2015
DOI: 10.1021/cb500843r
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HIV Protease Inhibitors Block Streptolysin S Production

Abstract: Streptolysin S (SLS) is a post-translationally modified peptide cytolysin that is produced by the human pathogen Streptococcus pyogenes. SLS belongs to a large family of azole-containing natural products that are biosynthesized via an evolutionarily conserved pathway. SLS is an important virulence factor during S. pyogenes infections, but despite an extensive history of study, further investigations are needed to clarify several steps of its biosynthesis. To this end, chemical inhibitors of SLS biosynthesis wo… Show more

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Cited by 16 publications
(30 citation statements)
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“…6B). Unlike class III lanthipeptide gene clusters from Actinobacteria that usually do not contain a protease [77], the III 3 clusters encode for a prolyl oligopeptidase (we propose the name LanP B for these with the name LanP A given to the previously characterized group of subtilisin-like leader peptide proteases [11]) as well as a CAAX family protease [78]. The smaller III 6 family is also found in Firmicutes but the phylogenetic distribution is more varied as these BGCs are found in different Bacillus and Staphylococcus species.…”
Section: Discussionmentioning
confidence: 99%
“…6B). Unlike class III lanthipeptide gene clusters from Actinobacteria that usually do not contain a protease [77], the III 3 clusters encode for a prolyl oligopeptidase (we propose the name LanP B for these with the name LanP A given to the previously characterized group of subtilisin-like leader peptide proteases [11]) as well as a CAAX family protease [78]. The smaller III 6 family is also found in Firmicutes but the phylogenetic distribution is more varied as these BGCs are found in different Bacillus and Staphylococcus species.…”
Section: Discussionmentioning
confidence: 99%
“…By homology to SagE, the previously described type II CaaX-like protease, BamE was hypothesized to remove the leader. 138 Additionally, methylation was anticipated based on the presence of a S -adenosylmethionine (SAM)-dependent methyltransferase (BamL). This methyltransferase was later shown to selectively dimethylate the newly formed N-terminus of PZN through a narrow substrate tunnel which limited access to the active site.…”
Section: Linear Azole-containing Peptides (Laps)mentioning
confidence: 99%
“…The C-protein serves to bind the N -terminal (leader) region of the precursor peptide, enhancing the rate of processing (1214). Following heterocyclization, the biosynthesis of PZN is completed by removal of the leader peptide, likely by the locally encoded type II CaaX protease (15, 16), and dimethylation of the new N -terminus by an S- adenosylmethionine (SAM)-dependent methyltransferase (17, 18). …”
Section: Introductionmentioning
confidence: 99%