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Article ; Online: Erratum for Nahm et al., "A Common Food Glycan, Pectin, Shares an Antigen with Streptococcus pneumoniae Capsule".

Nahm, Moon H / Yu, Jigui / Vlach, Jiri / Bar-Peled, Maor

mSphere

2020 Volume 5, Issue 2

Language	English
Publishing date	2020-04-29
Publishing country	United States
Document type	Journal Article ; Published Erratum
ISSN	2379-5042
ISSN (online)	2379-5042
DOI	10.1128/mSphere.00363-20
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Article ; Online: A Common Food Glycan, Pectin, Shares an Antigen with Streptococcus pneumoniae Capsule.

Nahm, Moon H / Yu, Jigui / Vlach, Jiri / Bar-Peled, Maor

mSphere

2020 Volume 5, Issue 2

Abstract: We are exposed daily to many glycans from bacteria and food plants. Bacterial glycans are generally antigenic and elicit antibody responses. It is unclear if food glycans' sharing of antigens with bacterial glycans influences our immune responses to ... ...

Abstract	We are exposed daily to many glycans from bacteria and food plants. Bacterial glycans are generally antigenic and elicit antibody responses. It is unclear if food glycans' sharing of antigens with bacterial glycans influences our immune responses to bacteria. We studied 14 different plant foods for cross-reactivity with monoclonal antibodies (MAbs) against 24 pneumococcal serotypes which commonly cause infections and are included in pneumococcal vaccines. Serotype 15B-specific MAb cross-reacts with fruit peels, and serotype 10A MAb cross-reacts with many natural and processed plant foods. The serotype 10A cross-reactive epitope is terminal 1,6-linked β-galactose [βGal(1-6)], present in the rhamno-galacturonan I (RG-I) domain of pectin. Despite wide consumption of pectin, the immune response to 10A is comparable to the responses to other serotypes. An antipectin antibody can opsonize serotype 10A pneumococci, and the shared βGal(1-6) may be useful as a simple vaccine against 10A. Impact of food glycans should be considered in host-pathogen interactions and future vaccine designs.
MeSH term(s)	Antibodies, Monoclonal/immunology ; Antigens, Bacterial/immunology ; Bacterial Capsules/immunology ; Cross Reactions ; Epitopes/immunology ; Fruit ; Humans ; Pectins/immunology ; Phagocytosis ; Serogroup ; Streptococcus pneumoniae/immunology ; Vegetables
Chemical Substances	Antibodies, Monoclonal ; Antigens, Bacterial ; Epitopes ; Pectins (89NA02M4RX)
Language	English
Publishing date	2020-04-08
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
ISSN	2379-5042
ISSN (online)	2379-5042
DOI	10.1128/mSphere.00074-20
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Article ; Online: Identification of an apiosyltransferase in the plant pathogen Xanthomonas pisi.

Smith, James Amor / Bar-Peled, Maor

PloS one

2018 Volume 13, Issue 10, Page(s) e0206187

Abstract: The rare branched-chain sugar apiose, once thought to only be present in the plant kingdom, was found in two bacterial species: Geminicoccus roseus and Xanthomonas pisi. Glycans with apiose residues were detected in aqueous methanol-soluble fractions as ... ...

