Proteomics

Dataset Information

0

Glycopeptides from recombinant EBV gH, gL and gp42 with EThcD


ABSTRACT: Soluble ectodomains of Epstein Barr Virus glycoproteins gH/gL and gp42 were expressed in HEK293F cells for structural characterization by cryo electron microscopy. The purified material was additionally analyzed by LC-MS/MS after digestion with trypsin or chymotrypsin to identify N-linked glycosylation from EThcD glycopeptide fragmentation spectra.

INSTRUMENT(S): Orbitrap Fusion ETD

ORGANISM(S): Human Herpesvirus 4

SUBMITTER: Joost Snijder  

LAB HEAD: David Veesler

PROVIDER: PXD006403 | Pride | 2018-04-10

REPOSITORIES: Pride

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Publications

An Antibody Targeting the Fusion Machinery Neutralizes Dual-Tropic Infection and Defines a Site of Vulnerability on Epstein-Barr Virus.

Snijder Joost J   Ortego Michael S MS   Weidle Connor C   Stuart Andrew B AB   Gray Matthew D MD   McElrath M Juliana MJ   Pancera Marie M   Veesler David D   McGuire Andrew T AT  

Immunity 20180401 4


Epstein-Barr virus (EBV) is a causative agent of infectious mononucleosis and is associated with 200,000 new cases of cancer and 140,000 deaths annually. Subunit vaccines against this pathogen have focused on the gp350 glycoprotein and remain unsuccessful. We isolated human antibodies recognizing the EBV fusion machinery (gH/gL and gB) from rare memory B cells. One anti-gH/gL antibody, AMMO1, potently neutralized infection of B cells and epithelial cells, the two major cell types targeted by EBV  ...[more]

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