Lipopolysaccharides and K-Antigens: Their Structures, Biosynthesis, and Functions

Kannenberg, Elmar L.; Reuhs, Bradley L.; Forsberg, Lennart S.; Carlson, Russell W.

doi:10.1007/978-94-011-5060-6_7

Cited by 93 publications

(174 citation statements)

References 185 publications

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“…LPS 1 constitutes an integral part of the outer cell membrane of Gram-negative bacteria. It is therefore intimately involved in the formation of the plant-bacterial interface during symbiosis (3).…”

mentioning

confidence: 99%

Sinorhizobium meliloti acpXL Mutant Lacks the C28 Hydroxylated Fatty Acid Moiety of Lipid A and Does Not Express a Slow Migrating Form of Lipopolysaccharide

Sharypova

Niehaus

Scheidle

et al. 2003

Journal of Biological Chemistry

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Lipid A is the hydrophobic anchor of lipopolysaccharide (LPS) in the outer membrane of Gram-negative bacteria. Lipid A of all Rhizobiaceae is acylated with a long fatty acid chain, 27-hydroxyoctacosanoic acid. Biosynthesis of this long acyl substitution requires a special acyl carrier protein, AcpXL, which serves as a donor of C28 (-1)-hydroxylated fatty acid for acylation of rhizobial lipid A (Brozek, K.A., Carlson, R.W., and Raetz, C. R. (1996) J. Biol. Chem. 271, 32126 -32136). To determine the biological function of the C28 acylation of lipid A, we constructed an acpXL mutant of Sinorhizobium meliloti strain 1021. Gas-liquid chromatography and mass spectrometry analysis of the fatty acid composition showed that the acpXL mutation indeed blocked C28 acylation of lipid A. SDS-PAGE analysis of acpXL mutant LPS revealed only a fast migrating band, rough LPS, whereas the parental strain 1021 manifested both rough and smooth LPS. Regardless of this, the LPS of parental and mutant strains had a similar sugar composition and exposed the same antigenic epitopes, implying that different electrophoretic profiles might account for different aggregation properties of LPS molecules with and without a long acyl chain. The acpXL mutant of strain 1021 displayed sensitivity to deoxycholate, delayed nodulation of Medicago sativa, and a reduced competitive ability. However, nodules elicited by this mutant on roots of M. sativa and Medicago truncatula had a normal morphology and fixed nitrogen. Thus, the C28 fatty acid moiety of lipid A is not crucial, but it is beneficial for establishing an effective symbiosis with host plants. acpXL lies upstream from a cluster of five genes, including msbB (lpxXL), which might be also involved in biosynthesis and transfer of the C28 fatty acid to the lipid A precursor.

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confidence: 99%

Sinorhizobium meliloti acpXL Mutant Lacks the C28 Hydroxylated Fatty Acid Moiety of Lipid A and Does Not Express a Slow Migrating Form of Lipopolysaccharide

Sharypova

Niehaus

Scheidle

et al. 2003

Journal of Biological Chemistry

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“…Although effects of purified LPSs on root hairs and the efficiency of wild-type nodulation have been reported (32), our data demonstrate a functional extracellular complementation of an LPS mutant. A signaling function in nodule development has been proposed for LPS, mainly as a suppressor of plant defense (6,32). Striking similarities exist between the ORS571-oac2 nodules and the indeterminate nodule phenotypes induced by LPS Ϫ mutants of S. meliloti (33,34) and Rhizobium leguminosarum bv.…”

Section: Discussionmentioning

confidence: 99%

“…As in other interactions between bacteria and plants or animals (4), bacterial surface polysaccharides (SPSs), especially exopolysaccharides (EPSs) and lipopolysaccharides (LPSs), are believed to play an important role in symbiosis either as structural components or as signaling molecules (1,(5)(6)(7)(8)(9).…”

mentioning

confidence: 99%

Lipopolysaccharides as a communication signal for progression of legume endosymbiosis

Mathis

Gijsegem

Rycke

et al. 2005

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

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“…K antigens of Sinorhizobium meliloti are analogous to the group II K antigens of Escherichia coli. They adhere tightly to the cell surface of the rhizobia and usually contain a high proportion of Kdo (3-deoxy-D-manno-2-octulosonic acid; Petrovics et al 1993;Reuhs et al 1993;Kannenberg et al 1998).…”

Section: Introductionmentioning

confidence: 99%

Sinorhizobium meliloti-induced chitinase gene expression in Medicago truncatula ecotype R108-1: a comparison between symbiosis-specific class�V and defence-related class�IV chitinases

Salzer

Feddermann

Wiemken

et al. 2004

Planta

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The Medicago truncatula (Gaertn.) ecotypes Jemalong A17 and R108-1 differ in Sinorhizobium meliloti-induced chitinase gene expression. The pathogen-inducible class IV chitinase gene, Mtchit 4, was strongly induced during nodule formation of the ecotype Jemalong A17 with the S. meliloti wild-type strain 1021. In the ecotype R108-1, the S. meliloti wild types Sm1021 and Sm41 did not induce Mtchit 4 expression. On the other hand, expression of the putative class V chitinase gene, Mtchit 5, was found in roots of M. truncatula cv. R108-1 nodulated with either of the rhizobial strains. Mtchit 5 expression was specific for interactions with rhizobia. It was not induced in response to fungal pathogen attack, and not induced in roots colonized with arbuscular mycorrhizal (AM) fungi. Elevated Mtchit 5 gene expression was first detectable in roots forming nodule primordia. In contrast to Mtchit 4, expression of Mtchit 5 was stimulated by purified Nod factors. Conversely, Mtchit 4 expression was strongly elevated in nodules formed with the K-antigen-deficient mutant PP699. Expression levels of Mtchit 5 were similarly increased in nodules formed with PP699 and its parental wild-type strain Sm41. Phylogenetic analysis of the deduced amino acid sequences of Mtchit 5 (calculated molecular weight = 41,810 Da, isoelectric point pH 7.7) and Mtchit 4 (calculated molecular weight 30,527 Da, isoelectric point pH 4.9) revealed that the putative Mtchit 5 chitinase forms a separate clade within class V chitinases of plants, whereas the Mtchit 4 chitinase clusters with pathogen-induced class IV chitinases from other plants. These findings demonstrate that: (i) Rhizobium-induced chitinase gene expression in M. truncatula occurs in a plant ecotype-specific manner, (ii) Mtchit 5 is a putative chitinase gene that is specifically induced by rhizobia, and (iii) rhizobia-specific and defence-related chitinase genes are differentially influenced by rhizobial Nod factors and K antigens.Keywords Class IV and V chitinase AE K antigen AE Medicago truncatula ecotypes R108-1 and Jemalong A17 AE Nod factors AE Sinorhizobium AE Suppression of plant defence

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Lipopolysaccharides and K-Antigens: Their Structures, Biosynthesis, and Functions

Cited by 93 publications

References 185 publications

Sinorhizobium meliloti acpXL Mutant Lacks the C28 Hydroxylated Fatty Acid Moiety of Lipid A and Does Not Express a Slow Migrating Form of Lipopolysaccharide

Sinorhizobium meliloti acpXL Mutant Lacks the C28 Hydroxylated Fatty Acid Moiety of Lipid A and Does Not Express a Slow Migrating Form of Lipopolysaccharide

Lipopolysaccharides as a communication signal for progression of legume endosymbiosis

Sinorhizobium meliloti-induced chitinase gene expression in Medicago truncatula ecotype R108-1: a comparison between symbiosis-specific class�V and defence-related class�IV chitinases

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