An N-linked glycoprotein with alpha(2,3)-linked sialic acid is a receptor for BK virus.

J Virol

Graduate Program in Pathobiology, Department of Molecular Biology, Cell Biology, and Biochemistry, Brown University, Providence, Rhode Island 02903, USA.

Published: November 2005

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.

Download full-text PDF

Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1280228PMC
http://dx.doi.org/10.1128/JVI.79.22.14442-14445.2005DOI Listing

Publication Analysis

Top Keywords

alpha23-linked sialic
12
sialic acid
12
n-linked glycoprotein
8
glycoprotein alpha23-linked
8
asialo cells
8
infection inhibition
8
infection
5
acid receptor
4
receptor virus
4
virus virus
4

Similar Publications

Synthesis and Characterization of Sialylated Lactose- and Lactulose-Derived Oligosaccharides by Trypanosoma cruzi Trans-sialidase.

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 PDF

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.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!