The modern pandemic of the bacterial kiwifruit pathogen Pseudomonas syringae pv actinidiae (Psa) is caused by a particular Psa lineage. To better understand the genetic basis of the virulence of this lineage, we compare the completely assembled genome of a pandemic New Zealand strain with that of the Psa type strain first isolated in Japan in 1983. Aligning the two genomes shows numerous translocations, constrained so as to retain the appropriate orientation of the Architecture Imparting Sequences (AIMs). There are several large horizontally acquired regions, some of which include Type I, Type II or Type III restriction systems. The activity of these systems is reflected in the methylation patterns of the two strains. The pandemic strain carries an Integrative Conjugative Element (ICE) located at a tRNA-Lys site. Two other complex elements are also present at tRNA-Lys sites in the genome. These elements are derived from ICE but have now acquired some alternative secretion function. There are numerous types of mobile element in the two genomes. Analysis of these elements reveals no evidence of recombination between the two Psa lineages.
Oral
dental infections are one of the most common diseases affecting
humans, with caries and periodontal disease having the highest incidence.
Caries and periodontal disease arise from infections caused by oral
bacterial pathogens. Current misuse and overuse of antibiotic treatments
have led to the development of antimicrobial resistance. However,
recent studies have shown that cationic antimicrobial peptides are
a promising family of antibacterial agents that are active against
oral pathogenic bacteria and also possess less propensity for development
of antimicrobial resistance. This timely Review has a focus on two
primary subjects: (i) the oral bacterial pathogens associated with
dental infections and (ii) the current development of antimicrobial
peptides targeting oral pathogens.
This review highlights the predominant role that NMR has had in determining the structures of cyclotides, a fascinating class of macrocyclic peptides found in plants. Cyclotides contain a cystine knot, a compact structural motif that is constrained by three disulfide bonds and able to resist chemical and biological degradation. Their resistance to proteolytic degradation has made cyclotides appealing as drug leads. Herein, we examine the developments that led to the identification and conclusive determination of the disulfide connectivity of cyclotides and describe in detail the structural features of exemplar cyclotides. We also review the role that X‐ray crystallography has played in resolving cyclotide structures and describe how racemic crystallography opened up the possibility of obtaining previously inaccessible X‐ray structures of cyclotides.
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