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PubMed1992

Identification and sequences of the lipopolysaccharide core biosynthetic genes rfaQ, rfaP, and rfaG of Escherichia coli K-12.

The rfa locus of Escherichia coli K-12 includes a block of about 10 closely spaced genes transcribed in the same direction which are involved in synthesis and modification of the hexose region of the lipopolysaccharide core. We have sequenced the first three genes in this block. The function of the first of these genes is unknown, but we have designated it rfaQ on the basis of its location and similarity to other rfa genes. Complementation of Salmonella typhimurium rfa mutants with E. coli rfa restriction fragments indicated that the second and third genes in the block were rfaG and rfaP. The deduced sizes of the RfaQ, RfaG, and RfaP proteins are 36,298, 42,284, and 30,872 Da, respectively, and the proteins are basic and lack extensive hydrophobic domains. RfaQ shares regions of homology with proteins RfaC and RfaF, which are involved in synthesis of the heptose region of the core. Proteins RfaB, RfaG, and RfaK share a region of homology, which suggests that they belong to a second family of Rfa proteins which are thought to be hexose transferases.

Amino Acid Sequence↗

PubMed1994

Structural studies of the side chain of outer membrane lipopolysaccharide from Pseudomonas syringae pv. coriandricola W-43.

The lipopolysaccharide (LPS) was isolated from Pseudomonas syringae pv. coriandricola W-43 by hot phenol-water extraction. Rhamnose and 3-N-acetyl-3-deoxyfucose were found to be the major sugar constituents of the LPS together with N-acetylglucosamine, N-acetylgalactosamine, heptose, and 3-deoxy-D-manno-octulosonic acid (Kdo). The main fatty acids of lipid A of the LPS were 3-OH-C:10, C12:0, 2-OH-C12:0, and 3-OH-C12:0. The O-specific polysaccharide liberated from the LPS by mild-acid hydrolysis was purified by gel permeation chromatography. The compositional analysis of the O-specific polysaccharide revealed the presence of L-rhamnose and 3-N-acetyl-3-deoxy-D-fucose in a molar ratio of 4:1. The primary structure of the O-specific polysaccharide was established by methylation analysis together with 1H and 13C nuclear magnetic resonance spectroscopy, including two-dimensional shift-correlated and one-dimensional nuclear Overhauser effect spectroscopy. The polysaccharide moiety was found to consist of a tetrasaccharide rhamnan backbone, and 3-N-acetyl-3-deoxy-D-fucose constitutes the side chain of the branched pentasaccharide repeating unit of the polysaccharide.

Carbohydrate Sequence↗

PubMed1996

Molecular cloning of the Haemophilus influenzae gmhA (lpcA) gene encoding a phosphoheptose isomerase required for lipooligosaccharide biosynthesis.

We have determined that gene HI#1181 of Haemophilus influenzae is a homolog of Escherichia coli gmhA (previously designated lpcA) (J. S. Brooke and M. A. Valvano, J. Biol. Chem. 271:3608-3614, 1996), which encodes a phosphoheptose isomerase catalyzing the first step of the biosynthesis of ADP-L-glycero-D-manno heptose. Mutations in this gene are associated with a heptoseless core lipopolysaccharide which determines an increased outer membrane permeability to hydrophobic compounds. The cloned H. influenzae gmhA restored the synthesis of a complete core in the gmhA-deleted E. coli strain chi711. Amino acid sequence comparisons of the GmhA proteins of E. coli and H. influenzae with other proteins in the databases revealed the existence of a novel family of phosphosugar a1do-keto isomerases.

Aldose-Ketose Isomerases↗

PubMed1996

Inner core biosynthesis of lipooligosaccharide (LOS) in Neisseria meningitidis serogroup B: identification and role in LOS assembly of the alpha1,2 N-acetylglucosamine transferase (RfaK).

