scholarly journals Characterization of Staphylococcus intermedius Group Isolates Associated with Animals from Antarctica and Emended Description of Staphylococcus delphini

2020 ◽  
Vol 8 (2) ◽  
pp. 204 ◽  
Author(s):  
Veronika Vrbovská ◽  
Ivo Sedláček ◽  
Michal Zeman ◽  
Pavel Švec ◽  
Vojtěch Kovařovic ◽  
...  
Keyword(s):  
Rpob Gene ◽  
Protein Distribution ◽  
Pathogenic Potential ◽  
Weddell Seals ◽  
Polymerase Beta ◽  
Flight Mass Spectrometry ◽  
Isolation And Characterization ◽  
Staphylococcus Intermedius ◽  
The Antarctic

Members of the genus Staphylococcus are widespread in nature and occupy a variety of niches, however, staphylococcal colonization of animals in the Antarctic environment has not been adequately studied. Here, we describe the first isolation and characterization of two Staphylococcus intermedius group (SIG) members, Staphylococcus delphini and Staphylococcus pseudintermedius, in Antarctic wildlife. Staphylococcus delphini were found exclusively in Adélie penguins. The report of S. pseudintermedius from Weddell seals confirmed its occurrence in all families of the suborder Caniformia. Partial RNA polymerase beta-subunit (rpoB) gene sequencing, repetitive PCR fingerprinting with the (GTG)5 primer, and matrix-assisted laser-desorption/ionization time-of-flight mass spectrometry gave consistent identification results and proved to be suitable for identifying SIG members. Comparative genomics of S. delphini isolates revealed variable genomic elements, including new prophages, a novel phage-inducible chromosomal island, and numerous putative virulence factors. Surface and extracellular protein distribution were compared between genomes and showed strain-specific profiles. The pathogenic potential of S. delphini was enhanced by a novel type of exfoliative toxin, trypsin-like serine protease cluster, and enterotoxin C. Detailed analysis of phenotypic characteristics performed on six Antarctic isolates of S. delphini and eight reference strains from different animal sources enabled us to emend the species description of S. delphini.

scholarly journals Isolation and Characterization of Campylobacter spp. from Antarctic Fur Seals (Arctocephalus gazella) at Deception Island, Antarctica

2010 ◽  
Vol 76 (17) ◽  
pp. 6013-6016 ◽  
Author(s):  
F. J. García-Peña ◽  
D. Pérez-Boto ◽  
C. Jiménez ◽  
E. San Miguel ◽  
A. Echeita ◽  
...  
Keyword(s):  
Marine Mammals ◽  
Arctocephalus Gazella ◽  
Deception Island ◽  
Weddell Seals ◽  
Isolation And Characterization ◽  
Fur Seals ◽  
Campylobacter Lari ◽  
The Antarctic ◽  
Antarctic Fur Seals

ABSTRACT The presence of Campylobacter spp. was investigated in 41 Antarctic fur seals (Arctocephalus gazella) and 9 Weddell seals (Leptonychotes weddellii) at Deception Island, Antarctica. Infections were encountered in six Antarctic fur seals. The isolates, the first reported from marine mammals in the Antarctic region, were identified as Campylobacter insulaenigrae and Campylobacter lari.

scholarly journals Isolation and Characterization of a Helicobacter sp. from the Gastric Mucosa of Dolphins, Lagenorhynchus acutusand Delphinus delphis

2000 ◽  
Vol 66 (11) ◽  
pp. 4751-4757 ◽  
Author(s):  
Claudia M. G. Harper ◽  
Charles A. Dangler ◽  
Shilu Xu ◽  
Yan Feng ◽  
Zeli Shen ◽  
...  
Keyword(s):  
Gastric Mucosa ◽  
Gastric Ulcers ◽  
Parasitic Infections ◽  
Common Dolphin ◽  
Pathogenic Potential ◽  
16S Rrna Analysis ◽  
Ulcer Disease ◽  
Delphinus Delphis ◽  
Isolation And Characterization

