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Inhibition of Human Immunodeficiency Virus Type 1 Entry by a Keggin Polyoxometalate.


ABSTRACT: Here, we report the anti-human immunodeficiency virus (HIV) potency and underlying mechanisms of a Keggin polyoxometalate (PT-1, K?HPTi?W10O40). Our findings showed that PT-1 exhibited highly potent effects against a diverse group of HIV type 1 (HIV-1) strains and displayed low cytotoxicity and genotoxicity. The time-addition assay revealed that PT-1 acted at an early stage of infection, and these findings were supported by the observation that PT-1 had more potency against Env-pseudotyped virus than vesicular stomatitis virus glycoprotein (VSVG) pseudotyped virus. Surface plasmon resonance binding assays and flow cytometry analysis showed that PT-1 blocked the gp120 binding site in the CD4 receptor. Moreover, PT-1 bound directly to gp41 NHR (N36 peptide), thereby interrupting the core bundle formation of gp41. In conclusion, our data suggested that PT-1 may be developed as a new anti-HIV-1 agent through its effects on entry inhibition.

SUBMITTER: Wang X 

PROVIDER: S-EPMC5977258 | biostudies-literature | 2018 May

REPOSITORIES: biostudies-literature

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Inhibition of Human Immunodeficiency Virus Type 1 Entry by a Keggin Polyoxometalate.

Wang Xiaoli X   Wang Jiao J   Zhang Wenmei W   Li Boye B   Zhu Ying Y   Hu Qin Q   Yang Yishu Y   Zhang Xiaoguang X   Yan Hong H   Zeng Yi Y  

Viruses 20180516 5


Here, we report the anti-human immunodeficiency virus (HIV) potency and underlying mechanisms of a Keggin polyoxometalate (PT-1, K₆HPTi₂W<sub>10</sub>O<sub>40</sub>). Our findings showed that PT-1 exhibited highly potent effects against a diverse group of HIV type 1 (HIV-1) strains and displayed low cytotoxicity and genotoxicity. The time-addition assay revealed that PT-1 acted at an early stage of infection, and these findings were supported by the observation that PT-1 had more potency against  ...[more]

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