Mass Spectrometry of an Intact Virus

Fuerstenau, Stephen D.; Benner, W. Henry; Thomas, John J.; Brugidou, Christophe; Bothner, Brian; Siuzdak, Gary

doi:10.1002/1521-3757(20010202)113:3<559::aid-ange559>3.0.co;2-#

Cited by 141 publications

(34 citation statements)

References 20 publications

(23 reference statements)

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“…The inherently high selectivity of MS greatly facilitates the detection of coexisting proteins and protein conformers, such that highly purified samples are not always an absolute requirement [35,36]. The practical upper mass limit of MS has yet to be established; the detection of very large proteins and MDa complexes, intact organelles, and even whole viruses has been reported [37][38][39][40][41].…”

Section: Introductionmentioning

confidence: 52%

“…Copyright 2007 Elsevier. example, the assembly of viruses represents a self-contained, problem amenable to study [38,39,196,203]. Several viruses have been recovered in viable and infective form by the use of "soft landing" techniques, thereby adding a preparative functionality to the mass spectrometer [39,204].…”

Section: Ongoing Developments and Future Di-rectionsmentioning

confidence: 99%

See 1 more Smart Citation

Protein Folding and Protein-Ligand Interactions Monitored by Electrospray Mass Spectrometry

Ferguson¹,

Kuprowski²,

Boys³

et al. 2009

CAC

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Electrospray ionization (ESI) mass spectrometry (MS) has become an indispensable tool for studies on protein structure, folding, dynamics, and interactions. The ESI process generates intact and multiply protonated ions from proteins in solution. The charge state distribution of these ions provides a highly sensitive probe for the overall compactness of a protein in solution. Unfolded conformers lead to the formation of higher charge states than natively folded proteins. Due to its very gentle nature, ESI allows the transfer of intact noncovalent assemblies (protein-ligand and protein-protein complexes) into the gas phase. Thus, ESI-MS is ideally suited for monitoring coupled folding/binding events. The remarkable selectivity of this technique facilitates the observation of co-existing conformers and binding states. This review discusses mechanistic aspects of the ionization process, as well as selected examples that illustrate the use of ESI-MS for monitoring protein folding and assembly reactions. The combination of ESI-MS with on-line mixing techniques can provide mechanistic insights into processes occurring on very rapid time scales. We also address the interesting question whether biomolecular structures in the gas phase resemble those in solution. Experimental approaches involving hydrogen exchange and covalent labeling techniques are covered in an accompanying article.

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Section: Introductionmentioning

confidence: 52%

Section: Ongoing Developments and Future Di-rectionsmentioning

confidence: 99%

Protein Folding and Protein-Ligand Interactions Monitored by Electrospray Mass Spectrometry

Ferguson¹,

Kuprowski²,

Boys³

et al. 2009

CAC

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show abstract

“…Methods of extending the detectable mass range include postseparation acceleration (29), postseparation dissociation into smaller-mass fragment ions (30), and cryogenic detection (31). Even with these extensions, there is a strong interest in mass spectrometry of still higher mass entities (28) that can currently be satisfied only by special types of mass analysis such as the charge-induction tube (32) and specially modified quadrupole ion traps (33,34). DOFMS provides a unique method for mass analysis in this very high mass region.…”

Section: Where Truly Unlimited M/z Range Is Neededmentioning

confidence: 99%

Distance-of-Flight Mass Spectrometry: A New Paradigm for Mass Separation and Detection

Enke

Ray

Graham

et al. 2012

Annual Rev. Anal. Chem.

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Distance-of-flight mass spectrometry (DOFMS) offers the advantages of physical separation of ions, array detection of ions, focusing of initial ion energy, great simplicity, and a truly unlimited mass range. DOFMS instrumentation is similar to that of time-of-flight mass spectrometry (TOFMS) and shares its ion-source versatility, batch analysis, and rapid spectral-generation rate. With constant-momentum ion acceleration and an ion mirror, there is a time at which ions of all mass-to-charge values are energy focused at their particular distances along the flight path. A pulsed field orthogonal to the flight path drives the ions to reach the detector array at this specific time. Results from a 0.29-m proof-of-principle instrument verify the theoretically predicted energy focus and demonstrate how the range of mass-to-charge values that impinge on the detector array can be readily changed. DOFMS could be combined sequentially with TOFMS to enable simultaneous scanless tandem mass spectrometry.

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“…Recent approaches utilize combinations of techniques (FIGURE 1), where differential enzymatic digestions of whole virions [10] or solubilized and deconvoluted virion proteins are analyzed [11]. Protein mixtures thus obtained are fragmented into peptides that are further separated by 1D or multidimensional liquid chromatography (LC) and analyzed by MS [12].…”

Section: Virion Proteomicsmentioning

confidence: 99%

“…Since virus particles are megadalton-sized molecular aggregates, the mass-to-charge ratio of unfragmented virus proteins is usually higher than 20 kDa, well above the detection limit of common MS instruments. Despite this limitation, there are some interesting reports on whole virion analysis by MS [38][39][40]. A whole virus analysis of cricket paralysis virus identified four capsid proteins: VP1, VP2, VP3 and a polypeptide homologous to human picorna virus VP4 [41].…”

Section: Analysis Of Whole Virionmentioning

confidence: 99%

Viral proteomics: global evaluation of viruses and their interaction with the host

Viswanathan

Früh

2007

Expert Review of Proteomics

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Viruses constantly adapt to and modulate the host environment during replication and propagation. Both DNA and RNA viruses encode multifunctional proteins that interact with and modify host cell proteins. While viral genomes were the first complete sequences known, the corresponding proteomes are only now elucidated, with some surprising results. Even more daunting is the task to globally monitor the impact of viral infection on the proteome of the host cell and many technical hurdles must still be overcome in order to facilitate robust and reproducible measurements. Further complicating the picture is the dynamic nature of proteins, including post-translational modifications, enzymatic cleavage and activation or destruction by proteolytic events. Nevertheless, several promising studies have been published using high-throughput methods directly measuring protein abundance. Particularly, quantitative or semiquantitative mass spectrometry-based analysis of viral and cellular proteomes are now being used to characterize viruses and their host interaction. In addition, the full set of interactions between viral and host proteins, the interactome, is beginning to emerge, with often unexpected interactions that need to be carefully validated. In this review, we will discuss two major areas of viral proteomics: first, virion proteomics (such as the protein characterization of viral particles) and second, proteoviromics, including the viral protein interactomics and the quantitative analysis of host cell proteome during viral infection.

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Mass Spectrometry of an Intact Virus

Cited by 141 publications

References 20 publications

Protein Folding and Protein-Ligand Interactions Monitored by Electrospray Mass Spectrometry

Protein Folding and Protein-Ligand Interactions Monitored by Electrospray Mass Spectrometry

Distance-of-Flight Mass Spectrometry: A New Paradigm for Mass Separation and Detection

Viral proteomics: global evaluation of viruses and their interaction with the host

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