Structure activity characterization of Bordetella petrii lipid A, from environment to human isolates

Basheer, Soorej M.; Bouchez, Valérie; Новиков, А. В.; Augusto, Luis; Guiso, Nicole; Caroff, Martine

doi:10.1016/j.biochi.2015.07.006

Cited by 6 publications

(5 citation statements)

References 51 publications

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“…Its lipid A structure contains a common bisphosphorylated disaccharide headgroup with hydroxytetradecanoic acid in the amide as well at the 3′ position (Figure S4). 40 Its shorter acyl chains enable the bacterium to escape the receptor signaling system.…”

Section: Introductionmentioning

confidence: 99%

Modeling Diversity in Structures of Bacterial Outer Membrane Lipids

Cummins

Edelstein

et al. 2017

J. Chem. Theory Comput.

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Lipopolysaccharides (LPSs) are vital components of the outer membrane of Gram-negative bacteria, and they act as extremely strong stimulators of innate immunity in diverse eukaryotic species. The primary immunostimulatory center of the LPS molecule is lipid A, a disaccharide-bound lipophilic domain. Considering the broad diversity in bacterial species, there are variations in the lipid A structures and their immunogenic potencies. In this work, we model the lipid A structures of eight commensal or human pathogenic bacterial species: Helicobacter pylori, Porphyromonas gingivalis, Bacteroides fragilis, Bordetella pertussis, Chlamydia trachomatis, Campylobacter jejuni, Neisseria meningitidis, and Salmonella minnesota. The membrane properties of these bacterial species were characterized and compared using molecular simulations. The structure-property relationships that emerge from this lipid A molecular library highlight the roles of acyl chain lengths, number of chains, phosphorylation state, membrane composition, and counterion charge in regulating the phase transition temperature of the membrane, diffusion coefficient of the lipids, and membrane thickness. The molecular and structural insights provided reveal the diversity in bacterial outer membrane lipids and their contribution to human disease and immunity.

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Section: Introductionmentioning

confidence: 99%

Modeling Diversity in Structures of Bacterial Outer Membrane Lipids

Cummins

Edelstein

et al. 2017

J. Chem. Theory Comput.

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“…Thus, we concluded that the difference observed in the length of the carbon FA at C3’ between FR4101 and the other isolates could be due to this difference within lpxA gene. Analysis of additional French B. holmesii isolates also led to the conclusion that this was not related to the blood or respiratory origin of the sample which was also confirmed by the lpxA sequence analysis of isolates with available genomes on NCBI.The presence of 10:0(3-OH) at C-3, like in B. pertussis [1] and B. petrii [41] is also a common trait between the three clinical isolates. In B. pertussis , this is the consequence of the lack of activity of the C-3 de- O -acylase PagL, which has been shown to result in a lower cytokine induction capacity of the Bordetella human pathogens [29,42].…”

Section: Discussionmentioning

confidence: 73%

“…The presence of 10:0(3-OH) at C-3, like in B. pertussis [1] and B. petrii [41] is also a common trait between the three clinical isolates. In B. pertussis , this is the consequence of the lack of activity of the C-3 de- O -acylase PagL, which has been shown to result in a lower cytokine induction capacity of the Bordetella human pathogens [29,42].…”

Section: Discussionmentioning

confidence: 99%

“…The efficiency of these traits, and especially the presence of the short-chain 10:0(3-OH) is already attested by the virulence of the whooping-cough pathogens B. pertussis and B. parapertussis [31,52] and were also recently characterized in B. petrii lipid A isolates [41]. However, no real difference of lipid A structure was observed between isolates from blood or respiratory origins which correlates with data from other studies [18,19].…”

Section: Discussionmentioning

confidence: 99%

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Bordetella holmesii: Lipid A Structures and Corresponding Genomic Sequences Comparison in Three Clinical Isolates and the Reference Strain ATCC 51541

