Mass spectrometric approaches to study enveloped viruses: New possibilities for structural biology and prophylactic medicine

Kordyukova, Larisa V.; Serebryakova, Marina V.

doi:10.1134/s0006297912080044

Cited by 8 publications

(3 citation statements)

References 86 publications

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“…The use of mass spectrometry for characterizing glycosylation in influenza viruses themselves has been comprehensively summarized in recent reviews. − By using MS coupled with PNGase F treatment, Beer et al identified a list of N-linked glycosylation sites on HA1 of a circulating influenza A (H3N2), among which the NYT at position 158-160 was determined to contribute largely to the alteration of the epitopes of some neutralizing monoclonal antibodies so that these antibodies may eventually lose their capacity to neutralize the viruses. In another work by Cruz et al, the site-specific glycosylation profile of influenza A (H1N1) hemagglutinin was straightforwardly determined by HCD/CID-MS/MS with the aid of data interpretation by the Byonic search engine.…”

Section: Glycosylationmentioning

confidence: 99%

Proteomics in Influenza Research: The Emerging Role of Posttranslational Modifications

et al. 2020

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Influenza viruses continue evolving and have the ability to cause a global pandemic, so it is very important to elucidate its pathogenesis and find new treatment methods. In recent years, proteomics has made important contributions to describing the dynamic interaction between influenza viruses and their hosts, especially in posttranslational regulation of a variety of key biological processes. Protein posttranslational modifications (PTMs) increase the diversity of functionality of the organismal proteome and affect almost all aspects of pathogen biology, primarily by regulating the structure, function, and localization of the modified proteins. Considerable technical achievements in mass spectrometry-based proteomics have been made in a large number of proteome-wide surveys of PTMs in many different organisms. Herein we specifically focus on the proteomic studies regarding a variety of PTMs that occur in both the influenza viruses, mainly influenza A viruses (IAVs), and their hosts, including phosphorylation, ubiquitination and ubiquitin-like modification, glycosylation, methylation, acetylation, and some types of acylation. Integration of these data sets provides a unique scenery of the global regulation and interplay of different PTMs during the interaction between IAVs and their hosts. Various techniques used to globally profiling these PTMs, mostly MS-based approaches, are discussed regarding their increasing roles in mechanical regulation of interaction between influenza viruses and their hosts.

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Section: Glycosylationmentioning

confidence: 99%

Proteomics in Influenza Research: The Emerging Role of Posttranslational Modifications

et al. 2020

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“…The same codons were verified by the next-generation sequencing (NGS) analysis (see below). Furthermore, the Cys-126/Val-219 (rWSN) and Ser-126/Ile-219 (WSN strain) residues were observed in the respective M1 proteins when an approach routinely used in our laboratory (Kordyukova & Serebryakova, 2012), based on the in situ trypsin hydrolysis/matrix-assisted laser desorption/ionization time-of-flight MS (MALDI-TOF MS) analysis of electrophoretic protein bands, was applied ( Fig. 6; Supplementary Figs.…”

Section: M1 Protein Bioinformatics and Structural Analysismentioning

confidence: 99%

Filamentous versus Spherical Morphology: A Case Study of the Recombinant A/WSN/33 (H1N1) Virus

et al. 2020

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Influenza A virus is a serious human pathogen that assembles enveloped virions on the plasma membrane of the host cell. The pleiomorphic morphology of influenza A virus, represented by spherical, elongated, or filamentous particles, is important for the spread of the virus in nature. Using fixative protocols for sample preparation and negative staining electron microscopy, we found that the recombinant A/WSN/33 (H1N1) (rWSN) virus, a strain considered to be strictly spherical, may produce filamentous particles when amplified in the allantoic cavity of chicken embryos. In contrast, the laboratory WSN strain and the rWSN virus amplified in Madin–Darby canine kidney cells exhibited a spherical morphology. Next-generation sequencing (NGS) suggested a rare Ser126Cys substitution in the M1 protein of rWSN, which was confirmed by the mass spectrometric analysis. No structurally relevant substitutions were found by NGS in other proteins of rWSN. Bioinformatics algorithms predicted a neutral structural effect of the Ser126Cys mutation. The mrWSN_M1_126S virus generated after the introduction of the reverse Cys126Ser substitution exhibited a similar host-dependent partially filamentous phenotype. We hypothesize that a shortage of some as-yet-undefined cellular components involved in virion budding and membrane scission may result in the appearance of filamentous particles in the case of usually “nonfilamentous” virus strains.

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“…Proteomics has been largely used for the study of virus structure, test vaccine preparation, and strain identification. [112][113][114][115][116] The potential for clinical applications of MS for studying host cell interaction and analyzing biomarkers of the virus itself or linked to the host response has been reviewed elsewhere. [117] The detection of viral proteins can be performed directly in various fluids or cells from infected patients.…”

Section: Analysis Of Virusesmentioning

confidence: 99%

Mass spectrometry for the detection of bioterrorism agents: from environmental to clinical applications

Duriez¹,

Armengaud

Fenaille

et al. 2016

J. Mass Spectrom.

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In the current context of international conflicts and localized terrorist actions, there is unfortunately a permanent threat of attacks with unconventional warfare agents. Among these, biological agents such as toxins, microorganisms, and viruses deserve particular attention owing to their ease of production and dissemination. Mass spectrometry (MS)-based techniques for the detection and quantification of biological agents have a decisive role to play for countermeasures in a scenario of biological attacks. The application of MS to every field of both organic and macromolecular species has in recent years been revolutionized by the development of soft ionization techniques (MALDI and ESI), and by the continuous development of MS technologies (high resolution, accurate mass HR/AM instruments, novel analyzers, hybrid configurations). New possibilities have emerged for exquisite specific and sensitive detection of biological warfare agents. MS-based strategies for clinical application can now address a wide range of analytical questions mainly including issues related to the complexity of biological samples and their available volume. Multiplexed toxin detection, discovery of new markers through omics approaches, and identification of untargeted microbiological or of novel molecular targets are examples of applications. In this paper, we will present these technological advances along with the novel perspectives offered by omics approaches to clinical detection and follow-up.

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Mass spectrometric approaches to study enveloped viruses: New possibilities for structural biology and prophylactic medicine

Cited by 8 publications

References 86 publications

Proteomics in Influenza Research: The Emerging Role of Posttranslational Modifications

Proteomics in Influenza Research: The Emerging Role of Posttranslational Modifications

Filamentous versus Spherical Morphology: A Case Study of the Recombinant A/WSN/33 (H1N1) Virus

Mass spectrometry for the detection of bioterrorism agents: from environmental to clinical applications

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