia coli, OmpA was previously reported to form complexes with RcsF, a surface-exposed lipoprotein that triggers the Rcs stress response when damage occurs in the outer membrane and the peptidoglycan. How OmpA interacts with RcsF and whether this interaction allows RcsF to reach the surface has remained unclear. Here, we integrated in vivo and in vitro approaches to establish that RcsF interacts with the C-terminal, periplasmic domain of OmpA, not with the N-terminal b-barrel, thus implying that RcsF does not reach the bacterial surface via OmpA. Our results suggest a novel function for OmpA in the cell envelope: OmpA competes with the inner membrane protein IgaA, the downstream Rcs component, for RcsF binding across the periplasm, thereby regulating the Rcs response.

show abstract

Section: Resultssupporting

confidence: 81%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Defining the function of OmpA in the Rcs stress response

Dekoninck

Létoquart

Laguri

et al. 2020

eLife

Self Cite

View full text Add to dashboard Cite

show abstract

“…Thus, these values confirm that IgaA has substantially more affinity for RcsF than OmpA (see Discussion). Interestingly, we noted that the BamA-RcsF complex was not modified by the increased expression of IgaA (lanes 7-10 in Figure 5B), which is consistent with the fact that BamA has a much higher affinity for RcsF ( K D ~400 nM; (Rodriguez-Alonso et al 2020)) than OmpA.…”

Section: Resultssupporting

confidence: 81%

“…A complex between RcsF and BamA, the core component of the β- b arrel a ssembly m achinery (BAM), was identified (Cho et al 2014, Konovalova et al 2014) and its structure solved (Rodriguez-Alonso et al 2020). This complex forms as an intermediate (Cho et al 2014, Konovalova et al 2014): delivery of unfolded OM β-barrels (OMPs) to BAM triggers the release of RcsF from BamA and its transfer to OMP partners (Rodriguez-Alonso et al 2020). Three abundant OMPs (OmpA, OmpC and OmpF) have been identified as RcsF partners (Cho et al 2014, Konovalova et al 2014).…”

Section: Introductionmentioning

confidence: 99%

Defining the function of OmpA in the Rcs stress response

Létoquart

Dekoninck

Laguri

et al. 2020

Preprint

Self Cite

View full text Add to dashboard Cite

OmpA, a protein commonly found in the outer membrane of Gram-negative bacteria, has served as a paradigm for the study of β-barrel proteins for several decades. In Escherichia coli, OmpA was previously reported to form complexes with RcsF, a surface-exposed lipoprotein that triggers the Rcs stress response when damage occurs in the outer membrane and the peptidoglycan. How OmpA interacts with RcsF and whether this interaction allows RcsF to reach the surface has remained unclear. Here, we integrated in vivo and in vitro approaches to establish that RcsF interacts with the C-terminal, periplasmic domain of OmpA, not with the N-terminal β-barrel, thus implying that RcsF does not reach the bacterial surface via OmpA. Our results reveal a novel function for OmpA in the cell envelope: OmpA competes with the inner membrane protein IgaA, the downstream Rcs component, for RcsF binding across the periplasm, thereby regulating the Rcs response.

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Reversing Multidrug‐Resistant Escherichia coli by Compromising Its BAM Biogenesis and Enzymatic Catalysis through Microwave Hyperthermia Therapy

Mao

Jin

Xiang

et al. 2022

Adv Funct Materials

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Multidrug‐resistant (MDR) bacteria are emerging and disseminating rapidly, undoubtedly posing an urgent threat to global public health. One particular concern is that MDR Gram‐negative bacteria are immunized to available antibiotics owing to a series of biogenetic effects, including the β‐barrel assembly machine (BAM complex) in the outer membrane, MDR efflux pumps, and enzymatic degradation/modification, which are known to induce antibiotic resistance (AbR). Here, this work identifies that the AbR mechanisms of MDR Escherichia coli become compromised and sensitive again to conventional antibiotics, when the temperature of infected tissues is elevated to ≈50 °C in situ. This thought is realized by the microwave‐driven poly(lactic‐co‐glycolic acid) microparticles that may effectively convert electromagnetic radiation to thermal energy. The microwave hyperthermia (MWH) therapy not only interrupts the essential surface‐exposed BamA protein of the BAM complex, but also enhances the permeability of the outer membrane and inhibits the action of MDR efflux pumps. MWH also impairs the hydrogen bond interaction between the catalytic residues of bacterial enzymes and functional groups of antibiotic molecules. Lastly, this work demonstrates these combined inhibitors can revitalize the bactericidal effects of conventional antibiotics in MDR Escherichia coli‐associated deep tissue infections.

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Structural insight into the formation of lipoprotein-β-barrel complexes

Cited by 38 publications

References 53 publications

Defining the function of OmpA in the Rcs stress response

Defining the function of OmpA in the Rcs stress response

Defining the function of OmpA in the Rcs stress response

Reversing Multidrug‐Resistant Escherichia coli by Compromising Its BAM Biogenesis and Enzymatic Catalysis through Microwave Hyperthermia Therapy

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