Abstract	The rare branched-chain sugar apiose, once thought to only be present in the plant kingdom, was found in two bacterial species: Geminicoccus roseus and Xanthomonas pisi. Glycans with apiose residues were detected in aqueous methanol-soluble fractions as well as in the insoluble pellet fraction of X. pisi. Genes encoding bacterial uridine diphosphate apiose (UDP-apiose) synthases (bUASs) were characterized in these bacterial species, but the enzyme(s) involved in the incorporation of the apiose into glycans remained unknown. In the X. pisi genome two genes flanking the XpUAS were annotated as hypothetical glycosyltransferase (GT) proteins. The first GT (here on named XpApiT) belongs to GT family 90 and has a Leloir type B fold and a putative lipopolysaccharide-modifying (LPS) domain. The second GT (here on XpXylT) belongs to GT family 2 and has a type A fold. The XpXylT and XpApiT genes were cloned and heterologously expressed in E. coli. Analysis of nucleotide sugar extracts from E. coli expressing XpXylT or XpApiT with UAS showed that recombinant XpApiT utilized UDP-apiose and XpXylT utilized UDP-xylose as substrate. Indirect activity assay (UDP-Glo) revealed that XpApiT is an apiosyltransferase (ApiT) able to specifically use UDP-apiose. Further support for the apiosyltransferase activity was demonstrated by in microbe co-expression of UAS and XpApiT in E. coli showing the utilization of UDP-apiose to generate an apioside detectable in the pellet fraction. This work provides evidence that X. pisi developed the ability to synthesize an apioside of indeterminate function; however, the evolution of the bacterial ApiT remains to be determined. From genetic and evolutionary perspectives, the apiose operon may provide a unique opportunity to examine how genomic changes reflect ecological adaptation during the divergence of a bacterial group.
MeSH term(s)	Bacterial Proteins/chemistry ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Cloning, Molecular ; Operon ; Pentoses/metabolism ; Pentosyltransferases/chemistry ; Pentosyltransferases/genetics ; Pentosyltransferases/metabolism ; Phylogeny ; Plants/microbiology ; Protein Domains ; Xanthomonas/enzymology ; Xanthomonas/genetics
Chemical Substances	Bacterial Proteins ; Pentoses ; apiose (E59T26TCEC) ; Pentosyltransferases (EC 2.4.2.-)
Language	English
Publishing date	2018-10-18
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, Non-P.H.S.
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0206187
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Article ; Online: Synthesis of UDP-apiose in Bacteria: The marine phototroph Geminicoccus roseus and the plant pathogen Xanthomonas pisi.

Smith, James Amor / Bar-Peled, Maor

PloS one

2017 Volume 12, Issue 9, Page(s) e0184953

Abstract: The branched-chain sugar apiose was widely assumed to be synthesized only by plant species. In plants, apiose-containing polysaccharides are found in vascularized plant cell walls as the pectic polymers rhamnogalacturonan II and apiogalacturonan. ... ...

Abstract	The branched-chain sugar apiose was widely assumed to be synthesized only by plant species. In plants, apiose-containing polysaccharides are found in vascularized plant cell walls as the pectic polymers rhamnogalacturonan II and apiogalacturonan. Apiosylated secondary metabolites are also common in many plant species including ancestral avascular bryophytes and green algae. Apiosyl-residues have not been documented in bacteria. In a screen for new bacterial glycan structures, we detected small amounts of apiose in methanolic extracts of the aerobic phototroph Geminicoccus roseus and the pathogenic soil-dwelling bacteria Xanthomonas pisi. Apiose was also present in the cell pellet of X. pisi. Examination of these bacterial genomes uncovered genes with relatively low protein homology to plant UDP-apiose/UDP-xylose synthase (UAS). Phylogenetic analysis revealed that these bacterial UAS-like homologs belong in a clade distinct to UAS and separated from other nucleotide sugar biosynthetic enzymes. Recombinant expression of three bacterial UAS-like proteins demonstrates that they actively convert UDP-glucuronic acid to UDP-apiose and UDP-xylose. Both UDP-apiose and UDP-xylose were detectable in cell cultures of G. roseus and X. pisi. We could not, however, definitively identify the apiosides made by these bacteria, but the detection of apiosides coupled with the in vivo transcription of bUAS and production of UDP-apiose clearly demonstrate that these microbes have evolved the ability to incorporate apiose into glycans during their lifecycles. While this is the first report to describe enzymes for the formation of activated apiose in bacteria, the advantage of synthesizing apiose-containing glycans in bacteria remains unknown. The characteristics of bUAS and its products are discussed.
MeSH term(s)	Alphaproteobacteria/growth & development ; Alphaproteobacteria/metabolism ; Carboxy-Lyases/metabolism ; Pisum sativum/microbiology ; Phylogeny ; Uridine Diphosphate Sugars/biosynthesis ; Xanthomonas/growth & development ; Xanthomonas/metabolism
Chemical Substances	UDP-apiose ; Uridine Diphosphate Sugars ; Carboxy-Lyases (EC 4.1.1.-) ; UDPglucuronate decarboxylase (EC 4.1.1.35)
Language	English
Publishing date	2017-09-20
Publishing country	United States
Document type	Journal Article
ZDB-ID	2267670-3
ISSN	1932-6203 ; 1932-6203
ISSN (online)	1932-6203
ISSN	1932-6203
DOI	10.1371/journal.pone.0184953
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Article ; Online: Discovery of a Unique Extracellular Polysaccharide in Members of the Pathogenic Bacillus That Can Co-form with Spores.

