Modular design of the Enterococcus hirae muramidase-2 and Streptococcus faecalis autolysin

Joris, Bernard; Englebert, S.; Chu, Chien-Peng; Kariyama, Reiko; Daneo-Moore, L; Shockman, Gérald D.; Ghuysen, Jean‐Marie

doi:10.1016/0378-1097(92)90707-u

Cited by 100 publications

(115 citation statements)

References 24 publications

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“…2C). The LysM motif was first identified in bacterial lysins and muramidases, enzymes that degrade cell wall peptidoglycans (12), and also found in the chitinases from various origins, including Caenorhabditis elegans (13), Volvox carteri (14), and Kluyveromyces lactis (15), but not from higher plants. A BAC clone in the rice genome database (GenBank accession no.…”

Section: Resultsmentioning

confidence: 99%

Plant cells recognize chitin fragments for defense signaling through a plasma membrane receptor

Kaku

Nishizawa

Ishii-Minami³

et al. 2006

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

1,015

798

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elicitor ͉ host-pathogen interaction ͉ N-acetylchitooligosaccharides ͉ pathogen-associated molecular patterns H igher plants have the ability to initiate various defense reactions such as hypersensitive responses, production of phytoalexins and antimicrobial proteins, and reinforcement of cell walls when they are infected by various pathogens (1, 2). They can distinguish self and non-self, or detect specific pathogens, through the perception of signal molecules (elicitors) mostly generated͞secreted from pathogens. Fragments of cell surface macromolecules typical of microorganisms such as cell wall polysaccharides, secreted proteins, as well as a flagella protein, often serve as a potent elicitor to induce defense reactions. They are classified as ''general elicitors'' that are commonly found in various microorganisms and induce defense responses in a wide range of plant species. Perception of general elicitors has been thought to play an important role in the basic resistance, or nonhost resistance, of plants to most potential pathogens. It has also been emerged in recent years that the defense systems mediated by the perception of these ''general elicitors'' have a considerable similarity with mammalian innate immunity, in the recognition of pathogen-associated molecular patterns as well as the molecules involved in the perception and transduction of these signal molecules (3).Chitin oligosaccharides (N-acetylchitooligosaccharides) are a representative general elicitor inducing defense responses in a wide range of plant cells including both monocots and dicots (4). Chitin oligosaccharides were reported to induce defense responses also in mammalian and insect cells (4, 5). Interestingly, specific modifications of chitin oligosaccharides by fatty acids, sulfate, or some sugars, generate ''Nod factors'' that induce nodulation in legume roots in the symbiotic interaction with rhizobial bacteria (6). Thus, the recognition of chitin oligosaccharides and related compounds seems to play a fundamental role in the establishment of basal resistance to potential pathogens in plants and in some cases the symbiotic relationships between leguminous plants and rhizobial bacteria.Concerning to the receptor for chitin oligosaccharide elicitor, we previously identified a high-affinity binding protein for this elicitor in the plasma membrane of rice cells by affinity labeling (7). Similar binding proteins were also detected in various plant cells that could respond to the elicitor (8,9). Correlation between the presence of the binding proteins and the elicitor responsiveness of these cells, correlation between the binding specificity and the preference of the structure of chitin oligosaccharides in defense responses, strongly indicated that the binding proteins function as a receptor, or a part of receptor complex, for chitin oligosaccharide elicitor. Here we report the purification of this chitin oligosaccharide elicitor-binding protein (hereafter designated as CEBiP), cloning of the corresponding cDNA and its functional characte...

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Section: Resultsmentioning

confidence: 99%

Plant cells recognize chitin fragments for defense signaling through a plasma membrane receptor

Kaku

Nishizawa

Ishii-Minami³

et al. 2006

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

1,015

798

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“…In addition to these structural proteins, several proteins are required for rod assembly (Kubori et al, 1992). Among such proteins, FlgJ of S. enterica (FlgJ Se ) possesses a sequence similar to 1,4-β-N-acetylmuramidase (Acm), a Gls that cleaves 1,4-β-linkages between the two amino sugars in glycan chains (Joris et al, 1992;Buist et al, 1995). On the basis of this sequence similarity, Dijkstra and Keck (1996) proposed that FlgJ acts as a PGase dedicated to flagellar rod formation.…”

Section: Edited By Hedeo Shinagawamentioning

confidence: 99%

Plasticity of the domain structure in FlgJ, a bacterial protein involved in flagellar rod formation

