scholarly journals Top-Down and Bottom-Up Proteomics Methods to Study RNA Virus Biology

Viruses ◽  
2021 ◽  
Vol 13 (4) ◽  
pp. 668
Author(s):  
Yogy Simanjuntak ◽  
Kira Schamoni-Kast ◽  
Alice Grün ◽  
Charlotte Uetrecht ◽  
Pietro Scaturro

RNA viruses cause a wide range of human diseases that are associated with high mortality and morbidity. In the past decades, the rise of genetic-based screening methods and high-throughput sequencing approaches allowed the uncovering of unique and elusive aspects of RNA virus replication and pathogenesis at an unprecedented scale. However, viruses often hijack critical host functions or trigger pathological dysfunctions, perturbing cellular proteostasis, macromolecular complex organization or stoichiometry, and post-translational modifications. Such effects require the monitoring of proteins and proteoforms both on a global scale and at the structural level. Mass spectrometry (MS) has recently emerged as an important component of the RNA virus biology toolbox, with its potential to shed light on critical aspects of virus–host perturbations and streamline the identification of antiviral targets. Moreover, multiple novel MS tools are available to study the structure of large protein complexes, providing detailed information on the exact stoichiometry of cellular and viral protein complexes and critical mechanistic insights into their functions. Here, we review top-down and bottom-up mass spectrometry-based approaches in RNA virus biology with a special focus on the most recent developments in characterizing host responses, and their translational implications to identify novel tractable antiviral targets.

FEBS Open Bio ◽  
2021 ◽  
Author(s):  
Khadija Daoudi ◽  
Christian Malosse ◽  
Ayoub Lafnoune ◽  
Bouchra Darkaoui ◽  
Salma Chakir ◽  
...  

2018 ◽  
Vol 90 (4) ◽  
pp. 2756-2764 ◽  
Author(s):  
Daniel A. Polasky ◽  
Frederik Lermyte ◽  
Michael Nshanian ◽  
Frank Sobott ◽  
Phillip C. Andrews ◽  
...  

2019 ◽  
Vol 19 (1) ◽  
pp. 221-237 ◽  
Author(s):  
Ada Soler-Ventura ◽  
Marina Gay ◽  
Meritxell Jodar ◽  
Mar Vilanova ◽  
Judit Castillo ◽  
...  

Radiocarbon ◽  
2021 ◽  
pp. 1-15
Author(s):  
G Salazar ◽  
S Szidat

ABSTRACT Since radiocarbon accelerator mass spectrometry (14C AMS) is considered a high-precision technique, reassessment of the measurement uncertainty has been a topic of interest. Scientists from analytical and metrological fields have developed the top-down and bottom-up measurement of uncertainty approaches. The 14C quoted error should approximate the uncertainty of long-term repetitions of the top-down approach in order to be realistic. The novelty of this paper is that the uncertainty of both approaches were approximated to each other. Furthermore, we apportioned the graphitization, instrumentation, and bias components in order to additively expand the quoted error. Our results are comparable to error multipliers and to long-term repeatability studies reported by other laboratories. Our laboratory was established in late 2012 with N2 as stripper gas and 7 years later, we changed to helium stripper. Thus, we were able to compare both gases, and demonstrate that helium is a better stripper gas. In absolute F14C units, the ranges of graphitization+bias combined uncertainties were (0.7 to 4.1) × 10–3 for N2 and (0.7–3.0) × 10–3 for He depending on the standard 14C content. The error multiplier for He defined as the expanded uncertainty over quoted error, in average, was 1.7; while without the bias, the multiplier was 1.3.


2017 ◽  
Vol 89 (16) ◽  
pp. 8244-8250 ◽  
Author(s):  
Nobuaki Takemori ◽  
Ayako Takemori ◽  
Piriya Wongkongkathep ◽  
Michael Nshanian ◽  
Rachel R. Ogorzalek Loo ◽  
...  

2015 ◽  
Vol 24 (8) ◽  
pp. 1292-1300 ◽  
Author(s):  
Albert Konijnenberg ◽  
Ludovic Bannwarth ◽  
Duygu Yilmaz ◽  
Armağan Koçer ◽  
Catherine Venien-Bryan ◽  
...  

2015 ◽  
Vol 26 (3) ◽  
pp. 482-492 ◽  
Author(s):  
Yelena Yefremova ◽  
Mahmoud Al-Majdoub ◽  
Kwabena F. M. Opuni ◽  
Cornelia Koy ◽  
Weidong Cui ◽  
...  

The Analyst ◽  
2015 ◽  
Vol 140 (20) ◽  
pp. 7020-7029 ◽  
Author(s):  
Russell E. Bornschein ◽  
Brandon T. Ruotolo

Multiprotein complexes have been shown to play critical roles across a wide range of cellular functions, but most probes of protein quaternary structure are limited in their ability to analyze complex mixtures and polydisperse structures using small amounts of total protein.


Sign in / Sign up

Export Citation Format

Share Document