Relationship of the Lipopolysaccharide Structure of Yersinia bpestis to Resistance to Antimicrobial Factors

Knirel, Yuriy A.; Dentovskaya, Svetlana V.; Bystrova, Olga V.; Kocharova, Nina A.; Senchenkova, Sof’ya N.; Shaikhutdinova, Rima Z.; Титарева, Г. М.; Бахтеева, И. В.; Lindner, Buko; Pier, Gerald B.; Anisimov, Andrey P.

doi:10.1007/978-0-387-72124-8_7

Cited by 32 publications

(53 citation statements)

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“…It was previously reported that inactivation of galU in Vibrio cholerae (38) or Proteus mirabilis (28) causes an increase in susceptibility to antimicrobial peptides. In addition, Yersinia enterocolitica serotype O:3 and O:9 mutants lacking the LPS outer core have defects in resistance to the cationic antimicrobial peptide polymyxin B (53,54), and Y. pestis mutants defective for the biosynthesis of the inner heptose core of LOS are sensitive to polymyxin B (2,29). To determine if galU is important for resistance of Y. pestis to antimicrobial peptides, the MICs of polymyxin B and the murine cathelicidin CRAMP for KIM6ϩ and KIM6ϩ galU were determined (see Materials and Methods).…”

Section: Resultsmentioning

confidence: 99%

“…UDP-glucose is used as a substrate by a glucosyltransferase to add a single glucose residue to the LOS inner core of Y. pestis. The LOS core of Y. pestis contains a single glucose (Glc) attached laterally to heptose I (Hep-I) (24,29). The absence of UDP-glucose in the galU mutant would prevent the addition of this Glc on Hep-1.…”

Section: Discussionmentioning

confidence: 99%

“…The Y. pestis outer membrane contains a lipooligosaccharide (LOS) that plays a key role in resistance to antimicrobial peptides (24,29). Products of the pmr genes promote antimicrobial peptide resistance in Y. pestis by the addition of the cationic sugar 4-amino-4-deoxy-L-arabinose (aminoarabinose) to lipid A (29,46,63).…”

mentioning

confidence: 99%

“…Products of the pmr genes promote antimicrobial peptide resistance in Y. pestis by the addition of the cationic sugar 4-amino-4-deoxy-L-arabinose (aminoarabinose) to lipid A (29,46,63). The inner heptose core of the LOS is also important for resistance of Y. pestis to antimicrobial peptides in vitro (2,29).…”

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confidence: 99%

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A Transposon Site Hybridization Screen IdentifiesgalUandwecBCas Important for Survival of Yersinia pestis in Murine Macrophages

et al. 2012

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Yersinia pestis is able to survive and replicate within murine macrophages. However, the mechanism by which Y. pestis promotes its intracellular survival is not well understood. To identify genes that are important for Y. pestis survival in macrophages, a library comprised of ϳ31,500 Y. pestis KIM6؉ transposon insertion mutants (input pool) was subjected to negative selection in primary murine macrophages. Genes underrepresented in the output pool of surviving bacteria were identified by transposon site hybridization to DNA oligonucleotide microarrays. The screen identified several genes known to be important for survival of Y. pestis in macrophages, including phoPQ and members of the PhoPQ regulon (e.g., pmrF). In addition, genes predicated to encode a glucose-1-phosphate uridylyltransferase (galU), a UDP-N-acetylglucosamine 2-epimerase (wecB) and a UDP-N-acetyl-D-mannosamine dehydrogenase (wecC) were identified in the screen. Viable-count assays demonstrated that a KIM6؉ galU mutant and a KIM6؉ wecBC mutant were defective for survival in murine macrophages. The galU mutant was studied further because of its strong phenotype. The KIM6؉ galU mutant exhibited increased susceptibility to the antimicrobial peptides polymyxin B and cathelicidin-related antimicrobial peptide (CRAMP). Polyacrylamide gel electrophoresis demonstrated that the lipooligosaccharide (LOS) of the galU mutant migrated faster than the LOS of the parent KIM6؉, suggesting the core was truncated. In addition, the analysis of LOS isolated from the galU mutant by mass spectrometry showed that aminoarabinose modification of lipid A is absent. Therefore, addition of aminoarabinose to lipid A and complete LOS core (galU), as well as enterobacterial common antigen (wecB and wecC), is important for survival of Y. pestis in macrophages.

