Lipo-oligosaccharides (LOS) of mucosal pathogens: Molecular mimicry and host-modification of LOS

Mandrell, Robert E.; Apicella, Michael A.

doi:10.1016/s0171-2985(11)80352-9

Cited by 176 publications

(138 citation statements)

References 70 publications

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“…This structure has been reported for strain 1291b (3) and reacts with mAb 1-17-L1. The fact that these structures are mimics of human glycolipids has been noted previously (7). The ca chain may be the pentasaccharide GalNAc [31-3Ga1131-4GlcNAc[31-3Ga1131-4Glc, which is identical to the human red cell X 2 antigen (8).…”

Section: Sultlnlarymentioning

confidence: 79%

“…The ca chain may be the pentasaccharide GalNAc [31-3Ga1131-4GlcNAc[31-3Ga1131-4Glc, which is identical to the human red cell X 2 antigen (8). When the terminal GalNAc is not added, the tetrasaccharide is identical to lacto-N-neotetraose, the core structure of the blood group substances (7). The Galc~l-4Gal~l-4Glc trisaccharide is found on globotriglycosyl ceramide or the pk blood group antigen (7).…”

Section: Sultlnlarymentioning

confidence: 99%

“…When the terminal GalNAc is not added, the tetrasaccharide is identical to lacto-N-neotetraose, the core structure of the blood group substances (7). The Galc~l-4Gal~l-4Glc trisaccharide is found on globotriglycosyl ceramide or the pk blood group antigen (7). Finally, the c~ chain can be limited to a disaccharide lactosyl unit and is then identical to lactosylceramide.…”

Section: Sultlnlarymentioning

confidence: 99%

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Variation of gonococcal lipooligosaccharide structure is due to alterations in poly-G tracts in lgt genes encoding glycosyl transferases.

Yang

Gotschlich

1996

The Journal of Experimental Medicine

116

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SUlTlnlaryThe lipooligosaccharide (LOS) expressed by gonococci spontaneously varies its structure at high frequency, but the underlying genetic mechanism has not been described. We have previously reported that the genes encoding the glycosyl transferases responsible for the biosynthesis of the variable o~ chain of the LOS of Neisseria gonorrhoeae are located in a locus containing five genes, lgtA, lgtB, IgtC, IgtD, and lgtE. Sequence analysis showed that tgtA, lgtC, and IgtD contained poly-G tracts within the coding frames, leading to the hypothesis that shiftsin the number of guanosine residues in the poly-G tracts might be responsible for the.high frequency variation in structure of gonococcal LOS. We now provide experimental evidence confirming this hypothesis.

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Section: Sultlnlarymentioning

confidence: 79%

Section: Sultlnlarymentioning

confidence: 99%

Section: Sultlnlarymentioning

confidence: 99%

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Variation of gonococcal lipooligosaccharide structure is due to alterations in poly-G tracts in lgt genes encoding glycosyl transferases.

Yang

Gotschlich

1996

The Journal of Experimental Medicine

116

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“…The core oligosaccharide structures reported so far indicate that LPSs of different Haemophilus species have a common inner core (9,22,25,26,29,30). This suggests that the frequent switching of LPS antigenic determinants (phase variation) observed for this genus may be a result of changes in the outer core, which in addition may be sialylated (9,17,21).…”

mentioning

confidence: 89%

Monoclonal antibodies againstHaemophilus ducreyi lipooligosaccharide and their diagnostic usefulness

Ahmed

Borrelli

Jonasson

et al. 1995

Eur. J. Clin. Microbiol. Infect. Dis.

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Mouse monoclonal antibodies (MAbs) DP8 [immunoglobulin G1()] and DH24 [immunoglobulin M()], which are specific for Haemophilus ducreyi lipopolysaccharide (LPS), were generated by fusing mouse myeloma NS0 cells with spleen cells of BALB/c mice immunized with a total membrane preparation of H. ducreyi. MAb DP8 reacted in whole-cell enzyme immunoassay (EIA) and colony dot immunoblotting with all 50 strains of H. ducreyi but not with any other bacteria tested, which suggests an exposed and species-specific epitope on the H. ducreyi cell surface. This conclusion was supported by the finding that DP8 bound to all six H. ducreyi LPSs tested but not to any of the Haemophilus influenzae or enterobacterial LPSs or synthetic glycoconjugates. The MAb DH24 bound to 43 of 50 strains of H. ducreyi and to few strains of H. influenzae, Neisseria gonorrhoeae, and Neisseria meningitidis, as evaluated by whole-cell EIA and colony dot immunoblotting. The MAb DH24 reacted with five of the six H. ducreyi LPSs tested and with the lacto-N-neotetraose (Gal␤134GlcNAc␤133Gal␤13 4Glc) series of synthetic glycoconjugates, as determined by EIA. By using polysaccharides obtained after both mild acidic hydrolysis and strong alkali treatment and dephosphorylated samples as inhibitors of the MAbs binding to H. ducreyi LPS antigens, it could be shown that phosphate groups were essential for the binding of DP8 to LPS but that they did not affect antigenic recognition by DH24. None of the MAbs bound to isolated lipid A, but aggregation caused by the fatty acids of lipid A was essential for epitope recognition.

