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Identification of Novel Interactions in HIV-1 Capsid Protein Assembly by High-resolution Mass Spectrometry

Lanman, Jason, Lam, TuKiet T., Barnes, Stephen, Sakalian, Michael, Emmett, Mark R., Marshall, Alan G., Prevelige, Peter E.·2003·Journal of Molecular Biology

DOI 10.1016/s0022-2836(02)01245-7

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Abstract

The pleomorphic nature of the immature and mature HIV-1 virions has made it difficult to characterize intersubunit interactions using traditional approaches. While the structures of isolated domains are known, the challenge is to identify intersubunit interactions and thereby pack these domains into supramolecular structures. Using high-resolution mass spectrometry, we have measured the amide hydrogen exchange protection factors for the soluble capsid protein (CA) and CA assembled in vitro. Comparison of the protection factors as well as chemical crosslinking experiments has led to a map of the subunit/subunit interfaces in the assembled tubes. This analysis provides direct biochemical evidence for the homotypic N domain and C domain interactions proposed from cryo-electron microscopy image reconstruction of CA tubes. Most significantly, we have identified a previously unrecognized intersubunit N domain-C domain interaction. The detection of this interaction reconciles previously discrepant biophysical and genetic data.

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Authors: Lanman, J., Lam, T. T., Barnes, S., Sakalian, M., Emmett, M. R., Marshall, A. G., & Prevelige, P. E.
Affiliations: University of Alabama at Birmingham (US)
Florida State University (US)
University of Oklahoma Health Sciences Center (US)
Corresponding author: Prevelige, Peter E.
ORCID: Lam, TuKiet T.
Barnes, Stephen
Emmett, Mark R.
Marshall, Alan G.
Venue: Journal of Molecular Biology
Publisher: Elsevier BV
Published: 2003-01
Volume: 325
Issue: 4
Pages: 759-772
ISSN: 0022-2836 (ISSN-L)
DOI: 10.1016/s0022-2836(02)01245-7
OpenAlex: W1968718594
Cited by: 206
References: 56
Citations by year: 2026: 1 · 2023: 1 · 2022: 3 · 2021: 2 · 2020: 3 · 2019: 3 · 2018: 1 · 2017: 3 · 2016: 2 · 2015: 6 · 2014: 7 · 2013: 14 · 2012: 8
FWCI: 5.06
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
Locations: Journal of Molecular Biology (publishedVersion)
PubMed (publishedVersion)
Funders: National Science Foundation
National High Magnetic Field Laboratory
National Institutes of Health (5r01gm031683-17)
National Cancer Institute (T32 CA 09467, T32CA009467)
National Institute of General Medical Sciences (GM 31683)
National Institute of Allergy and Infectious Diseases (AI 44626, R01AI044626)
Topics: Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
Physical Sciences › Chemistry › Spectroscopy › Mass Spectrometry Techniques and Applications
Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
Keywords: HIV-1 capsid protein, intersubunit interactions, amide hydrogen exchange, N-domain, C-domain, subunit interface, chemical crosslinking, supramolecular structure
MeSH terms: Amides, Cross-Linking Reagents, Deuterium, Hydrogen, Models, Molecular, Mass Spectrometry, HIV-1, Mutagenesis, Site-Directed, Protein Structure, Tertiary, Dimerization, Protein Structure, Quaternary, Protein Subunits, Capsid Proteins, Macromolecular Substances

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Identification of Novel Interactions in HIV-1 Capsid Protein Assembly by High-resolution Mass Spectrometry

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