Serotype-converting bacteriophages and O-antigen modification in Shigella flexneri

Allison, Gwen E.; Verma, Naresh K.

doi:10.1016/s0966-842x(99)01646-7

Cited by 277 publications

(317 citation statements)

References 37 publications

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“…Undecaprenol (i.e. C-55 polyprenol)-Pglucose is used to modify the O-antigen with a glucose residue for serotype conversion (39). In E. coli and Salmonella enterica, undecaprenol-P-pentose (4-amino-4-deoxy-L-arabinose) is the monosaccharide donor for the modification of lipid A to increase the resistance to polymyxin antibiotics (40).…”

Section: Discussionmentioning

confidence: 99%

Comparative Analysis of Archaeal Lipid-linked Oligosaccharides That Serve as Oligosaccharide Donors for Asn Glycosylation

Taguchi

Fujinami

Kohda

2016

Journal of Biological Chemistry

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The glycosylation of asparagine residues is the predominant protein modification in all three domains of life. An oligosaccharide chain is preassembled on a lipid-phospho carrier and transferred onto asparagine residues by the action of a membrane-bound enzyme, oligosaccharyltransferase. The oligosaccharide donor for the oligosaccharyl transfer reaction is dolichol-diphosphate-oligosaccharide in Eukaryota and polyprenol-diphosphate-oligosaccharide in Eubacteria. The donor in some archaeal species was reportedly dolichol-monophosphate-oligosaccharide. Thus, the difference in the number of phosphate groups aroused interest in whether the use of the dolichol-monophosphate type donors is widespread in the domain Archaea. Currently, all of the archaeal species with identified oligosaccharide donors have belonged to the phylum Euryarchaeota. Here, we analyzed the donor structures of two species belonging to the phylum Crenarchaeota, Pyrobaculum calidifontis and Sulfolobus solfataricus, in addition to two species from the Euryarchaeota, Pyrococcus furiosus and Archaeoglobus fulgidus. The electrospray ionization tandem mass spectrometry analyses confirmed that the two euryarchaeal oligosaccharide donors were the dolichol-monophosphate type and newly revealed that the two crenarchaeal oligosaccharide donors were the dolichol-diphosphate type. This novel finding is consistent with the hypothesis that the ancestor of Eukaryota is rooted within the TACK (Thaum-, Aig-, Cren-, and Korarchaeota) superphylum, which includes Crenarchaea. Our comprehensive study also revealed that one archaeal species could contain two distinct oligosaccharide donors for the oligosaccharyl transfer reaction. The A. fulgidus cells contained two oligosaccharide donors bearing oligosaccharide moieties with different backbone structures, and the S. solfataricus cells contained two oligosaccharide donors bearing stereochemically different dolichol chains.The glycosylation of asparagine residues is the predominant protein modification throughout all three domains of life (1-3). The oligosaccharides attached to asparagine residues in glycoproteins (N-glycan) affect various properties of the proteins, including folding, conformation, solubility, and antigenicity. Carbohydrate-binding proteins, such as lectins, recognize the N-glycans. Within the lumen of the endoplasmic reticulum in eukaryotic cells, the N-glycan functions as a quality control tag in the endoplasmic reticulum-associated degradation (4). The N-glycosylation occurs in the consensus motif (referred to as the sequon) represented by Asn-Xaa-Ser/Thr, where Xaa can be any residue except Pro. The formation of the N-glycosidic bond, between the monosaccharide residue at the reducing end of an oligosaccharide and the side chain amide group of the asparagine residues in proteins, is catalyzed by a membranebound enzyme, oligosaccharyltransferase (OST) 2 (3). The eukaryotic OST enzyme is a multisubunit protein complex. Among the eight different membrane subunit proteins, the catalytic subunit is a po...

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Section: Discussionmentioning

confidence: 99%

Comparative Analysis of Archaeal Lipid-linked Oligosaccharides That Serve as Oligosaccharide Donors for Asn Glycosylation

Taguchi

Fujinami

Kohda

2016

Journal of Biological Chemistry

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“…In addition to possessing these general Mu-like phage features, BcepMu additionally encodes a specific potential virulence factor: an acyltransferase homolog encoded by gene53. The acyltransferase encoded by Shigella phage Sf6 modifies the LPS O-antigen, resulting in serotype conversion and protection from superinfection [45,46]. The B. cenocepacia ET12 type strain J2315 is a BcepMu lysogen, whereas the related ET12 strain K56-2 lacks BcepMu [34].…”

Section: Mu and P2-related Phages Of Burkholderiamentioning

confidence: 99%

Role of phages in the pathogenesis of Burkholderia, or ‘Where are the toxin genes in Burkholderia phages?’