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“…possesses an active T4SS composed of an innermembrane complex, an outer-membrane complex, and several cytoplasmic chaperone proteins to release ssDNA into the environment for horizontal gene transfer (35). Neisseria shares multiple similarities with NTHI, including noted mosaicism between genomes, despite each organism failing to recognize each other's uptake signal sequence (46)(47)(48). Bioinformatic analysis of the NTHI strain 86-028NP genome identified several genes that are homologous to those of the Neisseria T4SS.…”

Section: Resultsmentioning

confidence: 99%

NontypeableHaemophilus influenzaereleases DNA and DNABII proteins via a T4SS-like complex and ComE of the type IV pilus machinery

Jurcisek

Brockman

Novotny

et al. 2017

Proc. Natl. Acad. Sci. U.S.A.

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Biofilms formed by nontypeable Haemophilus influenzae (NTHI) are central to the chronicity, recurrence, and resistance to treatment of multiple human respiratory tract diseases including otitis media, chronic rhinosinusitis, and exacerbations of both cystic fibrosis and chronic obstructive pulmonary disease. Extracellular DNA (eDNA) and associated DNABII proteins are essential to the overall architecture and structural integrity of biofilms formed by NTHI and all other bacterial pathogens tested to date. Although cell lysis and outermembrane vesicle extrusion are possible means by which these canonically intracellular components might be released into the extracellular environment for incorporation into the biofilm matrix, we hypothesized that NTHI additionally used a mechanism of active DNA release. Herein, we describe a mechanism whereby DNA and associated DNABII proteins transit from the bacterial cytoplasm to the periplasm via an inner-membrane pore complex (TraC and TraG) with homology to type IV secretion-like systems. These components exit the bacterial cell through the ComE pore through which the NTHI type IV pilus is expressed. The described mechanism is independent of explosive cell lysis or cell death, and the release of DNA is confined to a discrete subpolar location, which suggests a novel form of DNA release from viable NTHI. Identification of the mechanisms and determination of the kinetics by which critical biofilm matrix-stabilizing components are released will aid in the design of novel biofilmtargeted therapeutic and preventative strategies for diseases caused by NTHI and many other human pathogens known to integrate eDNA and DNABII proteins into their biofilm matrix.eDNA | Tra | secretin | IHF | HU B iofilms contribute substantially to the chronic and recurrent nature of many bacterial diseases of humans and animals, including those of the airway, urogenital tract, skin, and oral cavity (1-3). Bacteria within a biofilm are protected from environmental stresses by a self-produced extracellular matrix, called the extrapolymeric substance (EPS), whose composition varies greatly depending upon the microbes that produce it and the environment in which it is formed. Despite vast compositional variability, the EPS is typically composed of a complex mixture of lipopolysaccharides, proteins, lipids, glycolipids, and nucleic acids (4). Extracellular DNA (eDNA) is a major constituent of the EPS formed by multiple human pathogens (5-7) and serves diverse roles within the bacterial biofilm. eDNA provides structural stability to the matrix, acts as a sink for antimicrobial peptides, protects resident bacteria from the host immune response, provides a source of "common goods" for the resident bacteria, acts as a universal structural material conducive to microbial community architecture, and facilitates the uptake of genetic material between bacterial species via a process known as horizontal gene transfer (5,(8)(9)(10)(11)(12)(13)(14)(15)(16)(17). Members of the DNABII family of DNA-binding proteins, integ...

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Lipo-oligosaccharides (LOS) of mucosal pathogens: Molecular mimicry and host-modification of LOS

Cited by 176 publications

References 70 publications

Variation of gonococcal lipooligosaccharide structure is due to alterations in poly-G tracts in lgt genes encoding glycosyl transferases.

Variation of gonococcal lipooligosaccharide structure is due to alterations in poly-G tracts in lgt genes encoding glycosyl transferases.

Monoclonal antibodies againstHaemophilus ducreyi lipooligosaccharide and their diagnostic usefulness

NontypeableHaemophilus influenzaereleases DNA and DNABII proteins via a T4SS-like complex and ComE of the type IV pilus machinery

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