Identification and characterization of Bacillus anthracis spore-associated proteins

2012 ◽  
Author(s):  
Krista A. Spreng
Keyword(s):  
Bacillus Anthracis ◽  
Associated Proteins ◽  
Identification And Characterization

scholarly journals Identification and Characterization of Two Novel Proteins Affecting Fission Yeast γ-tubulin Complex Function

2004 ◽  
Vol 15 (5) ◽  
pp. 2287-2301 ◽  
Author(s):  
Srinivas Venkatram ◽  
Joseph J. Tasto ◽  
Anna Feoktistova ◽  
Jennifer L. Jennings ◽  
Andrew J. Link ◽  
...  
Keyword(s):  
Fission Yeast ◽  
Complex Function ◽  
Novel Proteins ◽  
Astral Microtubule ◽  
Different Types ◽  
Associated Proteins ◽  
Microtubule Formation ◽  
Identification And Characterization ◽  
Microtubule Function

The γ-tubulin complex, via its ability to organize microtubules, is critical for accurate chromosome segregation and cytokinesis in the fission yeast, Schizosaccharomyces pombe. To better understand its roles, we have purified the S. pombe γ-tubulin complex. Mass spectrometric analyses of the purified complex revealed known components and identified two novel proteins (i.e., Mbo1p and Gfh1p) with homology to γ-tubulin–associated proteins from other organisms. We show that both Mbo1p and Gfh1p localize to microtubule organizing centers. Although cells deleted for either mbo1+ or gfh1+ are viable, they exhibit a number of defects associated with altered microtubule function such as defects in cell polarity, nuclear positioning, spindle orientation, and cleavage site specification. In addition, mbo1Δ and gfh1Δ cells exhibit defects in astral microtubule formation and anchoring, suggesting that these proteins have specific roles in astral microtubule function. This study expands the known roles of γ-tubulin complex components in organizing different types of microtubule structures in S. pombe.

Identification and characterization of Bacillus anthracis by multiplex PCR on DNA chip

2004 ◽  
Vol 20 (4) ◽  
pp. 807-813 ◽  
Author(s):  
Shi-Hua Wang ◽  
Ji-Kai Wen ◽  
Ya-Feng Zhou ◽  
Zhi-Ping Zhang ◽  
Rui-Fu Yang ◽  
...  
Keyword(s):  
Bacillus Anthracis ◽  
Multiplex Pcr ◽  
Dna Chip ◽  
Identification And Characterization

scholarly journals Identification and characterization of clinical Bacillus spp. isolates phenotypically similar to Bacillus anthracis

2010 ◽  
Vol 313 (1) ◽  
pp. 47-53 ◽  
Author(s):  
Cari A. Beesley ◽  
Cynthia L. Vanner ◽  
Leta O. Helsel ◽  
Jay E. Gee ◽  
Alex R. Hoffmaster
Keyword(s):  
Bacillus Anthracis ◽  
Bacillus Spp ◽  
Identification And Characterization

scholarly journals Identification and Characterization of the gerH Operon of Bacillus anthracis Endospores: a Differential Role for Purine Nucleosides in Germination

2003 ◽  
Vol 185 (4) ◽  
pp. 1462-1464 ◽  
Author(s):  
Matthew A. Weiner ◽  
Timothy D. Read ◽  
Philip C. Hanna
Keyword(s):  
Amino Acids ◽  
Bacillus Anthracis ◽  
Germination Response ◽  
Identification And Characterization

ABSTRACT We identified a tri-cistronic operon, gerH, in Bacillus anthracis that is important for endospore germination triggered by two distinct germination response pathways termed inosine-His and purine-Ala. Together, the two pathways allow B. anthracis endospores a broader recognition of purines and amino acids that may be important for host-mediated germination.

Identification and characterization of a germination operon on the virulence plasmid pXOl of Bacillus anthracis

1999 ◽  
Vol 33 (2) ◽  
pp. 407-414 ◽  
Author(s):  
Chantal Guidi-Rontani ◽  
Yannick Pereira ◽  
Stephanie Ruffie ◽  
Jean-Claude Sirard ◽  
Martine Weber-Levy ◽  
...  
Keyword(s):  
Bacillus Anthracis ◽  
Virulence Plasmid ◽  
Identification And Characterization

scholarly journals Identification of Novel Virulence-Associated Proteins Secreted to Xylem by Verticillium nonalfalfae During Colonization of Hop Plants

2016 ◽  
Vol 29 (5) ◽  
pp. 362-373 ◽  
Author(s):  
Marko Flajsman ◽  
Stanislav Mandelc ◽  
Sebastjan Radisek ◽  
Natasa Stajner ◽  
Jernej Jakse ◽  
...  
Keyword(s):  
Plant Pathogens ◽  
Xylem Sap ◽  
Hypothetical Protein ◽  
Secreted Proteins ◽  
In Planta ◽  
Fungal Virulence ◽  
Associated Proteins ◽  
Verticillium Nonalfalfae ◽  
Identification And Characterization