A lipooligosaccharide (LOS) mutant of Neisseria meningitidis serogroup B strain NMB (immunotype L3,7,9) was identified in a Tn916 (tetM) mutant bank by loss of reactivity with monoclonal antibody 3F11, which recognizes the terminal Galbeta1-->4GlcNAc epitope in the lacto-N-neotetraose moiety of the wild-type LOS structure. The mutant, designated 559, was found to express a truncated LOS of 3.0 kDa. Southern and PCR analyses demonstrated that there was a single intact Tn916 insertion (class I) in the mutant 559 chromosome. Linkage of the LOS phenotype and the Tn916 insertion was confirmed by transformation of the wild-type parent. Nucleotide sequence analysis of the region surrounding the transposition site revealed a 1,065-bp open reading frame (ORF). A homology search of the GenBank/EMBL database revealed that the amino acid sequence of this ORF had 46.8% similarity and 21.2% identity with the alpha1,2 N-acetylglucosamine transferase (RfaK) from Salmonella typhimurium. Glycosyl composition and linkage analysis of the LOS produced by mutant 559 revealed that the lacto-N-neotetraose group which is attached to heptose I (HepI) and the N-acetylglucosamine and glucose residues that are attached to HepII in the inner core of the parental LOS were absent. These analyses also showed that the HepII residue in both the parent and the mutant LOS molecules was phosphorylated, presumably by a phosphoethanolamine substituent. The insertion of nonpolar and polar antibiotic resistance cartridges into the parental rfaK gene resulted in the expression of LOS with the same mobility as that produced by mutant 559. This result indicated that the inability to add the lacto-N-neotetraose group to the 559 LOS is not due to a polar effect on a gene(s) downstream of rfaK. Our data indicate that we have identified the meningococcal alpha1,2 N-acetylglucosamine transferase responsible for the addition of N-acetylglucosamine to HepII. We propose that the lack of alpha-chain extension from HepI in the LOS of mutant 559 may be due to structural constraints imposed by the incomplete biosynthesis of the LOS inner core.

Amino Acid Sequence↗

PubMed1996

A novel cell surface polysaccharide in Pseudomonas putida WCS358, which shares characteristics with Escherichia coli K antigens, is not involved in root colonization.

Previously we have shown that flagella and the O-specific polysaccharide of lipopolysaccharide play a role in colonization of the potato root by plant growth-promoting Pseudomonas strains WCS374 and WCS358. In this paper, we describe a novel cell surface-exposed structure in Pseudomonas putida WCS358 examined with a specific monoclonal antibody. This cell surface structure appeared to be a polysaccharide, which was accessible to the monoclonal antibody at the outer cell surface. Further study revealed that it does not contain 2-keto-3-deoxyoctonate, heptose, or lipid A, indicating that it is not a second type of lipopolysaccharide. Instead, the polysaccharide shared some characteristics with K antigen described for Escherichia coli. From a series of 49 different soil bacteria tested, only one other potato plant growth-promoting Pseudomonas strain reacted positively with the monoclonal antibody. Mutant cells lacking the novel antigen were efficiently isolated by an enrichment method involving magnetic antibodies. Mutant strains defective in the novel antigen contained normal lipopolysaccharide. One of these mutants was affected in neither its ability to adhere to sterile potato root pieces nor its ability to colonize potato roots. We conclude that the bacterial cell surface of P. putida WCS358 contains at least two different polysaccharide structures. These are the O-specific polysaccharide of lipopolysaccharide, which is relevant for potato root colonization, and the novel polysaccharide, which is not involved in adhesion to or colonization of the potato root.

Animals↗

PubMed1997

Isolation and characterization of two genes, waaC (rfaC) and waaF (rfaF), involved in Pseudomonas aeruginosa serotype O5 inner-core biosynthesis.

