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Bottom-up mapping of RSV nonstructural protein 1 (NS1) for HDX-MS data analysis

ABSTRACT: LC-MS/MS analysis of pepsin-digested RSV-NS1 protein to identify peptides for HDX-MS data processing

INSTRUMENT(S): LTQ FT

ORGANISM(S): Respiratory Syncytial Virus

SUBMITTER: Nicole Wagner

LAB HEAD: Michael L. Gross

PROVIDER: PXD054004 | Pride | 2025-05-07

REPOSITORIES: Pride

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			Action	DRS
	20171113_Map_NS1_1to139_4deg_50uM_001.raw	Raw
	20171113_Map_NS1_1to139_4deg_50uM_002.raw	Raw
	20171113_Map_NS1_1to139_4deg_50uM_003.raw	Raw
	NS1_peptide_list_2024_formatted.csv	Csv
	checksum.txt	Txt

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Publications

Molecular basis for human respiratory syncytial virus transcriptional regulator NS1 interactions with MED25.

Kalita Parismita P Khatavkar Oam O Uwase Grace G Korshunova Yulia Y Hu Yuying Y Wagner Nicole D ND Xu Jian J Pan Jiehong J Nix Jay C JC Gross Michael L ML Brody Steven L SL Borek Dominika D Amarasinghe Gaya K GK Payton Jacqueline E JE Leung Daisy W DW

Nature communications 20250325 1

The Mediator complex facilitates interactions between transcription factors and RNA polymerase II, a process that is required for host gene transcription, including in response to viral infections. Among the many subunits in the Mediator complex, the MED25 subunit has been shown to be a target for viral activators during infection. Here we provide the molecular basis for the interaction between human respiratory syncytial virus (hRSV) nonstructural 1 protein (NS1) and the activator interaction d ...[more]

PMID: 40128225

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RSV nonstructural protein 1 (NS1) HDX LC-MS data

Project description:Raw liquid chromatography-mass spectrometry (LC-MS) datafiles acquired for hydrogen-deuterium exchange (HDX) of RSV nonstructural protein 1 (NS1)

2025-05-07 | PXD054005 | Pride

Site-Selective Protein Conjugation by a Multicomponent Ugi Reaction

Project description:The chemical bioconjugation of proteins has seen tremendous applications in the past decades, with the booming of antibody-drug conjugates and their use in oncology. While genetic engineering has permitted to produce bespoke proteins featuring key (un-)natural amino acid residues poised for site-selective modifications, the conjugation of native proteins is riddled with selectivity issues. Chemoselective strategies are plentiful and enable the precise modification of virtually any residue with a reactive side-chain; site-selective methods are less common and usually most effective on small and medium-sized proteins. In this context, we studied the application of the Ugi multicomponent reaction for the site-selective conjugation of amine and carboxylate groups on proteins, and antibodies in particular. Through an in-depth mechanistic methodology work supported by peptide mapping studies, we managed to develop a set of conditions allowing the highly selective modification of antibodies bearing N-terminal glutamate and aspartate residues. We demonstrated that this strategy did not alter their affinity toward their target antigen and produced an antibody-drug conjugate with subnanomolar potency. Excitingly, we showed that the high site selectivity of our strategy was maintained on other protein formats, especially on anticalins, for which directed mutagenesis helped to highlight the key importance of a single lysine residue.

2024-09-09 | PXD045387 | Pride

mRNA display with library of even-distribution reveals cellular interactors of influenza virus NS1

Project description:The interactome of Influenza (A/WSN/33) NS1 protein (WT and D92Y mutant) was identifiedy by AP-MS.

2021-09-07 | PXD018377 | Pride

JEV NS1'-interacting cellular proteins

Project description:We identify NS1' interacting proteins via immunopreciptation of JEV-infected cell lysates with an NS1'-specific antibody.

2022-02-17 | PXD027412 | Pride

The respiratory syncytial virus (RSV) nonstructural proteins mediate RSV suppression of glucocorticoid receptor transactivation.

Project description:Respiratory syncytial virus (RSV)-induced bronchiolitis in infants is not responsive to glucocorticoids. We have shown that RSV infection impairs glucocorticoid receptor (GR) function. In this study, we have investigated the mechanism by which RSV impairs GR function. We have shown that RSV repression of GR-induced transactivation is not mediated through a soluble autocrine factor. Knock-down of mitochondrial antiviral signaling protein (MAVS), but not retinoic acid-inducible gene 1 (RIG-I) or myeloid differentiation primary response gene 88 (MyD88), impairs GR-mediated gene activation even in mock-infected cells. Over-expression of the RSV nonstructural protein NS1, but not NS2, impairs glucocorticoid-induced transactivation and viruses deleted in NS1 and/or NS2 are unable to repress glucocorticoid-induction of the known GR regulated gene glucocorticoid-inducible leucine zipper (GILZ). These data suggest that the RSV nonstructural proteins mediate RSV repression of GR-induced transactivation and that inhibition of the nonstructural proteins may be a viable target for therapy against RSV-related disease.

| S-EPMC3904736 | biostudies-literature

Transcriptional Profiling of B19 Virus Nonstructure Protein (NS1) transduced CD36+ Erythoid Progenitor Cells (EPCs)

Project description:B19V NS1 is known to be cytotoxic and involved in the pathogenesis of B19V infection. Our previous data demonstrated that NS1 impaired the cell-cycle progression of the CD36+ EPCs by inducing a stable G2 arrest. Microarray analysis was used to identify genes whose expressions were associated with the NS1-induced G2 arrest. A total of 1045 genes displayed a more than 1.5-fold differential expression in the NS1-transduced cells. Out of 1045 differentially expressed genes, 177 were involved in cell-cycle regulation and 51 were involved in the regulation of cell differentiation. Keywords: RNA CD36+ EPCs were generated from CD34+ stem cells, and transduced with B19V NS1 or control-lentivirus for 12, 24,and 48 hours. Each sample has triplicates. There are 18 samples analyzed.

