scholarly journals Characteristics of a Series of Three Bacteriophages Infecting Salmonella enterica Strains

2020 ◽  
Vol 21 (17) ◽  
pp. 6152 ◽  
Author(s):  
Katarzyna Kosznik-Kwaśnicka ◽  
Karolina Ciemińska ◽  
Michał Grabski ◽  
Łukasz Grabowski ◽  
Marcin Górniak ◽  
...  
Keyword(s):  
Salmonella Enterica ◽  
Phage Therapy ◽  
Functional Characterization ◽  
Bacterial Biofilm ◽  
Host Cells ◽  
Detailed Characterization ◽  
Food Protection ◽  
Adsorption Rates ◽  
Potential Use

Molecular and functional characterization of a series of three bacteriophages, vB_SenM-1, vB_SenM-2, and vB_SenS-3, infecting various Salmonella enterica serovars and strains is presented. All these phages were able to develop lytically while not forming prophages. Moreover, they were able to survive at pH 3. The phages revealed different host ranges within serovars and strains of S. enterica, different adsorption rates on host cells, and different lytic growth kinetics at various temperatures (in the range of 25 to 42 °C). They efficiently reduced the number of cells in the bacterial biofilm and decreased the biofilm mass. Whole genome sequences of these phages have been determined and analyzed, including their phylogenetic relationships. In conclusion, we have demonstrated detailed characterization of a series of three bacteriophages, vB_SenM-1, vB_SenM-2, and vB_SenS-3, which reveal favorable features in light of their potential use in phage therapy of humans and animals, as well as for food protection purposes.

scholarly journals Structural and Functional Characterization of ScsC, a Periplasmic Thioredoxin-Like Protein from Salmonella enterica Serovar Typhimurium

2013 ◽  
Vol 19 (13) ◽  
pp. 1494-1506 ◽  
Author(s):  
Mark Shepherd ◽  
Begoña Heras ◽  
Maud E. S. Achard ◽  
Gordon J. King ◽  
M. Pilar Argente ◽  
...  
Keyword(s):  
Salmonella Enterica ◽  
Salmonella Enterica Serovar Typhimurium ◽  
Functional Characterization ◽  
Serovar Typhimurium

scholarly journals Functional Characterization of a Redundant Plasmodium TRAP Family Invasin, TRAP-Like Protein, by Aldolase Binding and a Genetic Complementation Test

2008 ◽  
Vol 7 (6) ◽  
pp. 1062-1070 ◽  
Author(s):  
Kirsten Heiss ◽  
Hui Nie ◽  
Sumit Kumar ◽  
Thomas M. Daly ◽  
Lawrence W. Bergman ◽  
...  
Keyword(s):  
Functional Characterization ◽  
Cell Entry ◽  
Host Cells ◽  
Complementation Test ◽  
Type I ◽  
Cycle Progression ◽  
Targeted Gene Disruption ◽  
Specific Host ◽  
Host Cell Entry

ABSTRACT Efficient and specific host cell entry is of exquisite importance for intracellular pathogens. Parasites of the phylum Apicomplexa are highly motile and actively enter host cells. These functions are mediated by type I transmembrane invasins of the TRAP family that link an extracellular recognition event to the parasite actin-myosin motor machinery. We systematically tested potential parasite invasins for binding to the actin bridging molecule aldolase and complementation of the vital cytoplasmic domain of the sporozoite invasin TRAP. We show that the ookinete invasin CTRP and a novel, structurally related protein, termed TRAP-like protein (TLP), are functional members of the TRAP family. Although TLP is expressed in invasive stages, targeted gene disruption revealed a nonvital role during life cycle progression. This is the first genetic analysis of TLP, encoding a redundant TRAP family invasin, in the malaria parasite.

scholarly journals BspA and Pmp proteins ofTrichomonas vaginalismediate adherence to host cells

2018 ◽  
Author(s):  
Maria R. Handrich ◽  
Sriram G. Garg ◽  
Ewen W. Sommerville ◽  
Robert P. Hirt ◽  
Sven B. Gould
Keyword(s):  
Trichomonas Vaginalis ◽  
Functional Characterization ◽  
Surface Proteins ◽  
Host Cells ◽  
Protein Families ◽  
Sexually Transmitted ◽  
Trace Back ◽  
Oral Pathogens ◽  
Adhesion Performance

AbstractTrichomonas vaginalisis one of the most widespread, sexually transmitted pathogens. The infection involves a morphological switch from a free-swimming pyriform trophozoite to an amoeboid cell upon adhesion to host epithelial cells. While details on how the switch is induced and to what proteins of the host surface the parasite adheres remain poorly characterized, several surface proteins of the parasite itself have been identified as potential candidates. Among those are two expanded protein families that harbor domains that share similarity to functionally investigated surface proteins of prokaryotic oral pathogens; these are the BspA proteins of Bacteroidales and Spirochaetales, and the Pmp proteins of Chlamydiales. We sequenced the transcriptomes of five Trichomonads and screened for the presence of BspA and Pmp domain-containing proteins and tested the ability of individualT. vaginaliscandidates to mediate adhesion. Here we demonstrate that (i) BspA and Pmp domain-containing proteins are specifically expanded inT. vaginalisin comparison to other Trichomonads, and that (ii) individual proteins of both families have the ability to increase adhesion performance in a non-virulentT. vaginalisstrain andTetratrichomonas gallinarum, a parasite usually known to infect birds but not humans. Our results initiate the functional characterization of these two broadly distributed protein families, whose origin we trace back to the origin of Trichomonads themselves.

