@article {532861,
	title = {Inhibition of the β-barrel assembly machine by a peptide that binds BamD.},
	journal = {Proc Natl Acad Sci U S A},
	volume = {112},
	year = {2015},
	month = {2015 Feb 17},
	pages = {2011-6},
	abstract = {The protein complex that assembles integral membrane β-barrel proteins in the outer membranes of Gram-negative bacteria is an attractive target in the development of new antibiotics. This complex, the β-barrel assembly machine (Bam), contains two essential proteins, BamA and BamD. We have identified a peptide that inhibits the assembly of β-barrel proteins in vitro by characterizing the interaction of BamD with an unfolded substrate protein. This peptide is a fragment of the substrate protein and contains a conserved amino acid sequence. We have demonstrated that mutations of this sequence in the full-length substrate protein impair the protein{\textquoteright}s assembly, implying that BamD{\textquoteright}s interaction with this sequence is an important part of the assembly mechanism. Finally, we have found that in vivo expression of a peptide containing this sequence causes growth defects and sensitizes Escherichia coli to antibiotics to which they are normally resistant. Therefore, inhibiting the binding of substrates to BamD is a viable strategy for developing new antibiotics directed against Gram-negative bacteria.},
	issn = {1091-6490},
	doi = {10.1073/pnas.1415955112},
	author = {Hagan, Christine L and Wzorek, Joseph S and Kahne, Daniel}
}
