scholarly journals Complete Genome Sequence of Anaplasma marginale subsp. centrale

2009 ◽  
Vol 192 (1) ◽  
pp. 379-380 ◽  
Author(s):  
David R. Herndon ◽  
Guy H. Palmer ◽  
Varda Shkap ◽  
Donald P. Knowles ◽  
Kelly A. Brayton

ABSTRACT Anaplasma marginale subsp. centrale is a naturally attenuated subtype that has been used as a vaccine for a century. We sequenced the genome of this organism and compared it to those of virulent senso stricto A. marginale strains. The comparison markedly narrows the number of outer membrane protein candidates for development of a safer inactivated vaccine and provides insight into the diversity among strains of senso lato A. marginale.

BMC Genomics ◽  
2021 ◽  
Vol 22 (1) ◽  
Author(s):  
So-Ra Han ◽  
Byeollee Kim ◽  
Jong Hwa Jang ◽  
Hyun Park ◽  
Tae-Jin Oh

Abstract Background The Arthrobacter group is a known set of bacteria from cold regions, the species of which are highly likely to play diverse roles at low temperatures. However, their survival mechanisms in cold regions such as Antarctica are not yet fully understood. In this study, we compared the genomes of 16 strains within the Arthrobacter group, including strain PAMC25564, to identify genomic features that help it to survive in the cold environment. Results Using 16 S rRNA sequence analysis, we found and identified a species of Arthrobacter isolated from cryoconite. We designated it as strain PAMC25564 and elucidated its complete genome sequence. The genome of PAMC25564 is composed of a circular chromosome of 4,170,970 bp with a GC content of 66.74 % and is predicted to include 3,829 genes of which 3,613 are protein coding, 147 are pseudogenes, 15 are rRNA coding, and 51 are tRNA coding. In addition, we provide insight into the redundancy of the genes using comparative genomics and suggest that PAMC25564 has glycogen and trehalose metabolism pathways (biosynthesis and degradation) associated with carbohydrate active enzyme (CAZymes). We also explain how the PAMC26654 produces energy in an extreme environment, wherein it utilizes polysaccharide or carbohydrate degradation as a source of energy. The genetic pattern analysis of CAZymes in cold-adapted bacteria can help to determine how they adapt and survive in such environments. Conclusions We have characterized the complete Arthrobacter sp. PAMC25564 genome and used comparative analysis to provide insight into the redundancy of its CAZymes for potential cold adaptation. This provides a foundation to understanding how the Arthrobacter strain produces energy in an extreme environment, which is by way of CAZymes, consistent with reports on the use of these specialized enzymes in cold environments. Knowledge of glycogen metabolism and cold adaptation mechanisms in Arthrobacter species may promote in-depth research and subsequent application in low-temperature biotechnology.


2012 ◽  
Vol 86 (18) ◽  
pp. 10234-10235 ◽  
Author(s):  
Gaël Panis ◽  
Christophe Lambert ◽  
Patrick H. Viollier

φCbK is a B3 morphotype bacteriophage of theSiphoviridaefamily that infectsCaulobacter crescentus, the preeminent model system for bacterial cell cycle studies. The last 4 decades of research with φCbK as a genetic and cytological tool to study the biology of the host warrant an investigation of the phage genome composition. Herein, we report the complete genome sequence of φCbK and highlight unusual features that emerged from its annotation. The complete genome analysis of the φCbK phage provides new insight into its characteristics and potential interactions with itsCaulobacter crescentushost, setting the stage for future functional studies with φCbK.


2016 ◽  
Vol 4 (5) ◽  
Author(s):  
Yang Wang ◽  
Kaiyong He ◽  
Yongzhong Jiang ◽  
Jiate Shen ◽  
Bo Yu

Pontibacter akesuensis strain AKS 1 T was found in Akesu, Xinjiang Province, China, and exhibits the extraordinary ability to metabolize various substrates and is resistant to solar radiation. To gain insight into the bacterial genetic determinants for this adaptability, we report the complete genome sequence of strain AKS 1 T .


2017 ◽  
Vol 5 (23) ◽  
Author(s):  
Filip Zekic ◽  
Brian Weselowski ◽  
Ze-Chun Yuan

ABSTRACT Here, we report the complete genome sequence of the phosphate-solubilizing bacterium Burkholderia cenocepacia CR318, consisting of three circular chromosomes of 3,511,146 bp, 3,097,552 bp, and 1,056,069 bp. The data presented will facilitate further insight into the mechanisms of phosphate solubilization and its application for agricultural and ecological sustainability.