Li, Zi / Hwang, Soyoun / Bar-Peled, Maor

The Journal of biological chemistry

2016 Volume 291, Issue 36, Page(s) 19051–19067

Abstract: An exopolysaccharide, produced during the late stage of stationary growth phase, was discovered and purified from the culture medium of Bacillus cereus, Bacillus anthracis, and Bacillus thuringiensis when strains were grown in a defined nutrient medium ... ...

Abstract	An exopolysaccharide, produced during the late stage of stationary growth phase, was discovered and purified from the culture medium of Bacillus cereus, Bacillus anthracis, and Bacillus thuringiensis when strains were grown in a defined nutrient medium that induces biofilm. Two-dimensional NMR structural characterization of the polysaccharide, named pzX, revealed that it is composed of an unusual three amino-sugar sequence repeat of [-3)XylNAc4OAc(α1-3)GlcNAcA4OAc(α1-3)XylNAc(α1-]n The sugar residue XylNAc had never been described previously in any glycan structure. The XNAC operon that contains the genes for the assembly of pzX is also unique and so far has been identified only in members of the Bacillus cereus sensu lato group. Microscopic and biochemical analyses indicate that pzX co-forms during sporulation, so that upon the release of the spore to the extracellular milieu it becomes surrounded by pzX. The relative amounts of pzX produced can be manipulated by specific nutrients in the medium, but rich medium appears to suppress pzX formation. pzX has the following unique characteristics: a surfactant property that lowers surface tension, a cell/spore antiaggregant, and an adherence property that increases spores binding to surfaces. pzX in Bacillus could represent a trait shared by many spore-producing microorganisms. It suggests pzX is an active player in spore physiology and may provide new insights to the successful survival of the B. cereus species in natural environments or in the hosts.
MeSH term(s)	Bacillus anthracis/chemistry ; Bacillus anthracis/metabolism ; Bacillus cereus/chemistry ; Bacillus cereus/metabolism ; Bacillus thuringiensis/chemistry ; Bacillus thuringiensis/metabolism ; Polysaccharides, Bacterial/biosynthesis ; Spores, Bacterial/chemistry ; Spores, Bacterial/metabolism
Chemical Substances	Polysaccharides, Bacterial
Language	English
Publishing date	2016-07-11
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M116.724708
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Article ; Online: The Biosynthesis of UDP-D-QuiNAc in Bacillus cereus ATCC 14579.

Hwang, Soyoun / Aronov, Avi / Bar-Peled, Maor

PloS one

2015 Volume 10, Issue 7, Page(s) e0133790

Abstract: N-acetylquinovosamine (2-acetamido-2,6-di-deoxy-D-glucose, QuiNAc) is a relatively rare amino sugar residue found in glycans of few pathogenic gram-negative bacteria where it can play a role in infection. However, little is known about QuiNAc-related ... ...

