دورية أكاديمية
أعرض في EDS

Single-Point Mutations in Qβ Virus-like Particles Change Binding to Cells.

التفاصيل البيبلوغرافية
العنوان: Single-Point Mutations in Qβ Virus-like Particles Change Binding to Cells.
المؤلفون: Martino ML; Department of Chemistry, The Scripps Research Institute, La Jolla, California 92037, United States., Crooke SN; School of Chemistry and Biochemistry, School of Biological Sciences, Georgia Institute of Technology, Atlanta, Georgia 30332, United States., Manchester M; Skaggs School of Pharmacy and Pharmaceutical Sciences, University of California, San Diego, California 92093, United States., Finn MG; Department of Chemistry, The Scripps Research Institute, La Jolla, California 92037, United States.; School of Chemistry and Biochemistry, School of Biological Sciences, Georgia Institute of Technology, Atlanta, Georgia 30332, United States.
المصدر: Biomacromolecules [Biomacromolecules] 2021 Aug 09; Vol. 22 (8), pp. 3332-3341. Date of Electronic Publication: 2021 Jul 12.
نوع المنشور: Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S.
اللغة: English
بيانات الدورية: Publisher: American Chemical Society Country of Publication: United States NLM ID: 100892849 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1526-4602 (Electronic) Linking ISSN: 15257797 NLM ISO Abbreviation: Biomacromolecules Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Washington, DC : American Chemical Society, c2000-
مواضيع طبية MeSH: Allolevivirus* , Point Mutation*, Animals ; Capsid ; Capsid Proteins/genetics ; Cell Membrane
مستخلص: Virus-like particles (VLPs) constitute large, polyvalent platforms onto which a wide variety of functional units can be grafted. Their use in biological settings often depends on their specific binding to cells or receptors of interest; this can be compromised by excessive nonspecific association with other cells. We found that lysine residues mediate such nonspecific interactions, presumably by virtue of protonation and interaction with anionic membrane lipid headgroups and/or complementary residues of cell surface proteins and polysaccharides. Chemical acylation of surface-exposed amines of the Qβ VLP led to a significant reduction in the association of particles with mammalian cells. Single-point mutations of particular lysine residues to either glutamine, glutamic acid, tryptophan, or phenylalanine were mostly well-tolerated and formed intact capsids, but the introduction of double and triple mutants was far less forgiving. Introduction of glutamic acid at position 13 (K13E) led to a dramatic increase in cellular binding, whereas removal of the lysine at position 46 (K46Q) led to an equally striking reduction. Several plasma membrane components were found to specifically interact with the Qβ capsid irrespective of surface charge. These results suggest that specific cellular interactions are engaged or obviated by such mutations and provide us with more "benign" particles to which can be added binding functionality for targeted delivery applications.
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معلومات مُعتمدة: R01 CA112075 United States CA NCI NIH HHS
المشرفين على المادة: 0 (Capsid Proteins)
تواريخ الأحداث: Date Created: 20210712 Date Completed: 20210927 Latest Revision: 20220811
رمز التحديث: 20231215
مُعرف محوري في PubMed: PMC9068229
DOI: 10.1021/acs.biomac.1c00443
PMID: 34251176
قاعدة البيانات: MEDLINE
الوصف
تدمد:1526-4602
DOI:10.1021/acs.biomac.1c00443