2010-11-03 | E-GEOD-18906 | biostudies-arrayexpress

Dengue NS1 Antibodies Are Associated With Clearance of Viral Nonstructural Protein-1.

Project description:BackgroundDengue vascular permeability syndrome is the primary cause of death in severe dengue infections. The protective versus potentially pathogenic role of dengue nonstructural protein-1 (NS1) antibodies are not well understood. The main goal of this analysis was to characterize the relationship between free NS1 concentration and NS1 antibody titers in primary and secondary dengue infection to better understand the presence and duration of NS1 antibody complexes in clinical dengue infections.MethodsHospitalized participants with acute dengue infection were recruited from Northern Colombia between 2018 and 2020. Symptom assessment, including dengue signs and symptoms, chart review, and blood collection, was performed. Primary versus secondary dengue was assessed serologically. NS1 titers and anti-NS1 antibodies were measured daily.ResultsPatients with secondary infection had higher antibody titers than those in primary infection, and there was a negative correlation between anti-NS1 antibody titer and NS1 protein. We demonstrate that in a subset of secondary infection, there were indeed NS1 antigen-antibody complexes on the admission day during the febrile phase that were not detectable by the recovery phase. Furthermore, dengue infection status was associated with higher circulating sialidases.DiscussionThe negative correlation between antibody and protein suggests that antibodies may play a role in clearing this viral protein.

| S-EPMC11646586 | biostudies-literature

AP-MS analysis of FLAG-tagged Murine norovirus (NS1/2 and NS4)

Project description:Norovirus replication is accomplished by the use of a number of viral proteins derived from a long polyprotein. These components are named from NS1/2 to NS7. Having previously determined that the incorporation of FLAG epitope tags into certain positions in the norovirus genome was tolerated (Thorne et. al. 2012 J. Virol)

2019-09-09 | PXD011779 | Pride

Stability of Dengue 2 Nonstructural Glycoprotein 1 (NS1) Is Affected by the Nature of Basic Residue at Position NS1-324.

Project description:Dengue is the most prevalent mosquito-borne viral disease. It is caused by the infection of any of the four dengue virus (DENV) serotypes DENV-1 to DENV-4. The DENV non-structural glycoprotein 1 (NS1) plays an important role in virus replication and the immunopathogenesis of virus infection. The NS1 protein has been identified as both a cell-associated homodimer and a soluble secreted lipoprotein nanoparticle. The nature of the residues at positions NS1-272 and NS1-324 in the β-ladder domain may have an effect on the biological behaviors of DENV-2 NS1 protein in human hepatoma Huh7 cells. The stability of the NS1 protein from the Reunion 2018 DENV-2 strain was affected by the presence of lysine residues at positions 272 and 324. In the present study, we evaluated the impact of mutations into lysine at positions 272 and 324 on recombinant NS1 protein from the DES-14 DENV-2 strain bearing arginine residue on these two positions. The DES-14 NS1 protein mutant bearing a lysine at position 324 was deficient in protein stability and secretion compared to wild-type protein. The defect in the DES-14 NS1 protein mutant was associated to oxidative stress and pro-inflammatory cytokine activation in Huh7 cells. The ubiquitin-proteasome proteolytic pathway might play a key role in the stability of DENV-2 protein bearing a lysine residue at position 324.

| S-EPMC9955058 | biostudies-literature

Binding of flavivirus nonstructural protein NS1 to C4b binding protein modulates complement activation.

Project description:The complement system plays a pivotal protective role in the innate immune response to many pathogens including flaviviruses. Flavivirus nonstructural protein 1 (NS1) is a secreted nonstructural glycoprotein that accumulates in plasma to high levels and is displayed on the surface of infected cells but absent from viral particles. Previous work has defined an immune evasion role of flavivirus NS1 in limiting complement activation by forming a complex with C1s and C4 to promote cleavage of C4 to C4b. In this study, we demonstrate a second mechanism, also involving C4 and its active fragment C4b, by which NS1 antagonizes complement activation. Dengue, West Nile, or yellow fever virus NS1 directly associated with C4b binding protein (C4BP), a complement regulatory plasma protein that attenuates the classical and lectin pathways. Soluble NS1 recruited C4BP to inactivate C4b in solution and on the plasma membrane. Mapping studies revealed that the interaction sites of NS1 on C4BP partially overlap with the C4b binding sites. Together, these studies further define the immune evasion potential of NS1 in reducing the functional capacity of C4 in complement activation and control of flavivirus infection.

| S-EPMC3119735 | biostudies-literature