Influenza A H1N1 Virus 2009 Synthetic Hemagglutinin and Neuraminidase Peptides for Antibody Detection

Ávila, Guillermina; Cruz-Licea, Verónica; Rojas-Espinosa, Karla; Bermúdez-Álvarez, Yesenia; Grostieta, Estefanía; Romero‐Valdovinos, Mirza; Martínez‐Hernández, Fernando; Vaughan, Gilberto; Flisser, Ana

doi:10.1016/j.arcmed.2020.04.011

Cited by 7 publications

(2 citation statements)

References 25 publications

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“…Influenza virus neuraminidase (NA) is an enzyme that catalyzes the obliteration of terminal sialic acid residues (sialidase) which aids in liberating new virions formed from the infected cells and circulating to infect the neighboring cells ( Abed et al., 2016 ). As such, the NA inhibition can defend the host from being infected and prevent its proliferation ( Avila et al., 2020 ). Due to the highly preserved active site structure of neuraminidase ( Adams et al., 2019 ), it has become an attractive molecular target for the exploration and development of novel anti-influenza inhibitors.…”

Section: Introductionmentioning

confidence: 99%

RETRACTED: In-silico modelling studies of 5-benzyl-4-thiazolinone derivatives as influenza neuraminidase inhibitors via 2D-QSAR, 3D-QSAR, molecular docking, and ADMET predictions

Abdullahi

Uzairu

Shallangwa

et al. 2022

Heliyon

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Section: Introductionmentioning

confidence: 99%

RETRACTED: In-silico modelling studies of 5-benzyl-4-thiazolinone derivatives as influenza neuraminidase inhibitors via 2D-QSAR, 3D-QSAR, molecular docking, and ADMET predictions

Abdullahi

Uzairu

Shallangwa

et al. 2022

Heliyon

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“…Influenza virus neuraminidase is an enzyme that catalyzes the obliteration of terminal sialic acid residues (sialidase) which aids in liberating new virions formed from the infected cells and circulating to infect the neighboring cells [15]. The neuraminidase (NA) inhibition can defend the host cells from being infected and prevent its proliferation [16]. Due to the highly preserved active site structure of neuraminidase [17], it has become an attractive molecular target for the exploration and development of novel anti-influenza inhibitors.…”

mentioning

confidence: 99%

Computational modelling studies of some 1,3-thiazine derivatives as anti-influenza inhibitors targeting H1N1 neuraminidase via 2D-QSAR, 3D-QSAR, molecular docking, and ADMET predictions

Abdullahi

Uzairu

Shallangwa

et al. 2022

Beni-Suef Univ J Basic Appl Sci

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Background Influenza virus disease remains one of the most contagious diseases that aided the deaths of many patients, especially in this COVID-19 pandemic era. Recent discoveries have shown that the high prevalence of influenza and SARS-CoV-2 coinfection can rapidly increase the death rate of patients. Hence, it became necessary to search for more potent inhibitors for influenza disease therapy. The present study utilized some computational modeling concepts such as 2D-QSAR, 3D-QSAR, molecular docking simulation, and ADMET predictions of some 1,3-thiazine derivatives as inhibitors of influenza neuraminidase (NA). Results The 2D-QSAR modeling results showed GFA-MLR ($$R_{{\text{train }}}^{2}$$ R train 2 = 0.9192, Q2 = 0.8767, R2adj = 0.8991, RMSE = 0.0959, $$R_{{{\text{test}}}}^{2}$$ R test 2 = 0.8943, $$R_{{{\text{pred}}}}^{2}$$ R pred 2 = 0.7745) and GFA-ANN ($$R_{{\text{train }}}^{2}$$ R train 2 = 0.9227, Q2 = 0.9212, RMSE = 0.0940, $$R_{{{\text{test}}}}^{2}$$ R test 2 = 0.8831, $$R_{{{\text{pred}}}}^{2}$$ R pred 2 = 0.7763) models with the computed descriptors as ATS7s, SpMax5_Bhv, nHBint6, and TDB9m for predicting the NA inhibitory activities of compounds which have passed the global criteria of accepting QSAR model. The 3D-QSAR modeling was carried out based on the comparative molecular field analysis (CoMFA) and comparative similarity indices analysis (CoMSIA). The CoMFA_ES ($$R_{{\text{train }}}^{2}$$ R train 2 = 0.9620, Q2 = 0.643) and CoMSIA_SED ($$R_{{\text{train }}}^{2}$$ R train 2 = 0.8770, Q2 = 0.702) models were found to also have good and reliable predicting ability. The compounds were also virtually screened based on their binding scores via molecular docking simulations with the active site of the NA (H1N1) target receptor which also confirms their resilient potency. Four potential lead compounds (4, 7, 14, and 15) with the relatively high inhibitory rate (> 50%) and docking (> − 6.3 kcal/mol) scores were identified as the possible lead candidates for in silico exploration of improved anti-influenza agents. Conclusion The drug-likeness and ADMET predictions of the lead compounds revealed non-violation of Lipinski’s rule and good pharmacokinetic profiles as important guidelines for rational drug design. Hence, the outcome of this research set a course for the in silico design and exploration of novel NA inhibitors with improved potency.

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Evaluation of a mimotope of the Rickettsia outer membrane protein A (OmpA) as an antigen in enzyme-linked immunosorbent assay to detect rickettsiosis in capybaras (Hydrochoerus hydrochaeris), horses (Equus caballus), and opossums (Didelphis sp.)

et al. 2023

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Influenza A H1N1 Virus 2009 Synthetic Hemagglutinin and Neuraminidase Peptides for Antibody Detection

Cited by 7 publications

References 25 publications

RETRACTED: In-silico modelling studies of 5-benzyl-4-thiazolinone derivatives as influenza neuraminidase inhibitors via 2D-QSAR, 3D-QSAR, molecular docking, and ADMET predictions

RETRACTED: In-silico modelling studies of 5-benzyl-4-thiazolinone derivatives as influenza neuraminidase inhibitors via 2D-QSAR, 3D-QSAR, molecular docking, and ADMET predictions

Computational modelling studies of some 1,3-thiazine derivatives as anti-influenza inhibitors targeting H1N1 neuraminidase via 2D-QSAR, 3D-QSAR, molecular docking, and ADMET predictions

Evaluation of a mimotope of the Rickettsia outer membrane protein A (OmpA) as an antigen in enzyme-linked immunosorbent assay to detect rickettsiosis in capybaras (Hydrochoerus hydrochaeris), horses (Equus caballus), and opossums (Didelphis sp.)

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