Abstract	N-acetylquinovosamine (2-acetamido-2,6-di-deoxy-D-glucose, QuiNAc) is a relatively rare amino sugar residue found in glycans of few pathogenic gram-negative bacteria where it can play a role in infection. However, little is known about QuiNAc-related polysaccharides in gram-positive bacteria. In a routine screen for bacillus glycan grown at defined medium, it was surprising to identify a QuiNAc residue in polysaccharides isolated from this gram-positive bacterium. To gain insight into the biosynthesis of these glycans, we report the identification of an operon in Bacillus cereus ATCC 14579 that contains two genes encoding activities not previously described in gram-positive bacteria. One gene encodes a UDP-N-acetylglucosamine C4,6-dehydratase, (abbreviated Pdeg) that converts UDP-GlcNAc to UDP-4-keto-4,6-D-deoxy-GlcNAc (UDP-2-acetamido-2,6-dideoxy-α-D-xylo-4-hexulose); and the second encodes a UDP-4-reductase (abbr. Preq) that converts UDP-4-keto-4,6-D-deoxy-GlcNAc to UDP-N-acetyl-quinovosamine in the presence of NADPH. Biochemical studies established that the sequential Pdeg and Preq reaction product is UDP-D-QuiNAc as determined by mass spectrometry and one- and two-dimensional NMR experiments. Also, unambiguous evidence for the conversions of the dehydratase product, UDP-α-D-4-keto-4,6-deoxy-GlcNAc, to UDP-α-D-QuiNAc was obtained using real-time 1H-NMR spectroscopy and mass spectrometry. The two genes overlap by 4 nucleotides and similar operon organization and identical gene sequences were also identified in a few other Bacillus species suggesting they may have similar roles in the lifecycle of this class of bacteria important to human health. Our results provide new information about the ability of Bacilli to form UDP-QuiNAc and will provide insight to evaluate their role in the biology of Bacillus.
MeSH term(s)	Acetylglucosamine/analogs & derivatives ; Acetylglucosamine/biosynthesis ; Bacillus cereus/metabolism ; Bacterial Proteins/metabolism ; Oxidoreductases/metabolism ; Uridine Diphosphate N-Acetylglucosamine/metabolism
Chemical Substances	2-acetamido-2,6-dideoxy-glucose (N-acetyl-quinovosamine) ; Bacterial Proteins ; Uridine Diphosphate N-Acetylglucosamine (528-04-1) ; Oxidoreductases (EC 1.-) ; Acetylglucosamine (V956696549)
Language	English
Publishing date	2015
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, Non-P.H.S.
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0133790
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Book: A novel lectin controls wound-response in Arabidopsis

Fluhr, Robert / Bar-Peled, Maor

2011

Institution	United States-Israel Binational Agricultural Research and Development Fund
Author's details	principal investigator: Robert Fluhr ; co-principal investigator: Maor Bar-Peled
Keywords	Arabidopsis/Wounds and injuries. ; Plant lectins.
Language	English
Size	1 v. (various foliations) :, col. ill.
Publisher	BARD
Publishing place	Bet Dagan, Israel
Document type	Book
Note	Final report. ; Project no. IS-4141-08.
Database	NAL-Catalogue (AGRICOLA)

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Article: Genetic alteration of UDP‐rhamnose metabolism in Botrytis cinerea leads to the accumulation of UDP‐KDG that adversely affects development and pathogenicity

Ma, Liang / Salas, Omar / Bowler, Kyle / Oren‐Young, Liat / Bar‐Peled, Maor / Sharon, Amir

Molecular plant pathology. 2017 Feb., v. 18, no. 2

2017

Abstract: Botrytis cinerea is a model plant‐pathogenic fungus that causes grey mould and rot diseases in a wide range of agriculturally important crops. A previous study has identified two enzymes and corresponding genes (bcdh, bcer) that are involved in the ... ...

