Genetic and Structural Characterization of the Core Region of the Lipopolysaccharide from
            <i>Serratia marcescens</i>
            N28b (Serovar O4)

Coderch, Núria; Piqué, Núria; Lindner, Buko; Abitiu, Nihal; Merino, Susana; Izquierdo, Luís; Jiménez, Natàlia; Tomás, Juan M.; Holst, Otto; Regué, Miguel

doi:10.1128/jb.186.4.978-988.2004

Cited by 23 publications

(26 citation statements)

References 47 publications

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“…Thus, it is predicted that these strains contain wabG, wabH, and wabN homologues. This has been shown for S. marcescens N28b where these gene homologues are able to complement the corresponding K. pneumoniae mutants as shown in this and previous work (7,11,17). Interestingly these three genes are also found as predicted in P. mirabilis HI4320 (pedant.gsf.de/cgi-bin/wwwfly.pl?SetϭProteus_mirabilis& Pageϭindex).…”

Section: Discussionsupporting

confidence: 80%

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The Incorporation of Glucosamine into Enterobacterial Core Lipopolysaccharide

Regué

Izquierdo

Fresno

et al. 2005

Journal of Biological Chemistry

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The core lipopolysaccharide (LPS) of Klebsiella pneumoniae is characterized by the presence of disaccharide ␣GlcN-(1,4)-␣GalA attached by an ␣1,3 linkage to L-glycero-D-manno-heptopyranose II (LD-HeppII). Previously it has been shown that the WabH enzyme catalyzes the incorporation of GlcNAc from UDP-GlcNAc to outer core LPS. The presence of GlcNAc instead of GlcN and the lack of UDP-GlcN in bacteria indicate that an additional enzymatic step is required. In this work we identified a new gene (wabN) in the K. pneumoniae core LPS biosynthetic cluster. Chemical and structural analysis of K. pneumoniae non-polar wabN mutants showed truncated core LPS with GlcNAc instead of GlcN. In vitro assays using LPS truncated at the level of D-galacturonic acid (GalA) and cell-free extract containing WabH and WabN together led to the incorporation of GlcN, whereas none of them alone were able to do it. This result suggests that the later enzyme (WabN) catalyzes the deacetylation of the core LPS containing the GlcNAc residue. Thus, the incorporation of the GlcN residue to core LPS in K. pneumoniae requires two distinct enzymatic steps. WabN homologues are found in Serratia marcescens and some Proteus strains that show the same disaccharide ␣GlcN-(1,4)-␣GalA attached by an ␣1,3 linkage to LD-HeppII.

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Section: Discussionsupporting

confidence: 80%

“…The K. pneumoniae outer core disaccharide ␣GlcN-(1,4)-␣GalA linked by an ␣1,3 bond to LD-HeppII is also found in S. marcescens (17); P. mirabilis serovars O3/S1959, R110/1959, and OXK; Proteus vulgaris O25; and Proteus penneri strains 37 and 34 (for a review, see Ref. 30).…”

Section: Discussionmentioning

confidence: 99%

The Incorporation of Glucosamine into Enterobacterial Core Lipopolysaccharide

Regué

Izquierdo

Fresno

et al. 2005

Journal of Biological Chemistry

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“…11). This common fragment is also found in the core LPS of Klebsiella pneumoniae and Serratia marcescens (12)(13)(14), and we have shown that two enzymes are required for the incorporation of GlcN into the core LPS of K. pneumoniae: the WabH enzyme catalyzing the incorporation of GlcNAc from UDP-GlcNAc to outer core LPS and WabN catalyzing the deacetylation of the incorporated GlcNAc (15). The rest of the Proteus core OS is quite variable, with up to 37 different structures recognized in the genus Proteus and 11 in P. mirabilis (11).…”

mentioning

confidence: 86%

“…P. mirabilis core OS structures and genetic organization of the core OS biosynthetic clusters. A, the common part of core OS shared by all of the studied strains of P. mirabilis (11), K. pneumoniae, and S. marcescens (11,13,14). Broken lines denote the truncation level for the different core biosynthetic gene mutations (13,14,15,16,35).…”

Section: P Mirabilis Wa Genementioning

confidence: 99%

Three Enzymatic Steps Required for the Galactosamine Incorporation into Core Lipopolysaccharide

Aquilini

Azevedo

Merino

et al. 2010

Journal of Biological Chemistry

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The core lipopolysaccharides (LPS) of Proteus mirabilis as well as those of Klebsiella pneumoniae and Serratia marcescens are characterized by the presence of a hexosamine-galacturonic acid disaccharide (␣HexN-(1,4)-␣GalA) attached by an ␣1,3 linkage to L-glycero-D-manno-heptopyranose II (L-glycero-␣-D-manno-heptosepyranose II). In K. pneumoniae, S. marcescens, and some P. mirabilis strains, HexN is D-glucosamine, whereas in other P. mirabilis strains, it corresponds to D-galactosamine. Previously, we have shown that two enzymes are required for the incorporation of D-glucosamine into the core LPS of K. pneumoniae; the WabH enzyme catalyzes the incorporation of GlcNAc from UDP-GlcNAc to outer core LPS, and WabN catalyzes the deacetylation of the incorporated GlcNAc. Here we report the presence of two different HexNAc transferases depending on the nature of the HexN in P. mirabilis core LPS. In vivo and in vitro assays using LPS truncated at the level of galacturonic acid as acceptor show that these two enzymes differ in their specificity for the transfer of GlcNAc or GalNAc. By contrast, only one WabN homologue was found in the studied P. mirabilis strains. Similar assays suggest that the P. mirabilis WabN homologue is able to deacetylate both GlcNAc and GalNAc. We conclude that incorporation of D-galactosamine requires three enzymes: Gne epimerase for the generation of UDP-GalNAc from UDP-GlcNAc, N-acetylgalactosaminyltransferase (WabP), and LPS:HexNAc deacetylase.

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“…The resulting molecule serves as an acceptor for the transfer of the first heptose residue to position 5 of the first Kdo residue, which is accomplished by the heptosyltransferase I WaaC (14,31). Heptosyltransferase I genes in Salmonella enterica, Escherichia coli, Klebsiella pneumoniae (29), and Serratia marcescens (8,9,31), as well as genes in Pseudomonas aeruginosa (11), Neisseria spp. (32,39), Campylobacter spp.…”

mentioning

confidence: 99%

OpsX from Haemophilus influenzae Represents a Novel Type of Heptosyltransferase I in Lipopolysaccharide Biosynthesis

Gronow¹,

Brabetz²,

Lindner

et al. 2005

J Bacteriol

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The inner core region of the lipopolysaccharide (LPS) of Haemophilus influenzae is characterized by the presence of a phosphorylated 3-deoxy-␣-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.

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Genetic and Structural Characterization of the Core Region of the Lipopolysaccharide from Serratia marcescens N28b (Serovar O4)

Cited by 23 publications

References 47 publications

The Incorporation of Glucosamine into Enterobacterial Core Lipopolysaccharide

The Incorporation of Glucosamine into Enterobacterial Core Lipopolysaccharide

Three Enzymatic Steps Required for the Galactosamine Incorporation into Core Lipopolysaccharide

OpsX from Haemophilus influenzae Represents a Novel Type of Heptosyltransferase I in Lipopolysaccharide Biosynthesis

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