Characterization of the Antiviral Activity for Influenza Viruses M1 Zinc Finger Peptides

Wang, Yongjin; Xiao, Huihui; Wu, Nannan; Shi, Huiling; Xu, Hongwei; Zhou, Linan; Xi, Xu-Guang; Wang, Xiaoming

doi:10.1007/s00284-010-9682-6

Cited by 3 publications

(2 citation statements)

References 22 publications

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“…Zn fingers bind RNA and mediate protein-protein interactions. A Zn finger protein was found to inhibit influenza virus replication [35][36][37][38]. Under experimental conditions, Zn combines with TMP forming fixed complex preserving the anti-bacterial properties of TMP but without evidence of anti-virus [39,40].…”

Section: Discussionmentioning

confidence: 99%

Combination therapy of zinc and trimethoprim inhibits infection of influenza A virus in chick embryo

Habbal

Magdi²

2021

Virol J

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Background Respiratory RNA viruses including influenza virus have been a cause of health and economic hardships. These viruses depend on its host for replication and infection. Influenza virus infection is lethal to the chick embryo. We examined whether a combination of trimethoprim and zinc (Tri-Z), that acts on the host, can reduce the lethal effect of influenza A virus in chick embryo model. Method Influenza virus was isolated from patients and propagated in eggs. We determined viral load that infects 50% of eggs (50% egg lethal dose, ELD50). We introduced 10 ELD50 into embryonated eggs and repeated the experiments using 100 ELD50. A mixture of zinc oxide (Zn) and trimethoprim (TMP) (weight/weight ratios ranged from 0.01 to 0.3, Zn/TMP with increment of 0.1) was tested for embryo survival of the infection (n = 12 per ratio, in triplicates). Embryo survival was determined by candling eggs daily for 7 days. Controls of Zn, TMP, saline or convalescent serum were conducted in parallel. The effect of Tri-Z on virus binding to its cell surface receptor was evaluated in a hemagglutination inhibition (HAI) assay using chicken red cells. Tri-Z was prepared to concentration of 10 mg TMP and 1.8 mg Zn per ml, then serial dilutions were made. HAI effect was expressed as scores where ++++ = no effect; 0 = complete HAI effect. Results TMP, Zn or saline separately had no effect on embryo survival, none of the embryos survived influenza virus infection. All embryos treated with convalescent serum survived. Tri-Z, at ratio range of 0.15–0.2 (optimal ratio of 0.18) Zn/TMP, enabled embryos to survive influenza virus despite increasing viral load (> 80% survival at optimal ratio). At concentration of 15 µg/ml of optimal ratio, Tri-Z had total HAI effect (scored 0). However, at clinical concentration of 5 µg/ml, Tri-Z had partial HAI effect (+ +). Conclusion Acting on host cells, Tri-Z at optimal ratio can reduce the lethal effect of influenza A virus in chick embryo. Tri-Z has HAI effect. These findings suggest that combination of trimethoprim and zinc at optimal ratio can be provided as treatment for influenza and possibly other respiratory RNA viruses infection in man.

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Section: Discussionmentioning

confidence: 99%

Combination therapy of zinc and trimethoprim inhibits infection of influenza A virus in chick embryo

Habbal

Magdi²

2021

Virol J

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“…Peptides mimicking influenza virus RdRp binding sites also showed anti-influenza activity [41–43]. However, the results for the zinc finger motif peptide of M1 being used for the inhibition of influenza virus are controversial [44–46]. Zanamivir was developed from the non-inhibitory prototype sialidase inhibitor [47,48].…”

Section: Discussionmentioning

confidence: 99%

Inhibition of Influenza Virus Replication by Constrained Peptides Targeting Nucleoprotein

Jiang

et al. 2011

Antivir Chem Chemother

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Cytoplasmic tails of bunyavirus Gn glycoproteins—Could they act as matrix protein surrogates?

2013

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Viruses of the family Bunyaviridae are negative-sense RNA viruses (NRVs). Unlike other NRVs bunyaviruses do not possess a matrix protein, which typically facilitates virus release from host cells and acts as an anchor between the viral membrane and its genetic core. Therefore the functions of matrix protein in bunyaviruses need to be executed by other viral proteins. In fact, the cytoplasmic tail of glycoprotein Gn (Gn-CT) of various bunyaviruses interacts with the genetic core (nucleocapsid protein and/or genomic RNA). In addition the Gn-CT of phleboviruses (a genus in the family Bunyaviridae) has been demonstrated to be essential for budding. This review brings together what is known on the role of various bunyavirus Gn-CTs in budding and assembly, and hypothesizes on their yet unrevealed functions in viral life cycle by comparing to the matrix proteins of NRVs.

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Characterization of the Antiviral Activity for Influenza Viruses M1 Zinc Finger Peptides

Cited by 3 publications

References 22 publications

Combination therapy of zinc and trimethoprim inhibits infection of influenza A virus in chick embryo

Combination therapy of zinc and trimethoprim inhibits infection of influenza A virus in chick embryo

Inhibition of Influenza Virus Replication by Constrained Peptides Targeting Nucleoprotein

Cytoplasmic tails of bunyavirus Gn glycoproteins—Could they act as matrix protein surrogates?

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