Molecular Characterization of Fructose-1,6-bisphosphate Aldolase From Trichinella spiralis and Its Potential in Inducing Immune Protection [PDF]
Frontiers in Cellular and Infection Microbiology, 2019 Trichinella spiralis is a major food-borne parasite worldwide. Trichinellosis caused by T. spiralis is not only a public health problem, but also an economic hazard in food safety. The development of effective vaccines to prevent Trichinella infection in
, Xue Bai, Xiaolei Liu
exaly +4 more sources
Multifunctional Fructose 1,6-Bisphosphate Aldolase as a Therapeutic Target [PDF]
Frontiers in Molecular Biosciences, 2021 Fructose 1,6-bisphosphate aldolase is a ubiquitous cytosolic enzyme that catalyzes the fourth step of glycolysis. Aldolases are classified into three groups: Class-I, Class-IA, and Class-II; all classes share similar structural features but low amino ...
David B. Pirovich +2 more
doaj +2 more sources
Molecular characterization and immune efficacy of fructose-1,6-bisphosphate aldolase from Haemaphysalis longicornis (Acari: Ixodidae) [PDF]
Parasites & Vectors, 2023 Background Ticks are obligate hematophagous ectoparasites that transmit a variety of pathogens to humans, wildlife and domestic animals. Vaccination is an effective and environmentally friendly method for tick control. Fructose-1,6-bisphosphate aldolase (
Yuan-Yuan Cao +6 more
doaj +2 more sources
Characterization of Fructose-1,6-Bisphosphate Aldolase 1 of Echinococcus multilocularis [PDF]
Veterinary Sciences, 2021 Glycolysis is one of the important ways by which Echinococcus multilocularis acquires energy. Fructose-1, 6-bisphosphate aldolase (FBA) plays an important role in this process, but it is not fully characterized in E. multilocularis yet.
Xuedong He +10 more
doaj +2 more sources
In silico study of 4-phosphorylated derivatives of 1,3-oxazole as inhibitors of Candida albicans fructose-1,6-bisphosphate aldolase II [PDF]
Heliyon, 2019 In this study, the synthesis, in vitro anti-Candida activity and molecular modeling of 4-phosphorylated derivatives of 1,3-oxazole as inhibitors of Candida albicans fructose-1,6-bisphosphate aldolase (FBA-II) are demonstrated and discussed.
Ivan V. Semenyuta +4 more
doaj +2 more sources
Fructose 1,6-Bisphosphate Aldolase, a Novel Immunogenic Surface Protein on Listeria Species. [PDF]
PLoS ONE, 2016 Listeria monocytogenes is a ubiquitous food-borne pathogen, and its presence in food or production facilities highlights the importance of surveillance.
Marcelo Mendonça +9 more
doaj +2 more sources
The metabolic enzyme fructose-1,6-bisphosphate aldolase acts as a transcriptional regulator in pathogenic Francisella [PDF]
Nature Communications, 2017 The enzyme fructose-bisphosphate aldolase (FBA) plays central roles in glycolysis and gluconeogenesis. Here, Ziveri et al. show that FBA of the pathogen Francisella novicida acts, in addition, as a transcriptional regulator and is important for bacterial
Jason Ziveri +11 more
doaj +2 more sources
Fructose-1,6-bisphosphate aldolase encoded by a core gene of Mycoplasma hyopneumoniae contributes to host cell adhesion [PDF]
Veterinary Research, 2018 Mycoplasma hyopneumoniae is an important respiratory pathogen that causes great economic losses to the pig industry worldwide. Although some putative virulence factors have been reported, pathogenesis remains poorly understood.
Yanfei Yu +9 more
doaj +2 more sources
Porphyrin Excretion Resulting From Mutation of a Gene Encoding a Class I Fructose 1,6-Bisphosphate Aldolase in Rhodobacter capsulatus [PDF]
Frontiers in Microbiology, 2019 This paper describes a mutant (called SB1707) of the Rhodobacter capsulatus wild type strain SB1003 in which a transposon-disrupted rcc01707 gene resulted in a ∼25-fold increase in the accumulation of coproporphyrin III in the medium of phototrophic ...
Hao Ding +3 more
doaj +2 more sources
Fructose‐1,6‐bisphosphate aldolase of Neisseria meningitidis binds human plasminogen via its C‐terminal lysine residue [PDF]
MicrobiologyOpen, 2016 Neisseria meningitidis is a leading cause of fatal sepsis and meningitis worldwide. As for commensal species of human neisseriae, N. meningitidis inhabits the human nasopharynx and asymptomatic colonization is ubiquitous.
Fariza Shams +5 more
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