BackgroundXanthomonas oryzae pv. oryzae causes bacterial blight of rice (Oryza sativa L.), a major disease that constrains production of this staple crop in many parts of the world. We report here on the complete genome sequence of strain PXO99A and its comparison to two previously sequenced strains, KACC10331 and MAFF311018, which are highly similar to one another.ResultsThe PXO99A genome is a single circular chromosome of 5,240,075 bp, considerably longer than the genomes of the other strains (4,941,439 bp and 4,940,217 bp, respectively), and it contains 5083 protein-coding genes, including 87 not found in KACC10331 or MAFF311018. PXO99A contains a greater number of virulence-associated transcription activator-like effector genes and has at least ten major chromosomal rearrangements relative to KACC10331 and MAFF311018. PXO99A contains numerous copies of diverse insertion sequence elements, members of which are associated with 7 out of 10 of the major rearrangements. A rapidly-evolving CRISPR (clustered regularly interspersed short palindromic repeats) region contains evidence of dozens of phage infections unique to the PXO99A lineage. PXO99A also contains a unique, near-perfect tandem repeat of 212 kilobases close to the replication terminus.ConclusionOur results provide striking evidence of genome plasticity and rapid evolution within Xanthomonas oryzae pv. oryzae. The comparisons point to sources of genomic variation and candidates for strain-specific adaptations of this pathogen that help to explain the extraordinary diversity of Xanthomonas oryzae pv. oryzae genotypes and races that have been isolated from around the world.

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We have studied the electronic structure of the diluted magnetic semiconductor Ga 1−x Mn x N ͑x = 0.0, 0.02, and 0.042͒ grown on Sn-doped n-type GaN using photoemission and soft x-ray absorption spectroscopy. Mn L-edge x-ray absorption have indicated that the Mn ions are in the tetrahedral crystal field and that their valence is divalent. Upon Mn doping into GaN, new states were found to form within the band gap of GaN, and the Fermi level was shifted downward. Satellite structures in the Mn 2p core level and the Mn 3d partial density of states were analyzed using configuration-interaction calculation on a MnN 4 cluster model. The deduced electronic structure parameters reveal that the p-d exchange coupling in Ga 1−x Mn x N is stronger than that in Ga 1−x Mn x As.

SlyA, a MarR family transcriptional regulator, controls an assortment of biological functions in several animal-pathogenic bacteria. In order to elucidate the functions of SlyA in the phytopathogen Dickeya dadantii (formerly Erwinia chrysanthemi) 3937, a slyA gene deletion mutant (denoted ⌬slyA) was constructed. The mutant exhibited increased sensitivity to sodium hypochlorite, the cationic antimicrobial peptide polymyxin B, and oxidative stress. The mutant showed reduced production of pectate lyase and exopolysaccharide and an inability to form a pellicle. The mutant lacking a functional slyA gene showed a significantly reduced ability to cause maceration of potato tubers. Accordingly, the mutant exhibited significantly reduced bacterial growth and failed to hyperinduce pectate lyase production in planta. Introduction of a plasmid containing slyA into the ⌬slyA mutant caused all of these phenotypes to recover to wild-type levels. These results suggest that SlyA plays an important role in virulence to plants by positively regulating the expression of multiple pathogenicityrelated traits of D. dadantii 3937.

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The cellular localization of Babesia bovis rhoptry-associated protein 1 (RAP-1) and its erythrocyte-binding affinity were examined with anti-RAP-1 antibodies. In an indirect immunofluorescent antibody test, RAP-1 was detectable in all developmental stages of merozoites and in extracellular merozoites. In the early stage of merozoite development, RAP-1 appears as a dense accumulation, which later thins out and blankets the host cell cytoplasm, but retains a denser mass around newly formed parasite nuclei. The preferential accumulations of RAP-1 on the inner surface of a host cell membrane and bordering the parasite's outer surface were demonstrable by immunoelectron microscopy. An erythrocyte-binding assay with the lysate of merozoites demonstrated RAP-1 binding to both bovine and equine erythrocytes. Anti-RAP-1 monoclonal antibody 1C1 prevented the interaction of RAP-1 with bovine erythrocytes and significantly inhibited parasite proliferation in vitro. With the recombinant RAP-1, the addition of increasing concentrations of Ca 2؉ accentuated its binding affinity with bovine erythrocytes. The present findings lend support to an earlier proposition of an erythrocytic binding role for RAP-1 expressed in B. bovis merozoites and, possibly, its involvement in the escape of newly formed merozoites from host cells.Babesia bovis is a hemoprotozoan parasite that causes great economic losses to the cattle industry worldwide. It is transmitted by tick vectors and has an asexual intraerythrocytic cycle in the infected cattle (5, 9). Understanding the basic molecular mechanism(s) of the asexual intraerythrocytic cycle, particularly the process of merozoite invasion into and escape from infected erythrocytes (RBC), may accelerate the development of an effective vaccine. Extracellular merozoites are directly exposed to the host humoral immune components. Consequently, efforts to identify potential components for the development of a vaccine are primarily directed at the merozoite stage.Apicomplexans utilize several rhoptry proteins in their invasion into and development within the host cell (16, 18). Extracellular merozoites attach to the host RBC and reorient to bring the apical organelles close to the attachment interface, and through the interaction of protozoan ligands with several surface receptors, the rhoptry products are released at the point of membrane invagination. Although the morphological events during host cell recognition and penetration appear to be similar among the apicomplexans, some molecular events mediated by each secretory component of the rhoptry vary and are unique (16,18).The rhoptry-associated protein 1 (RAP-1) of B. bovis merozoites bears substantial sequence homology to the RAP-1 of other Babesia parasites (3, 4) and contains immunogenic B-cell epitopes (20), and the purified recombinant RAP-1 has proven effective in inducing protective immunity in the vaccinated cattle (22). All of these earlier findings point to the biological and immunological characteristics of RAP-1 that would justify its inc...

HrpG, a two-component response regulatorlike protein, is a key regulator of the type III secretion system (T3SS) in Xanthomonas spp. In X. campestris pv. vesicatoria, HrpG with a single amino acid substitution (HrpG*) gains the ability to induce the expression of T3SS-related genes even under nutrient-rich conditions. In this study, we investigated the role of HrpG in the synthesis of the secretory protein using HrpG* in strain NA-1 of X. axonopodis pv. citri (Xac NA-1), a causal agent of citrus canker. Eleven proteins secreted via a type II secretion system (T2SS) were induced by HrpG*. In proteomic analyses, six of the 11 proteins were identified as extracellular enzymes, and the others as a fimbrial biogenesisrelated protein, a type IV-related protein, two hypothetical proteins, and a conserved hypothetical protein. Further analysis of these proteins revealed that the genes coding all 11 proteins were upregulated by HrpG*, even though they had different expression patterns for HrpXct-dependency. The data indicated that HrpG, a key regulator of T3SS, also acts as a positive regulator of certain proteins secreted via a T2SS in Xac NA-1.