Summer

Gill

Upton

et al. 2007

Current Opinion in Microbiology

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“…43) and Salmonella spp (44). It is not known exactly at what stage this O antigen glucosylation occurs, but it is thought to occur prior to, or during, O antigen polymerization rather than after (45).…”

Section: Discussionmentioning

confidence: 99%

Post-assembly Modification of Bordetella bronchiseptica O Polysaccharide by a Novel Periplasmic Enzyme Encoded by wbmE

King

Vinogradov

Preston

et al. 2009

Journal of Biological Chemistry

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Bordetella bronchiseptica is a pathogen of humans and animals that colonizes the respiratory tract. It produces a lipopolysaccharide O antigen that contains a homopolymer of 2,3-dideoxy-2,3-diacetamido-L-galacturonic acid (L-GalNAc3NAcA). Some of these sugars are found in the uronamide form (L-GalNAc3NAcAN), and there is no discernible pattern in the distribution of amides along the chain. A B. bronchiseptica wbmE mutant expresses an O polysaccharide unusually rich in uronamides. The WbmE protein localizes to the periplasm and catalyzes the deamidation of uronamide-rich O chains in lipopolysaccharide purified from the mutant, to attain a wildtype uronamide/uronic acid ratio. WbmE is a member of the papain-like transglutaminase superfamily, and this categorization is consistent with a deamidase role. The periplasmic location of WbmE and its acceptance of complete lipopolysaccharide as substrate indicate that it operates at a late stage in lipopolysaccharide biosynthesis, after polymerization and export of the O chain from the cytoplasm. This is the first report of such a modification of O antigen after assembly. The expression of wbmE is controlled by the Bordetella virulence gene two-component regulatory system, BvgAS, suggesting that this deamidation is a novel mechanism by which these bacteria modify their cell surface charge in response to environmental stimuli.Bordetella bronchiseptica is a Gram-negative coccobacillus, which colonizes the mammalian respiratory tract. It has a broad host range and is commonly associated with atrophic rhinitis in pigs (1) and infectious tracheobronchitis (kennel cough) in dogs (2). Most of the genes implicated in host colonization and virulence are under the transcriptional control of the two-component regulatory system BvgAS (reviewed in Ref. One of the Bvg-regulated bacterial structures is lipopolysaccharide (LPS).3 LPS is the major component of the outer leaflet of the outer membrane. LPS has three domains: first, Lipid A is the lipophilic domain that anchors LPS into the outer membrane; second, a complex, branched-chain oligosaccharide known as core is attached to lipid A and in Bordetella the lipid A-core structure is known as B-band LPS; third, a domain distal to the membrane consisting of saccharide repeats may be present, which is commonly called O antigen. In a proportion of B. bronchisepica LPS molecules the lipid A core is substituted with a trisaccharide, and this species is known as A-band LPS. The O polysaccharide consists of a homopolymer of 2,3-dideoxy-2,3-diacetamido-L-galacturonic acid (L-GalNAc3NAcA) (7) capped at the nonreducing terminus with a complex 2,3,4-trideoxy-2,3,4-triamino galacturonamide (GalN3N4NAN) derivative (8), and in B. bronchiseptica is attached to the A-band trisaccharide via a pentasaccharide linker (Fig. 1) (9). Expression of O antigen by B. bronchiseptica is required for full virulence in animal models of infection and for resistance to complement-mediated killing (10).A proportion of the O polysaccharide repeating units are present as ...

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Serotype-converting bacteriophages and O-antigen modification in Shigella flexneri

Cited by 277 publications

References 37 publications

Comparative Analysis of Archaeal Lipid-linked Oligosaccharides That Serve as Oligosaccharide Donors for Asn Glycosylation

Comparative Analysis of Archaeal Lipid-linked Oligosaccharides That Serve as Oligosaccharide Donors for Asn Glycosylation

Role of phages in the pathogenesis of Burkholderia, or ‘Where are the toxin genes in Burkholderia phages?’

Post-assembly Modification of Bordetella bronchiseptica O Polysaccharide by a Novel Periplasmic Enzyme Encoded by wbmE

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