Proteomics

Dataset Information

0

Recombinant Ag85B Glycoproteomics


ABSTRACT: A bacterial antigen (Ag85B) was recombinantly expressed in Expi293 cells in which non-native N-glycosylation occured. We used glycoproteomics to characterize site-specific glycosylation across the surface of Ag85B as informed by glycomics data.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Suspension Culture, Early Embryonic Cell

SUBMITTER: Trevor Adams  

LAB HEAD: Fikri Avci

PROVIDER: PXD077483 | Pride | 2026-05-25

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
Ag85b_alphalytic.raw Raw
Ag85b_trypgluc.raw Raw
checksum.txt Txt
ppmfixerOutput_alphalytic.txt Txt
ppmfixerOutput_trypgluc.txt Txt
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Publications

Molecular mechanisms of immune evasion by host protein glycosylation of a bacterial immunogen used in nucleic acid vaccines.

Cinar Mukaddes Sena MS   Adams Trevor M TM   Nawaz Fathima Zahra FZ   Demir Elif S ES   Erol Demirturk Mariye M   Keelaghan Aidan P AP   Nazaar Shaima M SM   Roberts Blaine R BR   Ozdilek Ahmet A   Avci Fikri Y FY  

The Journal of biological chemistry 20260402 5


Nucleic acid vaccines (DNA and mRNA) induce immunity by driving in situ antigen expression in host cells. For nonviral pathogens, however, host expression can impose post-translational modifications absent from the native microbial antigen. Tuberculosis remains a leading cause of infectious mortality, and nucleic acid vaccines targeting the Mycobacterium tuberculosis antigen 85 (Ag85) complex did not confer protective efficacy in clinical trials. We hypothesized that host-derived N-glycosylation  ...[more]

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