In-silico comparison of inhibition of wild and drug-resistant Haemonchus contortus β-tubulin isotype-1 by glycyrrhetinic acid, thymol and albendazole interactions

Athithan, Velan; Hoda, Muddasarul

doi:10.1007/s12639-020-01274-w

Cited by 7 publications

(2 citation statements)

References 20 publications

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“…Currently, the treatment options available for gastrointestinal nematode disease in sheep primarily include chemical prevention and chemotherapeutic control. However, the limitations of chemical anthelmintics, such as nematode resistance, environmental pollution, and food safety, are becoming a major concern in the prevention of the disease [2,3]. Therefore, biological control using nematophagous fungi has gained the focus of researchers for the prevention and control of gastrointestinal nematode diseases in sheep.…”

Section: Introductionmentioning

confidence: 99%

Biological Characteristics of Recombinant Arthrobotrys oligospora Chitinase AO-801

Gong

Meng²,

Qiao³

et al. 2022

Korean J Parasitol

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Chitinase AO-801 is a hydrolase secreted by Arthrobotrys oligospora during nematode feeding, while its role remained elusive. This study analyzed the molecular characteristics of recombinant chitinase of Arthrobotrys oligospora (reAO-801). AO-801 belongs to the typical glycoside hydrolase 18 family with conserved chitinase sequence and tertiary structure of (α/β)8 triose-phosphate isomerase (TIM) barrel. The molecular weight of reAO-801 was 42 kDa. reAO-801 effectively degraded colloidal and powdered chitin, egg lysate, and stage I larval lysate of Caenorhabditis elegans. The activity of reAO-801 reached its peak at 40˚C and pH values between 4-7. Enzyme activity was inhibited by Zn2+, Ca2+, and Fe3+, whereas Mg2+ and K+ potentiated its activity. In addition, urea, sodium dodecyl sulfate, and 2-mercaptoethanol significantly inhibited enzyme activity. reAO-801 showed complete nematicidal activity against C. elegans stage I larvae. reAO-801 broke down the C. elegans egg shells, causing them to die or die prematurely by hatching the eggs. It also invoked degradation of Haemonchus contortus eggs, resulting in apparent changes in the morphological structure. This study demonstrated the cytotoxic effect of reAO-801, which laid the foundation for further dissecting the mechanism of nematode infestation by A. oligospora.

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Section: Introductionmentioning

confidence: 99%

Biological Characteristics of Recombinant Arthrobotrys oligospora Chitinase AO-801

Gong

Meng²,

Qiao³

et al. 2022

Korean J Parasitol

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“…Molecular simulation studies showed that the binding of benzimidazole is also impaired by the mutation of amino acids at positions 198 in addition to 200, while the F167Y mutation has no discernible impact [18]. However, insignificant changes in the binding pocket of 167, 198, and 200 mutant β-tubulin models to the benzimidazoles were exemplified [19].…”

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confidence: 99%

Structural Diversity in Beta-Tubulin Isotype 1 Protein of Benzimidazole Resistant and Susceptible Haemonchus Contortus

K.A.,

V.K.,

C.S.

et al. 2024

EAMR

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INTRODUCTIONResistance of various parasites to different antiparasitic drugs by the parasites infecting sheep is not a contemporary problem but recorded more in recent times [1].In 1964, Drudge and co-workers first documented thiabendazole resistance [2]. Thereafter, several authors reported benzimidazole resistance from various parts of the world. At the molecular level, resistance to benzimidazole is linked primarily to the mutation in three amino acids at position F167Y, E198A, and F200Y in the gene β-tubulin isotype 1 [3,4,5].The mutations in the β-tubulin gene were reported in Teladorsagia circumcincta [5,6], Ascaris lumbricoides at position 167 [7], and 200 [8] from Brazil, Haemonchus contortus at position 198 and 200 from India [9, 10, 11] and at position 198 and 200 in China [12], Bunostomum trigonocephalum at position 200 [13], Trichuris trichiura and Necator americanus from Southern Mozambique [14].Mutation at these positions alters the binding pocket formed by the β-tubulin for the benzimidazole drugs, thus reducing the binding affinity of the drug [15,16]. Robinson et al. (2004) gave a possible explanation of the role of phenylalanine residue at position 200 interacting with albendazole based on the molecular docking study [17]. The substitution of tyrosine for

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Application of Box-Behnken design in the optimization and development of albendazole-loaded zein nanoparticles as a drug repurposing approach for colorectal cancer management

Mneimneh,

Hayar,

Al Hadeethi

et al. 2024

International Journal of Biological Macromolecules

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In-silico comparison of inhibition of wild and drug-resistant Haemonchus contortus β-tubulin isotype-1 by glycyrrhetinic acid, thymol and albendazole interactions

Cited by 7 publications

References 20 publications

Biological Characteristics of Recombinant Arthrobotrys oligospora Chitinase AO-801

Biological Characteristics of Recombinant Arthrobotrys oligospora Chitinase AO-801

Structural Diversity in Beta-Tubulin Isotype 1 Protein of Benzimidazole Resistant and Susceptible Haemonchus Contortus

Application of Box-Behnken design in the optimization and development of albendazole-loaded zein nanoparticles as a drug repurposing approach for colorectal cancer management

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