Recent studies have provided evidence to implicate involvement of the core oligosaccharide region of Pseudomonas aeruginosa lipopolysaccharide (LPS) in adherence to host tissues. To better understand the role played by LPS in the virulence of this organism, the aim of the present study was to clone and characterize genes involved in core biosynthesis. The inner-core regions of P. aeruginosa and Salmonella enterica serovar Typhimurium are structurally very similar; both contain two main chain residues of heptose linked to lipid A-Kdo2 (Kdo is 3-deoxy-D-manno-octulosonic acid). By electrotransforming a P. aeruginosa PAO1 library into Salmonella waaC and waaF (formerly known as rfaC and rfaF, respectively) mutants, we were able to isolate the homologous heptosyltransferase I and II genes of P. aeruginosa. Two plasmids, pCOREc1 and pCOREc2, which restored smooth LPS production in the waaC mutant, were isolated. Similarly, plasmid pCOREf1 was able to complement the Salmonella waaF mutant. Sequence analysis of the DNA insert of pCOREc2 revealed one open reading frame (ORF) which could code for a protein of 39.8 kDa. The amino acid sequence of the deduced protein exhibited 53% identity with the sequence of the WaaC protein of S. enterica serovar Typhimurium. pCOREf1 contained one ORF capable of encoding a 38.4-kDa protein. The sequence of the predicted protein was 49% identical to the sequence of the Salmonella WaaF protein. Protein expression by the Maxicell system confirmed that a 40-kDa protein was encoded by pCOREc2 and a 38-kDa protein was encoded by pCOREf1. Pulsed-field gel electrophoresis was used to determine the map locations of the cloned waaC and waaF genes, which were found to lie between 0.9 and 6.6 min on the PAO1 chromosome. Using a gene-replacement strategy, we attempted to generate P. aeruginosa waaC and waaF null mutants. Despite multiple attempts to isolate true knockout mutants, all transconjugants were identified as merodiploids.

Bacterial Proteins↗

PubMed2000

Mutation of the lipopolysaccharide core glycosyltransferase encoded by waaG destabilizes the outer membrane of Escherichia coli by interfering with core phosphorylation.

In Escherichia coli, phosphoryl substituents in the lipopolysaccharide core region are essential for outer membrane stability. Mutation of the core glucosyltransferase encoded by waaG (formerly rfaG) resulted in lipopolysaccharide truncated immediately after the inner core heptose residues, which serve as the sites for phosphorylation. Surprisingly, mutation of waaG also destabilized the outer membrane. Structural analyses of waaG mutant lipopolysaccharide showed that the cause for this phenotype was a decrease in core phosphorylation, an unexpected side effect of the waaG mutation.

Acylation↗

PubMed2001

Genetic characterization of the Klebsiella pneumoniae waa gene cluster, involved in core lipopolysaccharide biosynthesis.

A recombinant cosmid containing genes involved in Klebsiella pneumoniae C3 core lipopolysaccharide biosynthesis was identified by its ability to confer bacteriocin 28b resistance to Escherichia coli K-12. The recombinant cosmid contains 12 genes, the whole waa gene cluster, flanked by kbl and coaD genes, as was found in E. coli K-12. PCR amplification analysis showed that this cluster is conserved in representative K. pneumoniae strains. Partial nucleotide sequence determination showed that the same genes and gene order are found in K. pneumoniae subsp. ozaenae, for which the core chemical structure is known. Complementation analysis of known waa mutants from E. coli K-12 and/or Salmonella enterica led to the identification of genes involved in biosynthesis of the inner core backbone that are shared by these three members of the Enterobacteriaceae. K. pneumoniae orf10 mutants showed a two-log-fold reduction in a mice virulence assay and a strong decrease in capsule amount. Analysis of a constructed K. pneumoniae waaE deletion mutant suggests that the WaaE protein is involved in the transfer of the branch beta-D-Glc to the O-4 position of L-glycero-D-manno-heptose I, a feature shared by K. pneumoniae, Proteus mirabilis, and Yersinia enterocolitica.

Animals↗

PubMed2002

Characterization of the Campylobacter jejuni heptosyltransferase II gene, waaF, provides genetic evidence that extracellular polysaccharide is lipid A core independent.

Campylobacter jejuni produces both lipooligosaccharide (LOS) and a higher-molecular-weight polysaccharide that is believed to form a capsule. The role of these surface polysaccharides in C. jejuni-mediated enteric disease is unclear; however, epitopes associated with the LOS are linked to the development of neurological complications. In Escherichia coli and Salmonella enterica serovar Typhimurium the waaF gene encodes a heptosyltransferase, which catalyzes the transfer of the second L-glycero-D-manno-heptose residue to the core oligosaccharide moiety of lipopolysaccharide (LPS), and mutation of waaF results in a truncated core oligosaccharide. In this report we confirm experimentally that C. jejuni gene Cj1148 encodes the heptosyltransferase II enzyme, WaaF. The Campylobacter waaF gene complements an S. enterica serovar Typhimurium waaF mutation and restores the ability to produce full-sized lipopolysaccharide. To examine the role of WaaF in C. jejuni, waaF mutants were constructed in strains NCTC 11168 and NCTC 11828. Loss of heptosyltransferase activity resulted in the production of a truncated core oligosaccharide, failure to bind specific ligands, and loss of serum reactive GM(1), asialo-GM(1), and GM(2) ganglioside epitopes. The mutation of waaF did not affect the higher-molecular-weight polysaccharide supporting the production of a LOS-independent capsular polysaccharide by C. jejuni. The exact structural basis for the truncation of the core oligosaccharide was verified by comparative chemical analysis. The NCTC 11168 core oligosaccharide differs from that known for HS:2 strain CCUG 10936 in possessing an extra terminal disaccharide of galactose-beta(1,3) N-acetylgalactosamine. In comparison, the waaF mutant possessed a truncated molecule consistent with that observed with waaF mutants in other bacterial species.

