Journal article
Mechanical characterization of HIV-1 with a solid-state nanopore sensor
Electrophoresis, v 40(5), pp 776-783
Mar 2019
PMID: 30151981
Abstract
Enveloped viruses fuse with cells to transfer their genetic materials and infect the host cell. Fusion requires deformation of both viral and cellular membranes. Since the rigidity of viral membrane is a key factor in their infectivity, studying the rigidity of viral particles is of great significance in understating viral infection. In this paper, a nanopore is used as a single molecule sensor to characterize the deformation of pseudo-type human immunodeficiency virus type 1 at sub-micron scale. Non-infective immature viruses were found to be more rigid than infective mature viruses. In addition, the effects of cholesterol and membrane proteins on the mechanical properties of mature viruses were investigated by chemically modifying the membranes. Furthermore, the deformability of single virus particles was analyzed through a recapturing technique, where the same virus was analyzed twice. The findings demonstrate the ability of nanopore resistive pulse sensing to characterize the deformation of a single virus as opposed to average ensemble measurements.
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Details
- Title
- Mechanical characterization of HIV-1 with a solid-state nanopore sensor
- Creators
- Armin Darvish - Drexel UniversityJung Soo Lee - Southern Methodist UniversityBin Peng - Southern Methodist UniversityJugal Saharia - Southern Methodist UniversityRamalingam VenkatKalyana Sundaram - Department of Biochemistry and Molecular Biology, Drexel University College of Medicine, Philadelphia, PA, USAGaurav Goyal - Quantum Biosystems Inc Menlo Park CA USANuwan Bandara - Department of Mechanical Engineering, Southern Methodist University, Dallas, TX, USAChi Won Ahn - National NanoFab CenterJungsuk Kim - Department of Biomedical Engineering Gachon University Incheon Republic of KoreaPrashanta Dutta - Washington State UniversityIrwin Chaiken - Drexel UniversityMin Jun Kim - Southern Methodist University
- Publication Details
- Electrophoresis, v 40(5), pp 776-783
- Publisher
- Wiley
- Grant note
- NRF-2015M3A7B6027973 / National Research Foundation of Korea CMMI #1707818 / National Science Foundation R01GM111029 / NIH HHS #1712069 / National Science Foundation NRF-2015K1A4A3047100 / National Research Foundation of Korea R03 EB022759 / NIBIB NIH HHS R03EB022759 / NIH HHS NRF-2015M3A6B3068660 / National Research Foundation of Korea P01GM56550 / NIH HHS
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Biochemistry and Molecular Biology; Mechanical Engineering and Mechanics
- Web of Science ID
- WOS:000460305100018
- Scopus ID
- 2-s2.0-85052975529
- Other Identifier
- 991019169688104721
InCites Highlights
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- Collaboration types
- Domestic collaboration
- International collaboration
- Web of Science research areas
- Biochemical Research Methods
- Chemistry, Analytical