Abstract	Botrytis cinerea is a model plant‐pathogenic fungus that causes grey mould and rot diseases in a wide range of agriculturally important crops. A previous study has identified two enzymes and corresponding genes (bcdh, bcer) that are involved in the biochemical transformation of uridine diphosphate (UDP)‐glucose, the major fungal wall nucleotide sugar precursor, to UDP‐rhamnose. We report here that deletion of bcdh, the first biosynthetic gene in the metabolic pathway, or of bcer, the second gene in the pathway, abolishes the production of rhamnose‐containing glycans in these mutant strains. Deletion of bcdh or double deletion of both bcdh and bcer has no apparent effect on fungal development or pathogenicity. Interestingly, deletion of the bcer gene alone adversely affects fungal development, giving rise to altered hyphal growth and morphology, as well as reduced sporulation, sclerotia production and virulence. Treatments with wall stressors suggest the alteration of cell wall integrity. Analysis of nucleotide sugars reveals the accumulation of the UDP‐rhamnose pathway intermediate UDP‐4‐keto‐6‐deoxy‐glucose (UDP‐KDG) in hyphae of the Δbcer strain. UDP‐KDG could not be detected in hyphae of the wild‐type strain, indicating fast conversion to UDP‐rhamnose by the BcEr enzyme. The correlation between high UDP‐KDG and modified cell wall and developmental defects raises the possibility that high levels of UDP‐KDG result in deleterious effects on cell wall composition, and hence on virulence. This is the first report demonstrating that the accumulation of a minor nucleotide sugar intermediate has such a profound and adverse effect on a fungus. The ability to identify molecules that inhibit Er (also known as NRS/ER) enzymes or mimic UDP‐KDG may lead to the development of new antifungal drugs.
Keywords	Botrytis cinerea ; adverse effects ; antifungal agents ; biochemical pathways ; cell wall components ; cell walls ; crops ; enzymes ; genes ; gray mold ; hyphae ; metabolism ; models ; mutants ; plant pathogenic fungi ; polysaccharides ; sclerotia ; sporulation ; sugars ; uridine diphosphate ; virulence
Language	English
Dates of publication	2017-02
Size	p. 263-275.
Publishing place	John Wiley & Sons, Ltd
Document type	Article
Note	JOURNAL ARTICLE
ZDB-ID	2020755-4
ISSN	1364-3703 ; 1464-6722
ISSN (online)	1364-3703
ISSN	1464-6722
DOI	10.1111/mpp.12398
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Article ; Online: Identification of a novel UDP-sugar pyrophosphorylase with a broad substrate specificity in Trypanosoma cruzi.

Yang, Ting / Bar-Peled, Maor

The Biochemical journal

2010 Volume 429, Issue 3, Page(s) 533–543

Abstract: The diverse types of glycoconjugates synthesized by trypanosomatid parasites are unique compared with the host cells. These glycans are required for the parasite survival, invasion or evasion of the host immune system. Synthesis of those glycoconjugates ... ...