Campylobacter jejuni↗

PubMed2004

lpt6, a gene required for addition of phosphoethanolamine to inner-core lipopolysaccharide of Neisseria meningitidis and Haemophilus influenzae.

We previously described a gene, lpt3, required for the addition of phosphoethanolamine (PEtn) at the 3 position on the beta-chain heptose (HepII) of the inner-core Neisseria meningitidis lipopolysaccharide (LPS), but it has long been recognized that the inner-core LPS of some strains possesses PEtn at the 6 position (PEtn-6) on HepII. We have now identified a gene, lpt6 (NMA0408), that is required for the addition of PEtn-6 on HepII. The lpt6 gene is located in a region previously identified as Lgt-3 and is associated with other LPS biosynthetic genes. We screened 113 strains, representing all serogroups and including disease and carriage strains, for the lpt3 and lpt6 genes and showed that 36% contained both genes, while 50% possessed lpt3 only and 12% possessed lpt6 only. The translated amino acid sequence of lpt6 has a homologue (72.5% similarity) in a product of the Haemophilus influenzae Rd genome sequence. Previous structural studies have shown that all H. influenzae strains investigated have PEtn-6 on HepII. Consistent with this, we found that, among 70 strains representing all capsular serotypes and nonencapsulated H. influenzae strains, the lpt6 homologue was invariably present. Structural analysis of LPS from H. influenzae and N. meningitidis strains where lpt6 had been insertionally inactivated revealed that PEtn-6 on HepII could not be detected. The translated amino acid sequences from the N. meningitidis and H. influenzae lpt6 genes have conserved residues across their lengths and are part of a family of proven or putative PEtn transferases present in a wide range of gram-negative bacteria.

Amino Acid Sequence↗

PubMed2005

OpsX from Haemophilus influenzae represents a novel type of heptosyltransferase I in lipopolysaccharide biosynthesis.

The inner core region of the lipopolysaccharide (LPS) of Haemophilus influenzae is characterized by the presence of a phosphorylated 3-deoxy-alpha-D-manno-octulosonic acid (Kdo). In this study, we show that the heptosyltransferase I adding the first L-glycero-D-manno-heptose residue to this acceptor is encoded by the gene opsX, which differs in substrate specificity from the other heptosyltransferase I, known as WaaC.

Bacterial Proteins↗

PubMed2006

Glycosylation of the self-recognizing Escherichia coli Ag43 autotransporter protein.

Glycosylation is a common modulation of protein function in eukaryotes and is biologically important. However, in bacteria protein glycosylation is rare, and relatively few bacterial glycoproteins are known. In Escherichia coli only two glycoproteins have been described to date. Here we introduce a novel member to this exclusive group, namely, antigen 43 (Ag43), a self-recognizing autotransporter protein. By mass spectrometry Ag43 was demonstrated to be glycosylated by addition of heptose residues at several positions in the passenger domain. Glycosylation of Ag43 by the action of the Aah and TibC glycosyltransferases was observed in laboratory strains. Importantly, Ag43 was also found to be glycosylated in a wild-type strain, suggesting that Ag43-glycosylation may be a widespread phenomenon. Glycosylation of Ag43 does not seem to interfere with its self-associating properties. However, the glycosylated form of Ag43 enhances bacterial binding to human cell lines, whereas the nonglycosylated version of Ag43 does not to confer this property.

Adhesins, Bacterial↗

PubMed2006

A complete lipopolysaccharide inner core oligosaccharide is required for resistance of Burkholderia cenocepacia to antimicrobial peptides and bacterial survival in vivo.

