The genome of Azoarcus olearius DQS-4 , a N -fixing Betaproteobacterium isolated from oil-contaminated soil in Taiwan, was sequenced and compared with other Azoarcus strains. The genome sequence showed high synteny with Azoarcus sp. BH72, a model endophytic diazotroph, but low synteny with five non-plant-associated strains (Azoarcus CIB, Azoarcus EBN1, Azoarcus KH32C, A. toluclasticus MF63 and Azoarcus PA01). Average Nucleotide Identity (ANI) revealed that DQS-4 shares 98.98% identity with Azoarcus BH72, which should now be included in the species A. olearius. The genome of DQS-4 contained several genes related to plant colonization and plant growth promotion, such as nitrogen fixation, plant adhesion and root surface colonization. In accordance with the presence of these genes, DQS-4 colonized rice (Oryza sativa) and Setaria viridis, where it was observed within the intercellular spaces and aerenchyma mainly of the roots. Although they promote the growth of grasses, the mechanism(s) of plant growth promotion by A. olearius strains is unknown, as the genomes of DQS-4 and BH72 do not contain genes for indole acetic acid (IAA) synthesis nor phosphate solubilization. In spite of its original source, both the genome and behaviour of DQS-4 suggest that it has the capacity to be an endophytic, nitrogen-fixing plant growth-promoting bacterium.

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A slightly thermophilic bacterial strain, designated AT-A2 T , was isolated from a hot spring water sample taken from the Antun hot spring in Taiwan and characterized using a polyphasic taxonomic approach. Cells of strain AT-A2 T were aerobic, Gram-negative, motile by a single polar flagellum and formed non-pigmented colonies. Growth occurred at 35-60 6C (optimum, 55 6C), with 0-1.0 % NaCl (optimum, 0.2 %) and at pH 7.0-9.0 (optimum, pH 7.0). Phylogenetic analyses based on 16S rRNA gene sequences showed that strain AT-A2 T belonged to the genus Tepidimonas and its closest neighbour was Tepidimonas thermarum AA-1 T with a sequence similarity of 97.5 %. The predominant cellular fatty acids were C 16 : 0 (40.2 %), summed feature 3 (C 16 : 1 v7c and/or C 16 : 1 v6c; 20.1 %) and C 17 : 0 cyclo (11.5 %). The major respiratory quinone was Q-8. The polar lipid profile consisted of phosphatidylethanolamine, phosphatidylglycerol, diphosphatidylglycerol, an uncharacterized aminolipid and several uncharacterized phospholipids. The DNA G+C content of strain AT-A2 T was 70.1 mol%. The mean level of DNA-DNA relatedness between strain AT-A2 T and Tepidimonas thermarum AA-1 T was 23.9 %. On the basis of the phylogenetic and phenotypic data, strain AT-A2 T should be classified as representing a novel species, for which the name Tepidimonas fonticaldi sp. nov. is proposed. The type strain is

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In the serum of hepatitis B virus (HBV)-infected patients, two different types of particles, a 42 nm virion and a 22 nm subviral particle, were identified. The envelope of both particles is composed of three proteins, the large (L), middle (M), and major/small (S) surface proteins but the ratio between these components varies in each.The M protein appears in a lesser amount than the S protein in both virion and subviral particles, although it is translated from the same subgenomic RNA, and this is due to its poor initiation context of translation. In addition, only the glycosylated form of M protein is secreted in contrast to both glycosylated and unglycosylated forms of L and S proteins that are secreted. To investigate the biogenesis of M protein, human hepatoma cells transfected with plasmids containing a mutated HBV DNA were used to produce a high amount of M protein. Electron microscopic observation revealed that despite a higher proportion of the M protein being found in the transfected cells, the secreted surface antigen particles possess similar size and density to 22 nm subviral particles. Detailed biochemical analyses showed the following. (1) The unglycosylated M protein was predominantly present in the microsomal fraction but not present in any other subcellular fractions. (2) The M protein formed 22-nm-like particles in the endoplasmic reticulum (ER) and was retained in the post-ER or preGolgi regions. (3) In addition to the complex glycosylated form of M protein, a high-mannose form of M protein could be secreted. (4) Normally, no unglycosylated M protein was secreted. However, glycosylation was not essential for M protein secretion since M protein deprived of glycosylation by tunicamycin treatment was detected in the medium. These findings suggest that (i) the M protein was probably translated and co-translocated into the ER and at least one site was glycosylated before leaving the ER resulting in no secretion of unglycosylated M protein, and (ii) the M protein had two secretion pathways, one through the conventional pathway and the other probably directly through the ER.

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