Document Detail


Diversity in prokaryotic glycosylation: an archaeal-derived N-linked glycan contains legionaminic acid.
MedLine Citation:
PMID:  22435790     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
Lina Kandiba; Olli Aitio; Jari Helin; Ziqiang Guan; Perttu Permi; Dennis H Bamford; Jerry Eichler; Elina Roine
Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.     Date:  2012-04-11
Journal Detail:
Title:  Molecular microbiology     Volume:  84     ISSN:  1365-2958     ISO Abbreviation:  Mol. Microbiol.     Publication Date:  2012 May 
Date Detail:
Created Date:  2012-04-20     Completed Date:  2012-10-15     Revised Date:  2013-06-26    
Medline Journal Info:
Nlm Unique ID:  8712028     Medline TA:  Mol Microbiol     Country:  England    
Other Details:
Languages:  eng     Pagination:  578-93     Citation Subset:  IM    
Copyright Information:
© 2012 Blackwell Publishing Ltd.
Affiliation:
Department of Life Sciences, Ben Gurion University of the Negev, Beersheva 84105, Israel.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Archaeal Viruses / chemistry,  genetics,  metabolism*
Glycosylation
Haloferax volcanii / metabolism*,  virology
Mass Spectrometry
Molecular Sequence Data
Peptide Mapping
Polysaccharides / chemistry*,  metabolism*
Sialic Acids / analysis,  metabolism*
Viral Proteins / chemistry,  genetics,  metabolism*
Grant Support
ID/Acronym/Agency:
GM-069338/GM/NIGMS NIH HHS; U54 GM069338/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/5,7-diacetamido-8-O-acetyl-3,5,7,9-tetradeoxy-glycero-talo-nonulosonic acid; 0/Polysaccharides; 0/Sialic Acids; 0/Viral Proteins
Comments/Corrections

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