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Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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confidence: 99%

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A Transposon Site Hybridization Screen IdentifiesgalUandwecBCas Important for Survival of Yersinia pestis in Murine Macrophages

et al. 2012

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“…While some Gram-negative bacteria possess constitutive mechanisms of resistance, others such as Salmonella enterica serovar Typhimurium and Y. pestis possesses inducible resistances. Exposure to sublethal concentrations of CAMPs induces modifications to the LPS, including addition of 4-amino-4-deoxy-L-arabinose (L-Ara4N) (Guo et al, 1997;Knirel et al, 2007), palmitoylation and myristoylation (Guo et al, 1998;Tran et al, 2005) to resist CAMP action. These modifications increase the net charge of the membrane repelling CAMPs (Guo et al, 1998;Raetz et al, 2009;Tran et al, 2005).…”

Section: Introductionmentioning

confidence: 99%

Mechanisms of intrinsic resistance to antimicrobial peptides of Edwardsiella ictaluri and its influence on fish gut inflammation and virulence

et al. 2013

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The genus Edwardsiella comprises a genetically distinct taxon related to other members of the family Enterobacteriaceae. It consists of bacteria differing strongly in their biochemical and physiological features, natural habitats, and pathogenic properties. Intrinsic resistance to cationic antimicrobial peptides (CAMPs) is a specific property of the genus Edwardsiella. In particular, Edwardsiella ictaluri, an important pathogen of the catfish (Ictalurus punctatus) aquaculture and the causative agent of a fatal systemic infection, is highly resistant to CAMPs. E. ictaluri mechanisms of resistance to CAMPs are unknown. We hypothesized that E. ictaluri lipopolysaccharide (LPS) plays a role in both virulence and resistance to CAMPs. The putative genes related to LPS oligo-polysaccharide (O-PS) synthesis were in-frame deleted. Individual deletions of wibT, gne and ugd eliminated synthesis of the O-PS, causing auto-agglutination, rough colonies, biofilm-like formation and motility defects. Deletion of ugd, the gene that encodes the UDP-glucose dehydrogenase enzyme responsible for synthesis of UDP-glucuronic acid, causes sensitivity to CAMPs, indicating that UDP-glucuronic acid and its derivatives are related to CAMP intrinsic resistance. E. ictaluri OP-S mutants showed different levels of attenuation, colonization of lymphoid tissues and immune protection in zebrafish (Danio rerio) and catfish. Orally inoculated catfish with O-PS mutant strains presented different degrees of gut inflammation and colonization of lymphoid tissues. Here we conclude that intrinsic resistance to CAMPs is mediated by Ugd enzyme, which has a pleiotropic effect in E. ictaluri influencing LPS synthesis, motility, agglutination, fish gut inflammation and virulence.

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Complement evasion mechanisms of the systemic pathogens Yersiniae and Salmonellae

Krukonis

Thomson

2020

FEBS Letters

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Pathogens that colonize deep tissues and spread systemically encounter the innate host resistance mechanism of complement-mediated lysis and complement opsonization leading to engulfment and degradation by phagocytic cells. Yersinia and Salmonella species have developed numerous strategies to block the antimicrobial effects of complement. These include recruitment of complement regulatory proteins factor H, C4BP, and vitronectin (Vn) as well as interference in late maturation events such as assembly of C9 into the membrane attack complex that leads to bacterial lysis. This review will discuss the contributions of various surface structures (proteins, lipopolysaccharide, and capsules) to evasion of complement-mediated immune clearance of the systemic pathogens Yersiniae and Salmonellae. Bacterial proteins required for recruitment of complement regulatory proteins will be described, including the details of their interaction with host regulatory proteins, where known. The potential role of the surface proteases Pla (Yersinia pestis) and PgtE (Salmonella species) on the activity of complement regulatory proteins will also be addressed. Finally, the implications of complement inactivation on host cell interactions and host cell targeting for type 3 secretion will be discussed.

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Relationship of the Lipopolysaccharide Structure of Yersinia bpestis to Resistance to Antimicrobial Factors

Cited by 32 publications

References 17 publications

A Transposon Site Hybridization Screen IdentifiesgalUandwecBCas Important for Survival of Yersinia pestis in Murine Macrophages

A Transposon Site Hybridization Screen IdentifiesgalUandwecBCas Important for Survival of Yersinia pestis in Murine Macrophages

Mechanisms of intrinsic resistance to antimicrobial peptides of Edwardsiella ictaluri and its influence on fish gut inflammation and virulence

Complement evasion mechanisms of the systemic pathogens Yersiniae and Salmonellae

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