Complete Lipopolysaccharide ofPlesiomonas shigelloidesO74:H5 (Strain CNCTC 144/92). 1. Structural Analysis of the Highly Hydrophobic Lipopolysaccharide, Including the O-Antigen, Its Biological Repeating Unit, the Core Oligosaccharide, and the Linkage between Them†,‡

Biochemistry ◽  
2006 ◽  
Vol 45 (35) ◽  
pp. 10422-10433 ◽  
Author(s):  
Tomasz Niedziela ◽  
Semiha Dag ◽  
Jolanta Lukasiewicz ◽  
Monika Dzieciatkowska ◽  
Wojciech Jachymek ◽  
...  
Keyword(s):  
Structural Analysis ◽  
Core Oligosaccharide ◽  
The Core ◽  
O Antigen ◽  
Highly Hydrophobic

scholarly journals Interactions of Pulmonary Collectins with Bordetella bronchiseptica and Bordetella pertussis Lipopolysaccharide Elucidate the Structural Basis of Their Antimicrobial Activities

2004 ◽  
Vol 72 (12) ◽  
pp. 7124-7130 ◽  
Author(s):  
Lyndsay M. Schaeffer ◽  
Francis X. McCormack ◽  
Huixing Wu ◽  
Alison A. Weiss
Keyword(s):  
Bordetella Pertussis ◽  
Lipid A ◽  
Antimicrobial Activities ◽  
Innate Immune ◽  
Bordetella Bronchiseptica ◽  
Structural Basis ◽  
Wild Type ◽  
Core Oligosaccharide ◽  
The Core ◽  
O Antigen

ABSTRACT Surfactant proteins A (SP-A) and D (SP-D) play an important role in the innate immune defenses of the respiratory tract. SP-A binds to the lipid A region of lipopolysaccharide (LPS), and SP-D binds to the core oligosaccharide region. Both proteins induce aggregation, act as opsonins for neutrophils and macrophages, and have direct antimicrobial activity. Bordetella pertussis LPS has a branched core structure and a nonrepeating terminal trisaccharide. Bordetella bronchiseptica LPS has the same structure, but lipid A is palmitoylated and there is a repeating O-antigen polysaccharide. The ability of SP-A and SP-D to agglutinate and permeabilize wild-type and LPS mutants of B. pertussis and B. bronchiseptica was examined. Previously, wild-type B. pertussis was shown to resist the effects of SP-A; however, LPS mutants lacking the terminal trisaccharide were susceptible to SP-A. In this study, SP-A was found to aggregate and permeabilize a B. bronchiseptica mutant lacking the terminal trisaccharide, while wild-type B. bronchiseptica and mutants lacking only the palmitoyl transferase or O antigen were resistant to SP-A. Wild-type B. pertussis and B. bronchiseptica were both resistant to SP-D; however, LPS mutants of either strain lacking the terminal trisaccharide were aggregated and permeabilized by SP-D. We conclude that the terminal trisaccharide protects Bordetella species from the bactericidal functions of SP-A and SP-D. The O antigen and palmitoylated lipid A of B. bronchiseptica play no role in this resistance.

Structural analysis of the core oligosaccharide from Pasteurella multocida strain X73

2005 ◽  
Vol 340 (6) ◽  
pp. 1253-1257 ◽  
Author(s):  
Frank St. Michael ◽  
Jianjun Li ◽  
Andrew D. Cox
Keyword(s):  
Structural Analysis ◽  
Pasteurella Multocida ◽  
Core Oligosaccharide ◽  
The Core

scholarly journals Functional Characterization of MigA and WapR: Putative Rhamnosyltransferases Involved in Outer Core Oligosaccharide Biosynthesis of Pseudomonas aeruginosa

