Document Detail


A Siglec-like sialic-acid-binding motif revealed in an adenovirus capsid protein.
MedLine Citation:
PMID:  22522600     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Sialic-acid-binding immunoglobulin-like lectins (Siglecs) are a family of transmembrane receptors that are well documented to play roles in regulation of innate and adaptive immune responses. To see whether the features that define the molecular recognition of sialic acid were found in other sialic-acid-binding proteins, we analyzed 127 structures with bound sialic acids found in the Protein Data Bank database. Of these, the canine adenovirus 2-fiber knob protein showed close local structural relationship to Siglecs despite low sequence similarity. The fiber knob harbors a noncanonical sialic-acid recognition site, which was then explored for detailed specificity using a custom glycan microarray comprising 58 diverse sialosides. It was found that the adenoviral protein preferentially recognizes the epitope Neu5Acα2-3[6S]Galβ1-4GlcNAc, a structure previously identified as the preferred ligand for Siglec-8 in humans and Siglec-F in mice. Comparison of the Siglec and fiber knob sialic-acid-binding sites reveal conserved structural elements that are not clearly identifiable from the primary amino acid sequence, suggesting a Siglec-like sialic-acid-binding motif that comprises the consensus features of these proteins in complex with sialic acid.
Authors:
Christoph Rademacher; Thierry Bru; Ryan McBride; Elizabeth Robison; Corwin M Nycholat; Eric J Kremer; James C Paulson
Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, P.H.S.     Date:  2012-04-21
Journal Detail:
Title:  Glycobiology     Volume:  22     ISSN:  1460-2423     ISO Abbreviation:  Glycobiology     Publication Date:  2012 Aug 
Date Detail:
Created Date:  2012-06-26     Completed Date:  2012-12-04     Revised Date:  2014-09-15    
Medline Journal Info:
Nlm Unique ID:  9104124     Medline TA:  Glycobiology     Country:  England    
Other Details:
Languages:  eng     Pagination:  1086-91     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Adenoviruses, Canine / genetics*
Animals
Biological Markers / metabolism
Capsid Proteins / genetics,  metabolism*
Dogs
Humans
Models, Molecular
Mutagenesis, Site-Directed
Mutation / genetics
Oligonucleotide Array Sequence Analysis
Polysaccharides / metabolism*
RNA, Messenger / genetics
Real-Time Polymerase Chain Reaction
Reverse Transcriptase Polymerase Chain Reaction
Sialic Acid Binding Immunoglobulin-like Lectins / genetics,  metabolism*
Sialic Acids / metabolism*
Grant Support
ID/Acronym/Agency:
200-2009-32562//PHS HHS; P01 AI058113/AI/NIAID NIH HHS; P01 AI058113-07/AI/NIAID NIH HHS; P01AI058113/AI/NIAID NIH HHS; U54 GM062116/GM/NIGMS NIH HHS; U54 GM062116-10/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Biological Markers; 0/Capsid Proteins; 0/Polysaccharides; 0/RNA, Messenger; 0/Sialic Acid Binding Immunoglobulin-like Lectins; 0/Sialic Acids; 0/hexon capsid protein, Adenovirus
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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