Plant pathogens employ various secreted proteins to suppress host immunity for their successful host colonization. Identification and characterization of pathogen-secreted proteins can contribute to an understanding of the pathogenicity mechanism and help in disease control. We used proteomics to search for proteins secreted to xylem by the vascular pathogen Verticillium nonalfalfae during colonization of hop plants. Three highly abundant fungal proteins were identified: two enzymes, α-N-arabinofuranosidase (VnaAbf4.216) and peroxidase (VnaPRX1.1277), and one small secreted hypothetical protein (VnaSSP4.2). These are the first secreted proteins so far identified in xylem sap following infection with Verticillium spp. VnaPRX1.1277, classified as a heme-containing peroxidase from Class II, similar to other Verticillium spp. lignin-degrading peroxidases, and VnaSSP4.2, a 14-kDa cysteine-containing protein with unknown function and with a close homolog in related V. alfalfae strains, were further examined. The in planta expression of VnaPRX1.1277 and VnaSSP4.2 genes increased with the progression of colonization, implicating their role in fungal virulence. Indeed, V. nonalfalfae deletion mutants of both genes exhibited attenuated virulence on hop plants, which returned to the level of the wild-type pathogenicity in the knockout complementation lines, supporting VnaPRX1.1277 and VnaSSP4.2 as virulence factors required to promote V. nonalfalfae colonization of hop plants.

scholarly journals Identification and Characterization of the Rhoptry Neck Protein 2 in Babesia divergens and B. microti

2016 ◽  
Vol 84 (5) ◽  
pp. 1574-1584 ◽  
Author(s):  
Rosalynn L. Ord ◽  
Marilis Rodriguez ◽  
Jeny R. Cursino-Santos ◽  
Hyunryung Hong ◽  
Manpreet Singh ◽  
...  
Keyword(s):  
Direct Role ◽  
Parasite Invasion ◽  
Content Type ◽  
Apicomplexan Parasites ◽  
Babesia Divergens ◽  
Associated Proteins ◽  
Identification And Characterization

Apicomplexan parasites include those of the generaPlasmodium,Cryptosporidium, andToxoplasmaand those of the relatively understudied zoonotic genusBabesia. In humans, babesiosis, particularly transfusion-transmitted babesiosis, has been emerging as a major threat to public health. Like malaria, the disease pathology is a consequence of the parasitemia which develops through cyclical replication ofBabesiaparasites in host erythrocytes. However, there are no exoerythrocytic stages inBabesia, so targeting of the blood stage and associated proteins to directly prevent parasite invasion is the most desirable option for effective disease control. Especially promising among such molecules are the rhoptry neck proteins (RONs), whose homologs have been identified in many apicomplexan parasites. RONs are involved in the formation of the moving junction, along with AMA1, but no RON has been identified and characterized in anyBabesiaspp. Here we identify the RON2 proteins ofBabesia divergens(BdRON2) andB. microti(BmRON2) and show that they are localized apically and that anti-BdRON2 antibodies are significant inhibitors of parasite invasionin vitro. Neither protein is immunodominant, as both proteins react only marginally with sera from infected animals. Further characterization of the direct role of both BdRON2 and BmRON2 in parasite invasion is required, but knowledge of the level of conformity of RON2 proteins within the apicomplexan phylum, particularly that of the AMA1-RON2 complex at the moving junction, along with the availability of an animal model forB. microtistudies, provides a key to target this complex with a goal of preventing the erythrocytic invasion of these parasites and to further our understanding of the role of these conserved ligands in invasion.

scholarly journals Identification and Characterization of Two Transmembrane Proteins Required for Virulence of Ustilago maydis

2021 ◽  
Vol 12 ◽  
Author(s):  
Paul Weiland ◽  
Florian Altegoer
Keyword(s):  
Virulence Factors ◽  
Biochemical Analysis ◽  
Transmembrane Proteins ◽  
Ustilago Maydis ◽  
Effector Proteins ◽  
Smut Fungi ◽  
Initial Characterization ◽  
Associated Proteins ◽  
Identification And Characterization

Smut fungi comprise a large group of biotrophic phytopathogens infecting important crops such as wheat and corn. Through the secretion of effector proteins, the fungus actively suppresses plant immune reactions and modulates its host’s metabolism. Consequently, how soluble effector proteins contribute to virulence is already characterized in a range of phytopathogens. However, membrane-associated virulence factors have been much less studied to date. Here, we investigated six transmembrane (TM) proteins that show elevated gene expression during biotrophic development of the maize pathogen Ustilago maydis. We show that two of the six proteins, named Vmp1 and Vmp2 (virulence-associated membrane protein), are essential for the full virulence of U. maydis. The deletion of the corresponding genes leads to a substantial attenuation in the virulence of U. maydis. Furthermore, both are conserved in various related smuts and contain no domains of known function. Our biochemical analysis clearly shows that Vmp1 and Vmp2 are membrane-associated proteins, potentially localizing to the U. maydis plasma membrane. Mass photometry and light scattering suggest that Vmp1 mainly occurs as a monomer, while Vmp2 is dimeric. Notably, the large and partially unstructured C-terminal domain of Vmp2 is crucial for virulence while not contributing to dimerization. Taken together, we here provide an initial characterization of two membrane proteins as virulence factors of U. maydis.

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