2008 ◽  
Vol 190 (6) ◽  
pp. 1857-1865 ◽  
Author(s):  
Karen K. H. Poon ◽  
Erin L. Westman ◽  
Evgeny Vinogradov ◽  
Shouguang Jin ◽  
Joseph S. Lam
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Functional Characterization ◽  
Outer Core ◽  
Resonance Spectroscopy ◽  
Core Oligosaccharide ◽  
Strain Pao1 ◽  
The Core ◽  
O Antigen ◽  
Knockout Mutants

ABSTRACT Pseudomonas aeruginosa lipopolysaccharide (LPS) contains two glycoforms of core oligosaccharide (OS); one form is capped with O antigen through an α-1,3-linked l-rhamnose (l-Rha), while the other is uncapped and contains an α-1,6-linked l-Rha. Two genes in strain PAO1, wapR (PA5000) and migA (PA0705), encode putative glycosyltransferases associated with core biosynthesis. We propose that WapR and MigA are the rhamnosyltransferases responsible for the two linkages of l-Rha to the core. Knockout mutants with mutations in both genes were generated. The wapR mutant produced LPS lacking O antigen, and addition of wapR in trans complemented this defect. The migA mutant produced LPS with a truncated outer core and showed no reactivity to outer core-specific monoclonal antibody (MAb) 5C101. Complementation of this mutant with migA restored reactivity of the LPS to MAb 5C101. Interestingly, LPS from the complemented migA strain was not reactive to MAb 18-19 (specific for the core-plus-one O repeat). This was due to overexpression of MigA in the complemented strain that caused an increase in the proportion of the uncapped core OS, thereby decreasing the amount of the core-plus-one O repeat, indicating that MigA has a regulatory role. The structures of LPS from both mutants were elucidated using nuclear magnetic resonance spectroscopy and mass spectrometry. The capped core of the wapR mutant was found to be truncated and lacked α-1,3-l-Rha. In contrast, uncapped core OS from the migA mutant lacked α-1,6-l-Rha. These results provide evidence that WapR is the α-1,3-rhamnosyltransferase, while MigA is the α-1,6-rhamnosyltransferase.

scholarly journals Identification of the Linkage between A-Polysaccharide and the Core in the A-Lipopolysaccharide of Porphyromonas gingivalis W50

2015 ◽  
Vol 197 (10) ◽  
pp. 1735-1746 ◽  
Author(s):  
Nikolay Paramonov ◽  
Joseph Aduse-Opoku ◽  
Ahmed Hashim ◽  
Minnie Rangarajan ◽  
Michael A. Curtis
Keyword(s):  
Porphyromonas Gingivalis ◽  
Biosynthetic Pathway ◽  
Attachment Site ◽  
Outer Core ◽  
Etiologic Agent ◽  
Core Oligosaccharide ◽  
Content Type ◽  
The Core ◽  
O Antigen ◽  
Mutant Strains

