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Chinese Hamster Ovary cell proteins co-purified with recombinant HIV-1 envelopes, part 2

ABSTRACT: Chinese Hamster Ovary (CHO) cells are frequently used to produce recombinant HIV envelope protein gp120. In this study, we characterized the CHO proteins that become co-purified with gp120 when lectin affinity chromatography is used. Many of co-purified CHO proteins identified were extracellular matrix components. We verified a method for separating gp120 from these CHO proteins with anion exchange chromatography, and assessed the biochemical activity of gp120 preparations with and without co-purified CHO proteins.

INSTRUMENT(S): Orbitrap Fusion

ORGANISM(S): Cricetulus Griseus (chinese Hamster) (cricetulus Barabensis Griseus)

SUBMITTER: David Plotnik

LAB HEAD: Shiu-Lok Hu

PROVIDER: PXD006061 | Pride | 2017-09-04

REPOSITORIES: Pride

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			Action	DRS
	20161205_DEAE-Peak1-MW959.mzXML	Mzxml
	20161205_DEAE-Peak1-MW959.pep.xml	Pepxml
	20161205_DEAE-Peak1-MW959.raw	Raw
	CRIGR.fasta.20161205	Fasta
	comet.params	Other

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Publications

Extracellular Matrix Proteins Mediate HIV-1 gp120 Interactions with α4β7.

Plotnik David D Guo Wenjin W Cleveland Brad B von Haller Priska P Eng Jimmy K JK Guttman Miklos M Lee Kelly K KK Arthos James J Hu Shiu-Lok SL

Journal of virology 20171013 21

Gut-homing α4β7high CD4+ T lymphocytes have been shown to be preferentially targeted by human immunodeficiency virus type 1 (HIV-1) and are implicated in HIV-1 pathogenesis. Previous studies demonstrated that HIV-1 envelope protein gp120 binds and signals through α4β7 and that this likely contributes to the infection of α4β7high T cells and promotes cell-to-cell virus transmission. Structures withi ...[more]

PMID: 28814519

Similar Datasets

Chinese Hamster Ovary cell proteins co-purified with recombinant HIV-1 envelopes, part 1

Project description:Chinese Hamster Ovary (CHO) cells are frequently used to produce recombinant HIV envelope protein gp120. In this study, we characterized the CHO proteins that become co-purified with gp120 when lectin affinity chromatography is used. Many of co-purified CHO proteins identified were extracellular matrix components. We verified a method for separating gp120 from these CHO proteins with anion exchange chromatography, and assessed the biochemical activity of gp120 preparations with and without co-purified CHO proteins.

2017-09-04 | PXD006060 | Pride

Chinese Hamster Ovary cell proteins co-purified with recombinant HIV-1 envelopes, part 4

2017-09-04 | PXD006063 | Pride

Chinese Hamster Ovary cell proteins co-purified with recombinant HIV-1 envelopes, part 3

2017-09-04 | PXD006062 | Pride

Chinese Hamster Ovary cell proteins co-purified with recombinant HIV-1 envelopes, part 2

2018-01-25 | MSV000081975 | MassIVE

Chinese Hamster Ovary cell proteins co-purified with recombinant HIV-1 envelopes, part 1

2018-01-25 | MSV000081974 | MassIVE

Chinese Hamster Ovary cell proteins co-purified with recombinant HIV-1 envelopes, part 3

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Chinese Hamster Ovary cell proteins co-purified with recombinant HIV-1 envelopes, part 4

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Mitochondrial interactome quantitation reveals structural changes in metabolic machinery in failing murine heart

Project description:Advancements of cross-linking mass spectrometry (XL-MS) for structural analysis of proteins bridges the gap between purified systems and native tissue environments. Here, we utilize isobaric quantitative protein interaction reporter technology (iqPIR) to further extend XL-MS to the first system-wide comparative study of mitochondrial proteins from healthy and diseased murine hearts. The failing heart interactome includes 544 statistically significant cross-linked peptide pairs altered in disease condition. Structural insight into ketone oxidation metabolons, OXPHOS machinery, and nucleotide transporter hybrid-conformations, support mitochondrial remodeling in failing heart while bringing forth new hypotheses for pathological mechanisms. Application of quantitative cross-linking technology in live tissue provides molecular-level insight to complex biological systems difficult to model in cell culture, thus providing a valuable resource for study of human diseases.

2022-08-02 | PXD027757 | Pride

AP-MS analysis of human FUBIeS30/FAU WT and non-cleavable G73,4A and G74V mutants

Project description:To discover candidate FUBIeS30 proteases, we performed affinity purification from human cell lysates expressing tandem Strep II-hemagglutinin (StHA)-tagged WT or mutant (G73,74A or G74V) FUBIeS30-StHA constructs. Subsequent analysis of the co-purified proteins by mass spectrometry (LC-MS/MS) identified differentially interacting factors. We found that two deubiquitinases, USP10 and USP36, were enriched on the non-cleavable mutants compared to WT and subsequently confirmed that USP36 is involved in FUBIeS30 processing in vivo.

2021-08-05 | PXD021864 | Pride

Variability in the Glycosylation Patterns of gp120 Proteins from Different Human Immunodeficiency Virus Type 1 Isolates Expressed in Different Host Cells

Project description:The mature HIV-1 envelope (Env) glycoprotein is composed of gp120, the exterior subunit, and gp41, the transmembrane subunit assembled as trimer by noncovalent interaction. There is a great body of literature to prove that gp120 binds to CD4 first, then to the co-receptor. We have recently demonstrated that gp120 cannot bind to the co-receptor without first interacting with CD4. Previous studies provided different glycomic maps for the HIV-1 gp120. Here, we build on previous work to report that the use of LC-MS/MS, in conjunction with hydrophilic interaction liquid chromatography (HILIC) enrichment to glycosylation sites, is associated with the assorted neutralizing or binding events of glycosylation targeted antibodies from different clades or strains. In this study, the microheterogeneity of the glycosylation from 4 different clades of gp120s is deeply investigated. Aberrant glycosylation patterns were detected on gp120 originated from different clades, viral sequences and host cells. The results of this study may help provide better understanding of the mechanism of how the glycans participate in antibody neutralizing process that target glycosylation sites.

2021-11-01 | PXD027353 | Pride