Burkholderia cenocepacia is an important opportunistic pathogen of patients with cystic fibrosis. This bacterium is inherently resistant to a wide range of antimicrobial agents, including high concentrations of antimicrobial peptides. We hypothesized that the lipopolysaccharide (LPS) of B. cenocepacia is important for both virulence and resistance to antimicrobial peptides. We identified hldA and hldD genes in B. cenocepacia strain K56-2. These two genes encode enzymes involved in the modification of heptose sugars prior to their incorporation into the LPS core oligosaccharide. We constructed a mutant, SAL1, which was defective in expression of both hldA and hldD, and by performing complementation studies we confirmed that the functions encoded by both of these B. cenocepacia genes were needed for synthesis of a complete LPS core oligosaccharide. The LPS produced by SAL1 consisted of a short lipid A-core oligosaccharide and was devoid of O antigen. SAL1 was sensitive to the antimicrobial peptides polymyxin B, melittin, and human neutrophil peptide 1. In contrast, another B. cenocepacia mutant strain that produced complete lipid A-core oligosaccharide but lacked polymeric O antigen was not sensitive to polymyxin B or melittin. As determined by the rat agar bead model of lung infection, the SAL1 mutant had a survival defect in vivo since it could not be recovered from the lungs of infected rats 14 days postinfection. Together, these data show that the B. cenocepacia LPS inner core oligosaccharide is needed for in vitro resistance to three structurally unrelated antimicrobial peptides and for in vivo survival in a rat model of chronic lung infection.

Animals↗

PubMed2006

Mutation of waaC, encoding heptosyltransferase I in Campylobacter jejuni 81-176, affects the structure of both lipooligosaccharide and capsular carbohydrate.

Campylobacter jejuni 81-176 lipooligosaccharide (LOS) is composed of two covalently linked domains: lipid A, a hydrophobic anchor, and a nonrepeating core oligosaccharide, consisting of an inner and outer core region. We report the isolation and characterization of the deepest rough C. jejuni 81-176 mutant by insertional mutagenesis into the waaC gene, encoding heptosyltransferase I that catalyzes the transfer of the first L-glycero-D-manno-heptose residue to 3-deoxy-D-manno-octulosonic residue (Kdo)-lipid A. Tricine gel electrophoresis, followed by silver staining, showed that site-specific mutation in the waaC gene resulted in the expression of a severely truncated LOS compared to wild-type strain 81-176. Gas-liquid chromatography-mass spectrometry and nuclear magnetic resonance spectroscopy showed that the waaC LOS species lacked all sugars distal to Kdo-lipid A. Parallel structural studies of the capsular polysaccharides of the wild-type strain 81-176 and waaC mutant revealed loss of the 3-O-methyl group in the waaC mutant. Complementation of the C. jejuni mutant by insertion of the wild-type C. jejuni waaC gene into a chromosomal locus resulted in LOS and capsular structures identical to those expressed in the parent strain. We also report here the presence of O-methyl phosphoramidate in wild-type strain 81-176 capsular polysaccharide.

Bacterial Capsules↗

PubMed1965

COMPARISON OF LIPIDS AND LIPOPOLYSACCHARIDE FROM THE BACILLARY AND L FORMS OF PROTEUS P18.

Nesbitt, J. A., III (The Johns Hopkins University School of Medicine, Baltimore, Md.), and W. J. Lennarz. Comparison of lipids and lipopolysaccharides from the bacillary and L forms of Proteus P18. J. Bacteriol. 89:1020-1025. 1965.-Comparative studies on the L form of Proteus P18 and the parent bacterium grown in a defined medium showed that the L form contained 1.5 times as much extractable lipid (dry weight) as the bacillary form. The composition of the lipids extractable by chloroform-methanol was quite similar in the two bacterial forms. The occurrence of myristate and beta-hydroxymyristate in the bound, nonextractable lipid was found to be a reflection of the presence of lipopolysaccharide (LPS) in each organism. The bacillary organism contains three to four times as much LPS as the L form. The LPS isolated from both organisms contains heptose, hexosamine, phosphorus, 3-deoxyoctulosonate, glucose, galactose, and fatty acids.

Bacillus↗

PubMed1966

Cell wall lipopolysaccharides from xanthomonas species.