2006

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Bacterial flagellar rod structure is built across the peptidoglycan (PG) layer. A Salmonella enterica flagellar protein FlgJ is believed to consist of two functional domains, the N-terminal half acting as a scaffold or cap essential for rod assembly and the C-terminal half acting as a PG hydrolase (PGase) that makes a hole in the PG layer to facilitate rod penetration. In this study, molecular data analyses were conducted on FlgJ data sets sampled from a variety of bacterial species, and three types of FlgJ homologs were identified: (i) "canonical dual-domain" type found in β-and γ-proteobacteria that has a domain for one of the PGases, acetylmuramidase (Acm), at the C terminus, (ii) "non-canonical dual-domain" type found in the genus Desulfovibrio (δ-proteobacteria) that bears a domain for another PGase, M23/M37-family peptidase (Pep), at the C terminus and (iii) "singledomain" type found in phylogenetically diverged lineages that lacks the Acm or Pep domain. FlgJ phylogeny, together with the domain architecture, suggested that the single-domain type was the original form of FlgJ and the canonical dualdomain type had evolved from the single-domain type by fusion of the Acm domain to its C terminus in the common ancestor of β-and γ-proteobacteria. The noncanonical dual-domain type may have been formed by fusion of the Pep domain to the single-domain type in the ancestor of Desulfovibrio. In some lineages of γ-proteobacteria, the Acm domain appeared to be lost secondarily from the dual-domain type FlgJ to yield again a single-domain type one. To rationalize the underlying mechanism that gave rise to the two different types of dual-domain FlgJ homologs, we propose a model assuming the lineage-specific co-option of flagellum-specific PGase from diverged housekeeping PGases in bacteria.

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“…It is noteworthy that most of the variations observed between the pBClin15 predicted endolysin and those encoded by GIL01 and GIL16 are located at the C-terminal end. Since that domain has been shown to be implicated in cell wall binding (14,17), the observed differences may reflect the target specificity of these endolysins.…”

Section: Gil16 Is Morphologically Similar To Other Tectiviral Phagesmentioning

confidence: 99%

GIL16, a New Gram-Positive Tectiviral Phage Related to theBacillus thuringiensisGIL01 and theBacillus cereuspBClin15 Elements

2005

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One of the most notable characteristics of Tectiviridae resides in their double-layer coats: the doublestranded DNA is located within a flexible lipoprotein vesicle covered by a rigid protein capsid. Despite their apparent rarity, tectiviruses have an extremely wide distribution compared to other phage groups. Members of this family have been found to infect gram-negative (PRD1 and relatives) as well as gram-positive (Bam35, GIL01, AP50, and NS11) hosts. Several reports have shown that tectiviruses infecting gram-negative bacteria are closely related, whereas no information is currently available on the genetic relationship among those infecting gram-positive bacteria. The present study reports the sequence of GIL16, a new isolate originating from Bacillus thuringiensis, and a genetic comparison of this isolate with the tectiviral bacteriophages Bam35 and GIL01, which originated from B. thuringiensis serovars Alesti and Israelensis, respectively. In contrast to PRD1 and its relatives, these are temperate bacteriophages existing as autonomous linear prophages within the host cell. Mutations in a particular motif in both the GIL01 and GIL16 phages are also shown to correlate with a switch to the lytic cycle. Interestingly, both bacterial viruses displayed narrow, yet slightly different, host spectrums. We also explore the hypothesis that pBClin15, a linear plasmid hosted by the Bacillus cereus reference strain ATCC 14579, is also a prophage. Sequencing of its inverted repeats at both extremities and a comparison with GIL01 and GIL16 emphasize its relationship to the Tectiviridae.The bacteriophage GIL01 has a linear double-stranded DNA genome of 14,931 bp delineated by imperfect 73-bp inverted repeats and protected by proteins at its 5Ј ends. GIL01 is a temperate bacteriophage that was isolated from Bacillus thuringiensis serovar Israelensis whose prophage form, designated pGIL01, resides in the host cell as an autonomous linear plasmid without any apparent integration into the host chromosome. It has been suggested that GIL01 belongs to the family Tectiviridae (28), whose members are characterized by the presence of an internal lipid membrane. While tectiviruses infecting gram-negative bacteria have been extensively studied at the genetic level, those infecting gram-positive bacteria remain less well characterized. PRD1, for instance, is the family model and infects bacteria harboring conjugative plasmids of the P, N, or W incompatibility groups, such as Escherichia coli and Salmonella enterica. These plasmids encode the phage receptor but are not otherwise involved in the virus life cycle In addition to GIL01, three other tectiviruses that infect gram-positive bacteria have been identified so far. The bacteriophages AP50 and NS11, isolated from Bacillus anthracis (19) and Bacillus acidocaldarius (23, 24), respectively, have only been morphologically characterized. Bam35 was isolated from B. thuringiensis serovar Alesti in 1978 (1) and was recently sequenced (21), revealing that it differs from GIL01 by 11 bp. A p...

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Modular design of the Enterococcus hirae muramidase-2 and Streptococcus faecalis autolysin

Cited by 100 publications

References 24 publications

Plant cells recognize chitin fragments for defense signaling through a plasma membrane receptor

Plant cells recognize chitin fragments for defense signaling through a plasma membrane receptor

Plasticity of the domain structure in FlgJ, a bacterial protein involved in flagellar rod formation

GIL16, a New Gram-Positive Tectiviral Phage Related to theBacillus thuringiensisGIL01 and theBacillus cereuspBClin15 Elements

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