ABSTRACT Gastric ulcerations in dolphins have been reported for decades. Some of these lesions were associated with parasitic infections. However, cases of nonparasitic gastric ulcers with no clearly defined etiology also have been reported in wild and captive dolphins. Considerable speculation exists as to whether dolphins haveHelicobacter-associated gastritis and peptic ulcer disease. The stomachs of seven stranded Atlantic white-sided dolphins,Lagenorhynchus acutus, and 1 common dolphin,Delphinus delphis, were assessed for the presence ofHelicobacter species. Novel Helicobacterspecies were identified by culture in the gastric mucosa of two of the eight dolphins studied and by PCR in seven of the eight dolphins. The gram-negative organisms were urease, catalase, and oxidase positive. Spiral to fusiform bacteria were detected in gastric mucosa by Warthin Starry staining. Histopathology revealed mild to moderate diffuse lymphoplasmacytic gastritis within the superficial mucosa of the main stomach. The pyloric stomach was less inflamed, and bacteria did not extend deep into the glands. The lesions parallel those observed inHelicobacter pylori-infected humans. Bacteria from two dolphins classified by 16S rRNA analysis clustered with gastric helicobacters and represent a novel Helicobacter sp. most closely related to H. pylori. These findings suggest that a novel Helicobacter sp. may play a role in the etiopathogenesis of gastritis and gastric ulcers in dolphins. To our knowledge this represents the first isolation and characterization of a novel Helicobacter sp. from a marine mammal and emphasizes the wide host distribution and pathogenic potential of this increasingly important genus.

scholarly journals Purification and characterization of a tetrameric α-macroglobulin proteinase inhibitor from the gastropod mollusc Biomphalaria glabrata

1996 ◽  
Vol 316 (3) ◽  
pp. 893-900 ◽  
Author(s):  
Randall C. BENDER ◽  
Christopher J. BAYNE
Keyword(s):  
Quaternary Structure ◽  
Proteinase Inhibitors ◽  
Cysteine Proteinase ◽  
Serine Proteinase ◽  
Biomphalaria Glabrata ◽  
Sedimentation Equilibrium ◽  
Flight Mass Spectrometry ◽  
Isolation And Characterization ◽  
Α2 Macroglobulin

The α-macroglobulin proteinase inhibitors (αMs) are a family of proteins with the unique ability to inhibit a broad spectrum of proteinases. Whereas monomeric, dimeric and tetrameric αMs have been identified in vertebrates, all invertebrate αMs characterized so far have been dimeric. This paper reports the isolation and characterization of a tetrameric αM from the tropical planorbid snail Biomphalaria glabrata. The sequence of 18 amino acids at the N-terminus indicates homology with other αMs. The subunit mass of approx. 200 kDa was determined by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry and SDS/PAGE. The quaternary structure was determined by sedimentation equilibrium centrifugation and native pore-limit electrophoresis. Evidence for a thioester is provided by the fact that methylamine treatment prevents the autolytic cleavage of the snail αM subunit and results in the release of 4 mol of thiols per mol of snail αM. The snail αM inhibited the serine proteinase trypsin, the cysteine proteinase bromelain and the metalloproteinase thermolysin. The spectrum of proteinases inhibited, together with the demonstration of steric protection of the proteinase active site and a ‘slow to fast’ conformational change after reacting with trypsin, all suggest that the inhibitory mechanism of the snail αM is similar to the ‘trap mechanism’ of human α2-macroglobulin.

Revisiting theAcanthamoebaspecies that form star-shaped cysts (genotypes T7, T8, T9, and T17): characterization of seven new Brazilian environmental isolates and phylogenetic inferences

Parasitology ◽  
2011 ◽  
Vol 139 (1) ◽  
pp. 45-52 ◽  
Author(s):  
ANA C. M. MAGLIANO ◽  
MARTA M. G. TEIXEIRA ◽  
SILVIA C. ALFIERI
Keyword(s):  
Opportunistic Infections ◽  
Phylogenetic Analyses ◽  
Sequence Divergence ◽  
Rrna Gene ◽  
Pathogenic Potential ◽  
Morphological Group ◽  
Isolation And Characterization ◽  
Group I ◽  
Group 2

