ja3089229_si_001.pdf (1.56 MB)
Structural Characterization of the Highly Cyclized Lantibiotic Paenicidin A via a Partial Desulfurization/Reduction Strategy
journal contribution
posted on 2012-12-05, 00:00 authored by Christopher
T. Lohans, Zedu Huang, Marco J. van Belkum, Maude Giroud, Clarissa S. Sit, Erika M. Steels, Jing Zheng, Randy
M. Whittal, Lynn M. McMullen, John C. VederasLantibiotics
are ribosomally synthesized antimicrobial peptides
produced by bacteria that are increasingly of interest for food preservation
and possible therapeutic uses. These peptides are extensively post-translationally
modified, and are characterized by lanthionine and methyllanthionine
thioether cross-links. Paenibacillus polymyxa NRRL
B-30509 was found to produce polymyxins and tridecaptins, in addition
to a novel lantibiotic termed paenicidin A. A bacteriocin termed SRCAM
602 previously reported to be produced by this organism and claimed
to be responsible for inhibition of Campylobacter jejuni could not be detected either directly or by genomic analysis. The
connectivities of the thioether cross-links of paenicidin A were solved
using a novel partial desulfurization/reduction strategy in combination
with tandem mass spectrometry. This approach overcame the limitations
of NMR-based structural characterization that proved mostly unsuccessful
for this peptide. Paenicidin A is a highly cyclized lantibiotic, containing
six lanthionine and methyllanthionine rings, three of which are interlocking.