scholarly journals Structural and functional characterization of SiiA, an auxiliary protein from the SPI4‐encoded type 1 secretion system from Salmonella enterica

2019 ◽  
Vol 112 (5) ◽  
pp. 1403-1422 ◽  
Author(s):  
Peter Kirchweger ◽  
Sigrid Weiler ◽  
Claudia Egerer‐Sieber ◽  
Anna‐Theresa Blasl ◽  
Stefanie Hoffmann ◽  
...  
Keyword(s):  
Salmonella Enterica ◽  
Functional Characterization ◽  
Secretion System ◽  
Auxiliary Protein

Rheological and functional characterization of a biopolymer obtained from Beijerinckia sp. / Caracterización reológica y funcional de un biopolímero obtenido de Beijerinckia sp

1996 ◽  
Vol 2 (6) ◽  
pp. 405-411
Author(s):  
L.P. Martínez-Padilla ◽  
N. Cabada-Celis
Keyword(s):  
Food Industry ◽  
Culture Media ◽  
Functional Characterization ◽  
Dry Weight ◽  
Rheological Parameters ◽  
Power Law Model ◽  
Condi Tions ◽  
Almost All ◽  
Potential Use

An exopolysaccharide producer, Beijerinckia sp. was isolated and identified from a sample of soil. A sample of 10.3 g (dry weight) of polysaccharide/L was obtained by fermentation on liquid Czapek culture media supplemented with yeast extract. The functionality of the biopolymer was characterized for its potential use by the food industry. It showed shear thinning behaviour (pseudoplastic). The effects of concentration, temperature and pH were evaluated; almost all of the salts had no effect on rheological parameters of the power law model. There was a linear rela tionship between the percent of remaining emulsion after centrifugation and the polysaccharide biopolymer concentration, demonstrating the stabilizing effect of biopolymer on the emulsion. In contrast, the biopolymer was not able to form a gel under various pH and temperature condi tions, or with the addition of ions.

scholarly journals Identification and Functional Characterization of Chicken Toll-Like Receptor 5 Reveals a Fundamental Role in the Biology of Infection with Salmonella enterica Serovar Typhimurium

2005 ◽  
Vol 73 (4) ◽  
pp. 2344-2350 ◽  
Author(s):  
Muhammad Iqbal ◽  
Victoria J. Philbin ◽  
G. S. K. Withanage ◽  
Paul Wigley ◽  
Richard K. Beal ◽  
...  
Keyword(s):  
Salmonella Enterica ◽  
Salmonella Enterica Serovar Typhimurium ◽  
Functional Characterization ◽  
Systemic Infection ◽  
Structural Similarity ◽  
Conserved Sequence ◽  
Receptor Repertoire ◽  
Serovar Typhimurium ◽  
Toll Like Receptor 5

ABSTRACT Toll-like receptors (TLRs) are a major component of the pattern recognition receptor repertoire that detect invading microorganisms and direct the vertebrate immune system to eliminate infection. In chickens, the differential biology of Salmonella serovars (systemic versus gut-restricted localization) correlates with the presence or absence of flagella, a known TLR5 agonist. Chicken TLR5 (chTLR5) exhibits conserved sequence and structural similarity with mammalian TLR5 and is expressed in tissues and cell populations of immunological and stromal origin. Exposure of chTLR5+ cells to flagellin induced elevated levels of chicken interleukin-1β (chIL-1β) but little upregulation of chIL-6 mRNA. Consistent with the flagellin-TLR5 hypothesis, an aflagellar Salmonella enterica serovar Typhimurium fliM mutant exhibited an enhanced ability to establish systemic infection. During the early stages of infection, the fliM mutant induced less IL-1β mRNA and polymorphonuclear cell infiltration of the gut. Collectively, the data represent the identification and functional characterization of a nonmammalian TLR5 and indicate a role in restricting the entry of flagellated Salmonella into systemic sites of the chicken.

scholarly journals Structural and functional characterization of Salmonella enterica serovar Typhimurium YcbL: An unusual Type II glyoxalase

2010 ◽  
Vol 19 (10) ◽  
pp. 1897-1905 ◽  
Author(s):  
Anna L. Stamp ◽  
Paul Owen ◽  
Kamel El Omari ◽  
Charles E. Nichols ◽  
Michael Lockyer ◽  
...  
Keyword(s):  
Salmonella Enterica ◽  
Salmonella Enterica Serovar Typhimurium ◽  
Functional Characterization ◽  
Type Ii ◽  
Serovar Typhimurium ◽  
Unusual Type

scholarly journals Structural and functional characterization of the bacterial biofilm activator RemA

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Tamara Hoffmann ◽  
Devid Mrusek ◽  
Patricia Bedrunka ◽  
Fabiana Burchert ◽  
Christopher-Nils Mais ◽  
...  
Keyword(s):  
Functional Characterization ◽  
Regulatory Protein ◽  
Bacterial Biofilm ◽  
Binding Motifs ◽  
Expression Of Genes ◽  
Dna Binding Motifs ◽  
Matrix Production ◽  
In Vivo Characterization

AbstractBacillus subtilis can form structurally complex biofilms on solid or liquid surfaces, which requires expression of genes for matrix production. The transcription of these genes is activated by regulatory protein RemA, which binds to poorly conserved, repetitive DNA regions but lacks obvious DNA-binding motifs or domains. Here, we present the structure of the RemA homologue from Geobacillus thermodenitrificans, showing a unique octameric ring with the potential to form a 16-meric superstructure. These results, together with further biochemical and in vivo characterization of B. subtilis RemA, suggests that the protein can wrap DNA around its ring-like structure through a LytTR-related domain.

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