Abstract	The diverse types of glycoconjugates synthesized by trypanosomatid parasites are unique compared with the host cells. These glycans are required for the parasite survival, invasion or evasion of the host immune system. Synthesis of those glycoconjugates requires a constant supply of nucleotide-sugars (NDP-sugars), yet little is known about how these NDP-sugars are made and supplied. In the present paper, we report a functional gene from Trypanosoma cruzi that encodes a nucleotidyltransferase, which is capable of transforming different types of sugar 1-phosphates and NTP into NDP-sugars. In the forward reaction, the enzyme catalyses the formation of UDP-glucose, UDP-galactose, UDP-xylose and UDP-glucuronic acid, from their respective monosaccharide 1-phosphates in the presence of UTP. The enzyme could also convert glucose 1-phosphate and TTP into TDP-glucose, albeit at lower efficiency. The enzyme requires bivalent ions (Mg2+ or Mn2+) for its activity and is highly active between pH 6.5 and pH 8.0, and at 30-42 degrees C. The apparent Km values for the forward reaction were 177 microM (glucose 1-phosphate) and 28.4 microM (UTP) respectively. The identification of this unusual parasite enzyme with such broad substrate specificities suggests an alternative pathway that might play an essential role for nucleotide-sugar biosynthesis and for the regulation of the NDP-sugar pool in the parasite.
MeSH term(s)	Amino Acid Sequence ; Animals ; Arabidopsis Proteins/chemistry ; Arabidopsis Proteins/genetics ; Arabidopsis Proteins/metabolism ; Chromatography, High Pressure Liquid ; Cloning, Molecular ; DNA, Complementary ; Glucosephosphates/metabolism ; Kinetics ; Magnetic Resonance Spectroscopy ; Molecular Sequence Data ; Nucleotidyltransferases/chemistry ; Nucleotidyltransferases/genetics ; Nucleotidyltransferases/metabolism ; Sequence Homology, Amino Acid ; Substrate Specificity ; Trypanosoma cruzi/enzymology
Chemical Substances	Arabidopsis Proteins ; DNA, Complementary ; Glucosephosphates ; glucose-1-phosphate (CIX3U01VAU) ; Nucleotidyltransferases (EC 2.7.7.-) ; UDP-sugar pyrophosphorylase, Arabidopsis (EC 2.7.7.-)
Language	English
Publishing date	2010-08-01
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	2969-5
ISSN	1470-8728 ; 0006-2936 ; 0306-3275 ; 0264-6021
ISSN (online)	1470-8728
ISSN	0006-2936 ; 0306-3275 ; 0264-6021
DOI	10.1042/BJ20100238
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Article ; Online: UDP-4-Keto-6-Deoxyglucose, a Transient Antifungal Metabolite, Weakens the Fungal Cell Wall Partly by Inhibition of UDP-Galactopyranose Mutase.

Ma, Liang / Salas, Omar / Bowler, Kyle / Bar-Peled, Maor / Sharon, Amir

mBio

2017 Volume 8, Issue 6

Abstract: Can accumulation of a normally transient metabolite affect fungal biology? UDP-4-keto-6-deoxyglucose (UDP-KDG) represents an intermediate stage in conversion of UDP-glucose to UDP-rhamnose. Normally, UDP-KDG is not detected in living cells, because it is ...

Abstract	Can accumulation of a normally transient metabolite affect fungal biology? UDP-4-keto-6-deoxyglucose (UDP-KDG) represents an intermediate stage in conversion of UDP-glucose to UDP-rhamnose. Normally, UDP-KDG is not detected in living cells, because it is quickly converted to UDP-rhamnose by the enzyme UDP-4-keto-6-deoxyglucose-3,5-epimerase/-4-reductase (ER). We previously found that deletion of the
MeSH term(s)	Antifungal Agents/metabolism ; Botrytis/metabolism ; Cell Wall/metabolism ; Crystallography, X-Ray ; Glucose/analogs & derivatives ; Glucose/metabolism ; Intramolecular Transferases/antagonists & inhibitors ; Kinetics ; Metabolic Networks and Pathways ; Phaseolus/microbiology ; Plant Leaves/microbiology ; Uridine Diphosphate/analogs & derivatives ; Uridine Diphosphate/metabolism ; Uridine Diphosphate Sugars/metabolism
Chemical Substances	Antifungal Agents ; UDP-4-keto-6-deoxyglucose ; Uridine Diphosphate Sugars ; UDP-rhamnose (1955-26-6) ; Uridine Diphosphate (58-98-0) ; Intramolecular Transferases (EC 5.4.-) ; UDP-galactopyranose mutase (EC 5.4.99.9) ; Glucose (IY9XDZ35W2)
Language	English
Publishing date	2017-11-21
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2557172-2
ISSN	2150-7511 ; 2161-2129
ISSN (online)	2150-7511
ISSN	2161-2129
DOI	10.1128/mBio.01559-17
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