ABSTRACTPorphyromonas gingivalissynthesizes two lipopolysaccharides (LPSs), O-LPS and A-LPS. The structure of the core oligosaccharide (OS) of O-LPS and the attachment site of the O-polysaccharide (O-PS) repeating unit [→3)-α-d-Galp-(1→6)-α-d-Glcp-(1→4)-α-l-Rhap-(1→3)-β-d-GalNAcp-(1→] to the core have been elucidated using the ΔPG1051 (WaaL, O-antigen ligase) and ΔPG1142 (Wzy, O-antigen polymerase) mutant strains, respectively. The core OS occurs as an “uncapped” glycoform devoid of O-PS and a “capped” glycoform that contains the attachment site of O-PS via β-d-GalNAc at position O-3 of the terminal α-(1→3)-linked mannose (Man) residue. In this study, the attachment site of A-PS to the core OS was determined based on structural analysis of SR-type LPS (O-LPS and A-LPS) isolated from aP. gingivalisΔPG1142 mutant strain by extraction with aqueous hot phenol to minimize the destruction of A-LPS. Application of one- and two-dimensional nuclear magnetic resonance (NMR) spectroscopy in combination with methylation analysis showed that the A-PS repeating unit is linked to a nonterminal α-(1→3)-linked Man of the “capped core” glycoform of outer core OS at position O-4 via a →6)-[α-d-Man-α-(1→2)-α-d-Man-1-phosphate→2]-α-d-Man-(1→ motif. In order to verify that O-PS and A-PS are attached to almost identical core glycoforms, we identified a putative α-mannosyltransferase (PG0129) inP. gingivalisW50 that may be involved in the formation of core OS. Inactivation of PG0129 led to the synthesis of deep-R-type LPS with a truncated core that lacks α-(1→3)-linked mannoses and is devoid of either O-PS or A-PS. This indicated that PG0129 is an α-1,3-mannosyltransferase required for synthesis of the outer core regions of both O-LPS and A-LPS inP. gingivalis.IMPORTANCEPorphyromonas gingivalis, a Gram-negative anaerobe, is considered to be an important etiologic agent in periodontal disease, and among the virulence factors produced by the organism are two lipopolysaccharides (LPSs), O-LPS and A-LPS. The structures of the O-PS and A-PS repeating units, the core oligosaccharide (OS), and the linkage of the O-PS repeating unit to the core OS in O-LPS have been elucidated by our group. It is important to establish whether the attachment site of the A-PS repeating unit to the core OS in A-LPS is similar to or differs from that of the O-PS repeating unit in O-LPS. As part of understanding the biosynthetic pathway of the two LPSs inP. gingivalis, PG0129 was identified as an α-mannosyltransferase that is involved in the synthesis of the outer core regions of both O-LPS and A-LPS.

Characterization of the Core Oligosaccharide and the O-Antigen Biological Repeating Unit from Halomonas stevensii Lipopolysaccharide: The First Case of O-Antigen Linked to the Inner Core

2012 ◽  
Vol 18 (12) ◽  
pp. 3729-3735 ◽  
Author(s):  
Giuseppina Pieretti ◽  
Sara Carillo ◽  
Buko Lindner ◽  
Kwang Kyu Kim ◽  
Keun Chul Lee ◽  
...  
Keyword(s):  
Inner Core ◽  
Core Oligosaccharide ◽  
The Core ◽  
O Antigen ◽  
First Case

scholarly journals Lipopolysaccharide Structural Differences between Western and Asian Helicobacter pylori Strains

Toxins ◽  
2018 ◽  
Vol 10 (9) ◽  
pp. 364 ◽  
Author(s):  
Hong Li ◽  
Hong Tang ◽  
Aleksandra Debowski ◽  
Keith Stubbs ◽  
Barry Marshall ◽  
...  
Keyword(s):  
Helicobacter Pylori ◽  
Western World ◽  
Lewis Antigens ◽  
Core Oligosaccharide ◽  
The Core ◽  
O Antigen ◽  
Structural Differences ◽  
H Pylori ◽  
Linker Domain ◽  
Short Core

Recent structural analysis of the lipopolysaccharide (LPS) isolated from Helicobacter pylori G27 wild-type and O-antigen ligase mutant resulted in the redefinition of the core-oligosaccharide and O-antigen domains. The short core-oligosaccharide (Glc–Gal–Hep-III–Hep-II–Hep-I–KDO) and its attached trisaccharide (Trio, GlcNAc–Fuc–Hep) appear to be highly conserved structures among H. pylori strains. The G27 LPS contains a linear glucan–heptan linker between the core-Trio and distal Lewis antigens. This linker domain was commonly identified in Western strains. In contrast, out of 12 partial LPS structures of Asian strains, none displayed the heptan moiety, despite the presence of Lewis antigens. This raises the question of how Lewis antigens are attached to the Trio, and whether the LPS structure of Asian strains contain another linker. Of note, a riban was identified as a linker in LPS of the mouse-adapted SS1 strain, suggesting that alternative linker structures can occur. In summary, additional full structural analyses of LPS in Asian strains are required to assess the presence or absence of an alternative linker in these strains. It will also be interesting to study the glucan-heptan linker moieties in pathogenesis as H. pylori infections in Asia are usually more symptomatic than the ones presented in the Western world.