SUMMARYFree-living amoebae of the genusAcanthamoebaare the agents of both opportunistic and non-opportunistic infections and are frequently isolated from the environment. Of the 17 genotypes (T1–T17) identified thus far, 4 (T7, T8, T9, and T17) accommodate the rarely investigated species of morphological group I, those that form large, star-shaped cysts. We report the isolation and characterization of 7 new Brazilian environmentalAcanthamoebaisolates, all assigned to group I. Phylogenetic analyses based on partial (∼1200 bp) SSU rRNA gene sequences placed the new isolates in the robustly supported clade composed of the species of morphological group I. One of the Brazilian isolates is closely related toA. comandoni(genotype T9), while the other 6, together with 2 isolates recently assigned to genotype T17, form a homogeneous, well-supported group (2 0% sequence divergence) that likely represents a newAcanthamoebaspecies. Thermotolerance, osmotolerance, and cytophatic effects, features often associated with pathogenic potential, were also examined. The results indicated that all 7 Brazilian isolates grow at temperatures up to 40°C, and resist under hyperosmotic conditions. Additionally, media conditioned by each of the newAcanthamoebaisolates induced the disruption of SIRC and HeLa cell monolayers.

scholarly journals MDP1, a Saccharomyces cerevisiae Gene Involved in Mitochondrial/Cytoplasmic Protein Distribution, Is Identical to the Ubiquitin-Protein Ligase Gene RSP5

Genetics ◽  
1997 ◽  
Vol 145 (3) ◽  
pp. 595-603 ◽  
Author(s):  
Teresa Żołądek ◽  
Anna Tobiasz ◽  
Gabriela Vaduva ◽  
Magda Boguta ◽  
Nancy C Martin ◽  
...  
Keyword(s):  
Actin Cytoskeleton ◽  
Subcellular Distribution ◽  
Nonsense Suppression ◽  
Protein Distribution ◽  
Multicopy Suppressor ◽  
Ubiquitin Protein Ligase ◽  
Cytoskeleton Organization ◽  
Isolation And Characterization ◽  
Initiation Of Translation

Alteration of the subcellular distribution of Mod5p-I, a tRNA modification enzyme, member of the sorting isozyme family, affects tRNA-mediated nonsense suppression. Altered suppression efficiency was used to identify MDP genes, which, when mutant, change the mitochondrial/cytosolic distribution of Mod5p-I,KR6. MDP2 is the previously identified VRP1, which encodes verprolin, required for proper organization of the actin cytoskeleton. MDP3 is identical to PAN1, which encodes a protein involved in initiation of translation and actin cytoskeleton organization. We report here the cloning and characterization of wild-type and mutant MDP1 alleles and the isolation and characterization of a multicopy suppressor of mdp1 mutations. MDP1 is identical to RSP5, which encodes ubiquitin-protein ligase, and mdp1 mutations are suppressed by high copy expression of ubiquitin. All four characterized mdp1 mutations cause missense changes located in the hect domain of Rsp5p that is highly conserved among ubiquitin-protein ligases. In addition to its well-known function in protein turnover, ubiquitination has been proposed to play roles in subcellular sorting of proteins via endocytosis and in delivery of proteins to peroxisomes, the endoplasmic reticulum and mitochondria. mdp1, as well as mdp2/vrp1 and mdp3/pan1 mutations, affect endocytosis. Further, mdp1 mutations show synthetic interactions with mdp2/vrp1 and mdp3/pan1. Identification of MDP1 as RSP5, along with our previous identification of MDP2/VRP1 and MDP3/PAN1, implicate interactions of the ubiquitin system, the actin cytoskeleton and protein synthesis in the subcellular distribution of proteins.

Isolation and Characterization of Antifreeze Proteins from the Antarctic Marine Microalga Pyramimonas gelidicola

2014 ◽  
Vol 16 (5) ◽  
pp. 502-512 ◽  
Author(s):  
Woongsic Jung ◽  
Yunho Gwak ◽  
Peter L. Davies ◽  
Hak Jun Kim ◽  
EonSeon Jin
Keyword(s):  
Antifreeze Proteins ◽  
Marine Microalga ◽  
Isolation And Characterization ◽  
Antarctic Marine ◽  
The Antarctic
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