BK virus (BKV) is a common human polyomavirus infecting >80% of the population worldwide. Infection with BKV is asymptomatic, but reactivation in renal transplant recipients can lead to polyomavirus-associated nephropathy. In this report, we show that enzymatic removal of alpha(2,3)-linked sialic acid from cells inhibited BKV infection. Reconstitution of asialo cells with alpha(2,3)-specific sialyltransferase restored susceptibility to infection. Inhibition of N-linked glycosylation with tunicamycin reduced infection, but inhibition of O-linked glycosylation did not. An O-linked-specific alpha(2,3)-sialyltransferase was unable to restore infection in asialo cells. Taken together, these data indicate that an N-linked glycoprotein containing alpha(2,3)-linked sialic acid is a critical component of the cellular receptor for BKV.
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http://dx.doi.org/10.1128/JVI.79.22.14442-14445.2005 | DOI Listing |
J Agric Food Chem
March 2019
Microbial Physiology, Groningen Biomolecular Sciences and Biotechnology Institute (GBB) , University of Groningen, Nijenborgh 7 , 9747 AG Groningen , The Netherlands.
Sialylated oligosaccharides contribute 12.6-21.9% of total free oligosaccharides in human milk ( hMOS).
View Article and Find Full Text PDFGlycoconj J
December 2011
Department of Medical Microbiology, University Medical Center Utrecht, Utrecht, The Netherlands.
The structures of the branched capsular polysaccharides of group B streptococcus type III (GBSIIIPS) and Streptococcus pneumoniae type 14 (Pn14PS) are identical apart from the (α2→3)-linked sialic acid in the side chains of GBSIIIPS. The present study tries to determine the minimal epitope in GBSIIIPS, using both a panel of anti-Pn14PS mouse sera and sera of humans vaccinated with either Pn14PS or GBSIIIPS. Type-specific Pn14PS antibodies that recognize the branched structure of Pn14PS have a low affinity for the native GBSIIIPS.
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