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Diversity in prokaryotic glycosylation: an archaeal-derived N-linked glycan contains legionaminic acid.

Publication ,  Journal Article
Kandiba, L; Aitio, O; Helin, J; Guan, Z; Permi, P; Bamford, DH; Eichler, J; Roine, E
Published in: Mol Microbiol
May 2012

VP4, the major structural protein of the haloarchaeal pleomorphic virus, HRPV-1, is glycosylated. To define the glycan structure attached to this protein, oligosaccharides released by β-elimination were analysed by mass spectrometry and nuclear magnetic resonance spectroscopy. Such analyses showed that the major VP4-derived glycan is a pentasaccharide comprising glucose, glucuronic acid, mannose, sulphated glucuronic acid and a terminal 5-N-formyl-legionaminic acid residue. This is the first observation of legionaminic acid, a sialic acid-like sugar, in an archaeal-derived glycan structure. The importance of this residue for viral infection was demonstrated upon incubation with N-acetylneuraminic acid, a similar monosaccharide. Such treatment reduced progeny virus production by half 4 h post infection. LC-ESI/MS analysis confirmed the presence of pentasaccharide precursors on two different VP4-derived peptides bearing the N-glycosylation signal, NTT. The same sites modified by the native host, Halorubrum sp. strain PV6, were also recognized by the Haloferax volcanii N-glycosylation apparatus, as determined by LC-ESI/MS of heterologously expressed VP4. Here, however, the N-linked pentasaccharide was the same as shown to decorate the S-layer glycoprotein in this species. Hence, N-glycosylation of the haloarchaeal viral protein, VP4, is host-specific. These results thus present additional examples of archaeal N-glycosylation diversity and show the ability of Archaea to modify heterologously expressed proteins.

Duke Scholars

Published In

Mol Microbiol

DOI

EISSN

1365-2958

Publication Date

May 2012

Volume

84

Issue

3

Start / End Page

578 / 593

Location

England

Related Subject Headings

  • Viral Proteins
  • Sialic Acids
  • Polysaccharides
  • Peptide Mapping
  • Molecular Sequence Data
  • Microbiology
  • Mass Spectrometry
  • Haloferax volcanii
  • Glycosylation
  • Archaeal Viruses
 

Citation

APA
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MLA
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Kandiba, L., Aitio, O., Helin, J., Guan, Z., Permi, P., Bamford, D. H., … Roine, E. (2012). Diversity in prokaryotic glycosylation: an archaeal-derived N-linked glycan contains legionaminic acid. Mol Microbiol, 84(3), 578–593. https://doi.org/10.1111/j.1365-2958.2012.08045.x
Kandiba, Lina, Olli Aitio, Jari Helin, Ziqiang Guan, Perttu Permi, Dennis H. Bamford, Jerry Eichler, and Elina Roine. “Diversity in prokaryotic glycosylation: an archaeal-derived N-linked glycan contains legionaminic acid.Mol Microbiol 84, no. 3 (May 2012): 578–93. https://doi.org/10.1111/j.1365-2958.2012.08045.x.
Kandiba L, Aitio O, Helin J, Guan Z, Permi P, Bamford DH, et al. Diversity in prokaryotic glycosylation: an archaeal-derived N-linked glycan contains legionaminic acid. Mol Microbiol. 2012 May;84(3):578–93.
Kandiba, Lina, et al. “Diversity in prokaryotic glycosylation: an archaeal-derived N-linked glycan contains legionaminic acid.Mol Microbiol, vol. 84, no. 3, May 2012, pp. 578–93. Pubmed, doi:10.1111/j.1365-2958.2012.08045.x.
Kandiba L, Aitio O, Helin J, Guan Z, Permi P, Bamford DH, Eichler J, Roine E. Diversity in prokaryotic glycosylation: an archaeal-derived N-linked glycan contains legionaminic acid. Mol Microbiol. 2012 May;84(3):578–593.
Journal cover image

Published In

Mol Microbiol

DOI

EISSN

1365-2958

Publication Date

May 2012

Volume

84

Issue

3

Start / End Page

578 / 593

Location

England

Related Subject Headings

  • Viral Proteins
  • Sialic Acids
  • Polysaccharides
  • Peptide Mapping
  • Molecular Sequence Data
  • Microbiology
  • Mass Spectrometry
  • Haloferax volcanii
  • Glycosylation
  • Archaeal Viruses