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• W1709871131 abstract "We have previously shown that FLSC, a chimeric protein containing HIV-1BAL gp120 and the D1 and D2 domains of human CD4, blocks the binding and entry of HIV-1 into target cells by occluding CCR5, the major HIV-1 coreceptor. In an effort to improve the antiviral potential of FLSC, we fused it with the hinge-CH2-CH3 region of human IgG1. The IgG moiety should increase both the affinity and stability in vivo of FLSC, due to the resultant bivalency and an extended serum half-life, thereby increasing its antiviral potency. We previously showed that (FLSC) IgG1 indeed had greater antiviral activity against T cell infections. Here we extend these results to macrophages, for which (FLSC) IgG1 has a more potent antiviral activity than FLSC alone, due in part to its higher binding affinity for CCR5. We also test both compounds in a relevant humanized mouse model and show that, as anticipated, the IgG1 moiety confers a greatly extended half-life. These data, taken together with previous results, suggest potential clinical utility for (FLSC) IgG1 and support further developmental work toward eventual clinical trials." @default.
• W1709871131 created "2016-06-24" @default.
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• W1709871131 date "2016-02-01" @default.
• W1709871131 modified "2023-09-23" @default.
• W1709871131 title "Full Length Single Chain Fc Protein (FLSC IgG1) as a Potent Antiviral Therapy Candidate: Implications forIn VivoStudies" @default.
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• W1709871131 doi "https://doi.org/10.1089/aid.2015.0020" @default.
• W1709871131 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4761833" @default.
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