scholarly journals Structural Analysis of the Core Region of O-Lipopolysaccharide of Porphyromonas gingivalis from Mutants Defective in O-Antigen Ligase and O-Antigen Polymerase

2009 ◽  
Vol 191 (16) ◽  
pp. 5272-5282 ◽  
Author(s):  
Nikolay A. Paramonov ◽  
Joseph Aduse-Opoku ◽  
Ahmed Hashim ◽  
Minnie Rangarajan ◽  
Michael A. Curtis
Keyword(s):  
Porphyromonas Gingivalis ◽  
Inner Core ◽  
Outer Region ◽  
Outer Core ◽  
Core Region ◽  
Resonance Spectroscopy ◽  
Core Oligosaccharide ◽  
Unusual Structure ◽  
The Core ◽  
O Antigen

ABSTRACT Porphyromonas gingivalis synthesizes two lipopolysaccharides (LPSs), O-LPS and A-LPS. Here, we elucidate the structure of the core oligosaccharide (OS) of O-LPS from two mutants of P. gingivalis W50, ΔPG1051 (WaaL, O-antigen ligase) and ΔPG1142 (O-antigen polymerase), which synthesize R-type LPS (core devoid of O antigen) and SR-type LPS (core plus one repeating unit of O antigen), respectively. Structural analyses were performed using one-dimensional and two-dimensional nuclear magnetic resonance spectroscopy in combination with composition and methylation analysis. The outer core OS of O-LPS occurs in two glycoforms: an “uncapped core,” which is devoid of O polysaccharide (O-PS), and a “capped core,” which contains the site of O-PS attachment. The inner core region lacks l(d)-glycero-d(l)-manno-heptosyl residues and is linked to the outer core via 3-deoxy-d-manno-octulosonic acid, which is attached to a glycerol residue in the outer core via a monophosphodiester bridge. The outer region of the “uncapped core” is attached to the glycerol and is composed of a linear α-(1→3)-linked d-Man OS containing four or five mannopyranosyl residues, one-half of which are modified by phosphoethanolamine at position 6. An amino sugar, α-d-allosamine, is attached to the glycerol at position 3. In the “capped core,” there is a three- to five-residue extension of α-(1→3)-linked Man residues glycosylating the outer core at the nonreducing terminal residue. β-d-GalNAc from the O-PS repeating unit is attached to the nonreducing terminal Man at position 3. The core OS of P. gingivalis O-LPS is therefore a highly unusual structure, and it is the basis for further investigation of the mechanism of assembly of the outer membrane of this important periodontal bacterium.

scholarly journals A Fast and Exact Greedy Algorithm for the Core–Periphery Problem

Symmetry ◽  
2020 ◽  
Vol 12 (1) ◽  
pp. 94 ◽  
Author(s):  
Dario Fasino ◽  
Franca Rinaldi
Keyword(s):  
Structural Analysis ◽  
Optimization Problem ◽  
Polynomial Time Algorithm ◽  
Time Algorithm ◽  
Combinatorial Optimization Problem ◽  
Connected Subgraph ◽  
Optimal Solutions ◽  
The Core ◽  
Core Set ◽  
Key Concepts

The core–periphery structure is one of the key concepts in the structural analysis of complex networks. It consists of a partitioning of the node set of a given graph or network into two groups, called core and periphery, where the core nodes induce a well-connected subgraph and share connections with peripheral nodes, while the peripheral nodes are loosely connected to the core nodes and other peripheral nodes. We propose a polynomial-time algorithm to detect core–periphery structures in networks having a symmetric adjacency matrix. The core set is defined as the solution of a combinatorial optimization problem, which has a pleasant symmetry with respect to graph complementation. We provide a complete description of the optimal solutions to that problem and an exact and efficient algorithm to compute them. The proposed approach is extended to networks with loops and oriented edges. Numerical simulations are carried out on both synthetic and real-world networks to demonstrate the effectiveness and practicability of the proposed algorithm.

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