Proteomics

Dataset Information

0

O-Glycosylation of Mycobacteriophage Proteins


ABSTRACT: Provided herein is the first evidence that mycobacteriophage, indeed phage of any kind, have surface proteins (capsid and/or tail tube proteins) that are O-glycosylated. The glycosyltranferases that glycosylate these proteins are encoded in the phage genomes. In addition, for the three mycobacteriophages invested in this study, the glycans appear to be attached exclusively at a C-terminal serine residue. Each phage expresses a unique and novel O-glycan. The LC-MS files deposited here are the preliminary evidence that these mycobacteriophage proteins are glycosylated. A follow-up investigation will examine the composition and structure of the O-glycans in more detail.

INSTRUMENT(S): Orbitrap Eclipse, Q-Tof Premier, Synapt MS

ORGANISM(S): Mycobacterium Phage Myrna Mycobacterium Phage Corndog Mycobacterium Phage Che8

TISSUE(S): Cell Culture

SUBMITTER: John Kelly  

LAB HEAD: John Kelly

PROVIDER: PXD041690 | Pride | 2024-08-10

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
E220406P00DPTR20717S04.raw Raw
E220406P00DPTR20717S05.raw Raw
E220406P00DPTR20717S08.raw Raw
F035904.dat Other
F035904.mgf Mgf
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Publications


Glycosylation of eukaryotic virus particles is common and influences their uptake, trafficking, and immune recognition. In contrast, glycosylation of bacteriophage particles has not been reported; phage virions typically do not enter the cytoplasm upon infection, and they do not generally inhabit eukaryotic systems. We show here that several genomically distinct phages of Mycobacteria are modified with glycans attached to the C terminus of capsid and tail tube protein subunits. These O-linked gl  ...[more]

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