Bouchez

Albitar-Nehme

Новиков

et al. 2017

IJMS

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Bordetella holmesii can cause invasive infections but can also be isolated from the respiratory tract of patients with whooping-cough like symptoms. For the first time, we describe the lipid A structure of B. holmesii reference strain ATCC 51541 (alias NCTC12912 or CIP104394) and those of three French B. holmesii clinical isolates originating from blood (Bho1) or from respiratory samples (FR4020 and FR4101). They were investigated using chemical analyses, gas chromatography–mass spectrometry (GC–MS), and matrix-assisted laser desorption ionization–mass spectrometry (MALDI–MS). The analyses revealed a common bisphosphorylated β-(1→6)-linked d-glucosamine disaccharide with hydroxytetradecanoic acid in amide linkages. Similar to B. avium, B. hinzii and B. trematum lipids A, the hydroxytetradecanoic acid at the C-2′ position are carrying in secondary linkage a 2-hydroxytetradecanoic acid residue resulting of post-traductional biosynthesis modifications. The three clinical isolates displayed characteristic structural traits compared to the ATCC 51541 reference strain: the lipid A phosphate groups are more or less modified with glucosamine in the isolates and reference strain, but the presence of 10:0(3-OH) is only observed in the isolates. This trait was only described in B. pertussis and B. parapertussis strains, as well as in B. petrii isolates by the past. The genetic bases for most of the key structural elements of lipid A were analyzed and supported the structural data.

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“…LPSs were extracted following the isobutyric acid-1 M ammonium hydroxide method (19). They were further purified with an enzymatic treatment to remove DNA, RNA, and proteins, as previously described (20). Phospholipid and lipoprotein contaminants were also extracted with a mixture of solvents, chloroform/ methanol/water (30:15:2.5).…”

Section: Methodsmentioning

confidence: 99%

Antimicrobial Peptide Resistance Genes in the Plant Pathogen Dickeya dadantii

Pandin

Caroff

Condemine

2016

Appl Environ Microbiol

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Modification of teichoic acid through the incorporation of D-alanine confers resistance in Gram-positive bacteria to antimicrobial peptides (AMPs). This process involves the products of the dltXABCD genes. These genes are widespread in Gram-positive bacteria, and they are also found in a few Gram-negative bacteria. Notably, these genes are present in all soft-rot enterobacteria (Pectobacterium and Dickeya) whose dltDXBAC operons have been sequenced. We studied the function and regulation of these genes in Dickeya dadantii. dltB expression was induced in the presence of the AMP polymyxin. It was not regulated by PhoP, which controls the expression of some genes involved in AMP resistance, but was regulated by ArcA, which has been identified as an activator of genes involved in AMP resistance. However, arcA was not the regulator responsible for polymyxin induction of these genes in this bacterium, which underlines the complexity of the mechanisms controlling AMP resistance in D. dadantii. Two other genes involved in resistance to AMPs have also been characterized, phoS and phoH. dltB, phoS, phoH, and arcA but not dltD mutants were more sensitive to polymyxin than the wild-type strain. Decreased fitness of the dltB, phoS, and phoH mutants in chicory leaves indicates that their products are important for resistance to plant AMPs. IMPORTANCE Gram-negative bacteria can modify their lipopolysaccharides (LPSs) to resist antimicrobial peptides (AMPs). Soft-rot enterobacteria (Dickeya and Pectobacterium spp.) possess homologues of the dlt genes in their genomes which, in Gram-positive bacteria, are involved in resistance to AMPs. In this study, we show that these genes confer resistance to AMPs, probably by modifying LPSs, and that they are required for the fitness of the bacteria during plant infection. Two other new genes involved in resistance were also analyzed. These results show that bacterial resistance to AMPs can occur in bacteria through many different mechanisms that need to be characterized.

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Structure activity characterization of Bordetella petrii lipid A, from environment to human isolates

Cited by 6 publications

References 51 publications

Modeling Diversity in Structures of Bacterial Outer Membrane Lipids

Modeling Diversity in Structures of Bacterial Outer Membrane Lipids

Bordetella holmesii: Lipid A Structures and Corresponding Genomic Sequences Comparison in Three Clinical Isolates and the Reference Strain ATCC 51541

Antimicrobial Peptide Resistance Genes in the Plant Pathogen Dickeya dadantii

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