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Key interactions in HIV-1 maturation identified by hydrogen-deuterium exchange

Abstract

To characterize the intersubunit interactions underlying assembly and maturation in HIV-1, we determined the amide hydrogen exchange protection pattern of capsid protein in the immature virion and the mature virion using mass spectrometry. Alterations in protection upon maturation provide evidence for the maturation-induced formation of an interaction between the N- and C-terminal domains in half of the capsid molecules, indicating that only half of the capsid protein is assembled into the conical core.

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Figure 1: (a) Mass-to-charge ratio spectra for the 28+ charge state of CA in mVLP (red spectra) and in solution (black spectra) after 0 and 30 s, 5 and 45 min, and 9 and 30 h of H/D exchange.
Figure 2: ESI FT-ICR mass spectra for the peptide spanning CA residues 55–68 in iVLP (left) and mVLP (right) after H/D exchange.

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Acknowledgements

This work was supported by grants from the US National Institutes of Health (AI44626) and the US National Science Foundation (CHE-99-09502), Florida State University and the US National High Magnetic Field Laboratory.

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Correspondence to Peter E Prevelige Jr.

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The authors declare no competing financial interests.

Supplementary information

Supplementary Fig. 1

SDS-PAGE of immature and mature VLPs. (PDF 71 kb)

Supplementary Fig. 2

Exchange profiles for CA peptides. (PDF 135 kb)

Supplementary Methods (PDF 21 kb)

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Lanman, J., Lam, T., Emmett, M. et al. Key interactions in HIV-1 maturation identified by hydrogen-deuterium exchange. Nat Struct Mol Biol 11, 676–677 (2004). https://doi.org/10.1038/nsmb790

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