Volk, Wesley A. (University of Virginia, Charlottesville). Cell wall lipopolysaccharides from Xanthomonas species. J. Bacteriol. 91:39-42. 1966.-The lipopolysaccharides from 20 species of Xanthomonas were extracted and purified. Biological studies suggest that these lipopolysaccharides are analogous to the endotoxins extracted from enteric organisms, as judged by their mouse lethality and their ability to provoke the local Shwartzman reaction in rabbits. Studies on the composition of the polysaccharides revealed that all contained uronic acid, glucose, mannose, and a compound apparently identical to the 2-keto-3-deoxyoctonate previously described in enteric organisms. The polysaccharide also contains organic phosphate, and additional carbohydrates such as rhamnose, xylose, fucose, and galactose are found in some, but not all, species. In contrast to the composition of the enteric lipopolysaccharides, heptose was not found in any of the lipopolysaccharides of the Xanthomonas species studied.

Journal Article↗

PubMed1967

Transduction by bacteriophage P22 in nonsmooth mutants of Salmonella typhimurium.

The general transducing phage P22 attacks only smooth (S) Salmonella with O antigen 12, determined by the oligosaccharide repeating unit constituting the distal part of the somatic lipopolysaccharide (LPS) side chain; non-S mutants, whose LPS contain few or no O repeating units, appear to be resistant. Auxotrophic non-S mutants of Salmonella typhimurium LT2 were tested as transductional recipients. Some transductants (0.5 to 5% as many as from S recipients) were obtained from most semirough recipients, either of class D (presumed leaky rouA mutants) or of a class due to mutation near his (presumed leaky rouB mutants), and from recipients lacking uridine diphosphogalactose epimerase or phosphomannose isomerase. Transductants were not obtained from several rouA, rouB, "heptose-negative," and glucose-1-transferase mutants, nor from most semirough class C mutants, whose LPS side chains each bear a single O oligosaccharide unit. Most transductants evoked from non-S recipients by temperate (c(+)) phage P22 were nonlysogenic, and virulent P22.c2 phage was about as effective as P22.c(+) in transduction to non-S recipients; probably all P22 transducing particles neither lysogenize nor kill. The extended-host-range mutant P22h gave qualitatively similar results,but evoked 5- to 30-fold more transductants from some non-S recipients than did P22. Probably, the LPS of non-S mutants susceptible to transduction contains a few O-specific oligosaccharide units, conferring a slight ability to adsorb P22 and a greater ability to adsorb P22h.

Genetics↗

PubMed1968

Morphology and chemistry of cell walls of Micrococcus radiodurans.

Walls of the pigmented strain of Micrococcus radiodurans showed several layers in the electron microscope. These layers include an outermost network structure removed by trypsin, a fragile soft layer containing hexagonally packed subunits, and a rigid layer penetrated by numerous holes. The two inner layers were separated by a process of autolysis, trypsin treatment, and gradient centrifugation. The hexagonally packed layer was less dense, pink in color, and it contained carotenoids, lipid, protein, and polysaccharide. The lipid consisted of odd-numbered as well as even-numbered fatty acids, and the polysaccharide contained rhamnose and mannose, but it did not contain heptose. The "holey" layer was white and was composed of a mucopeptide containing glucosamine, muramic acid, and four main amino acids (glutamic acid, alanine, glycine, and l-ornithine, in the ratios of 1:1.7:1.8:1.2, respectively). This layer also contained phosphorus, glucose, and a trace of meso- and ll-diaminopimelic acid. A white mutant, W(1), of M. radiodurans had no pigment or lipid in its walls, but it contained small amounts of the "hexagonal" layer. The holey layer, constituting the bulk of the wall, was similar in morphology and composition to that layer in the pigmented strain. Lysozyme did not remove the lipoprotein-polysaccharide component from the walls of the pigmented strains, and the hexagonally packed structure was not visibly affected, except for change in a minor structure. Most of the mucopeptide layer was solubilized by lysozyme, but a structureless bag-shaped residue was left. This residue contained phosphorus, carbohydrate, and limited amino acids, but it did not contain muramic acid, glucosamine, or ornithine. Aqueous phenol removed a lipoprotein component from strain R(1), which contained limited fatty acids. It also removed meso- and ll-diaminopimelic acid.

Bacterial Proteins↗