Vaccine ◽  
2017 ◽  
Vol 35 (1) ◽  
pp. 77-83 ◽  
Author(s):  
Liang Zhao ◽  
Antonino S. Cavallaro ◽  
David Wibowo ◽  
Bing Zhang ◽  
Jun Zhang ◽  
...  

2016 ◽  
Vol 85 (3) ◽  
Author(s):  
Kathryn S. Hebert ◽  
David Seidman ◽  
Aminat T. Oki ◽  
Jerilyn Izac ◽  
Sarvani Emani ◽  
...  

ABSTRACT Anaplasma marginale causes bovine anaplasmosis, a debilitating and potentially fatal tick-borne infection of cattle. Because A. marginale is an obligate intracellular organism, its adhesins that mediate entry into host cells are essential for survival. Here, we demonstrate that A. marginale outer membrane protein A (AmOmpA; AM854) contributes to the invasion of mammalian and tick host cells. AmOmpA exhibits predicted structural homology to OmpA of A. phagocytophilum (ApOmpA), an adhesin that uses key lysine and glycine residues to interact with α2,3-sialylated and α1,3-fucosylated glycan receptors, including 6-sulfo-sialyl Lewis x (6-sulfo-sLex). Antisera against AmOmpA or its predicted binding domain inhibits A. marginale infection of host cells. Residues G55 and K58 are contributory, and K59 is essential for recombinant AmOmpA to bind to host cells. Enzymatic removal of α2,3-sialic acid and α1,3-fucose residues from host cell surfaces makes them less supportive of AmOmpA binding. AmOmpA is both an adhesin and an invasin, as coating inert beads with it confers adhesiveness and invasiveness. Recombinant forms of AmOmpA and ApOmpA competitively antagonize A. marginale infection of host cells, but a monoclonal antibody against 6-sulfo-sLex fails to inhibit AmOmpA adhesion and A. marginale infection. Thus, the two OmpA proteins bind related but structurally distinct receptors. This study provides a detailed understanding of AmOmpA function, identifies its essential residues that can be targeted by blocking antibody to reduce infection, and determines that it binds to one or more α2,3-sialylated and α1,3-fucosylated glycan receptors that are unique from those targeted by ApOmpA.


2016 ◽  
Vol 84 (10) ◽  
pp. 2740-2747 ◽  
Author(s):  
Telmo Graça ◽  
Marta G. Silva ◽  
Alla S. Kostyukova ◽  
Guy H. Palmer

Sequential expression of outer membrane protein antigenic variants is an evolutionarily convergent mechanism used by bacterial pathogens to escape host immune clearance and establish persistent infection. Variants must be sufficiently structurally distinct to escape existing immune effectors yet retain the core structural elements required for localization and function within the outer membrane. We examined this balance usingAnaplasma marginale, which generates antigenic variants in the outer membrane protein Msp2 using gene conversion. The overwhelming majority of Msp2 variants expressed during long-term persistent infection are mosaics, derived by recombination of oligonucleotide segments from multiple alleles to form unique hypervariable regions (HVR). As a result, the mosaics are not under long-term selective pressure to encode a functional protein; consequently, we hypothesized that the Msp2 HVR is structurally permissive for mosaic expression. Using an integrated approach of predictive modeling with determination of the native Msp2 protein structure and function, we demonstrate that structured elements, most notably, β-sheets, are significantly concentrated in the highly conserved N- and C-terminal domains. In contrast, the HVR is overwhelmingly a random coil, with the structured α-helices and β-sheets being confined to the genomically defined structural tethers that separate the antigenically variable microdomains. This structure is supported by the surface exposure of the HVR microdomains and the slow diffusion-type porin function in native Msp2. Importantly, the predominance of the random coil provides plasticity for the formation of functional HVR mosaics and realization of the full potential of segmental gene conversion to dramatically expand the variant repertoire.


2021 ◽  
Vol 10 (15) ◽  
Author(s):  
Irshad UI Haq ◽  
Kathryn R. Fixen

ABSTRACT The purple nonsulfur bacterium Rhodopseudomonas palustris RCB100 anaerobically degrades 3-chlorobenzoate (3-CBA), a halogenated pollutant. R. palustris RCB100 uses 3-CBA as a carbon source, while most R. palustris strains cannot. We report the complete genome sequence of strain RCB100 to help gain insight into how this bacterium degrades 3-CBA.


2015 ◽  
Vol 216 ◽  
pp. 65-66 ◽  
Author(s):  
Beiwen Zheng ◽  
Xiawei Jiang ◽  
Hong Cheng ◽  
Zemin Xu ◽  
Ang Li ◽  
...  

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